NC1131: Molecular Mechanisms Regulating Skeletal Muscle Growth and Differentiation (NC131)

(Multistate Research Project)

Status: Inactive/Terminating

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SAES-422 Reports

Annual/Termination Reports:

[09/02/2005] [12/01/2006] [12/03/2007] [11/08/2008] [04/15/2010] [01/03/2010]

Date of Annual Report: 09/02/2005

Report Information

Annual Meeting Dates: 10/21/2005 - 10/22/2005
Period the Report Covers: 10/01/2005 - 10/01/2005

Participants

Refer to termination report of NC131.

Brief Summary of Minutes

Accomplishments

Refer to termination report of NC131.

Publications

Refer to termination report of NC131.

Impact Statements

Refer to termination report of NC131.

Date of Annual Report: 12/01/2006

Report Information

Annual Meeting Dates: 11/02/2006 - 11/03/2006
Period the Report Covers: 10/01/2005 - 09/01/2006

Participants

Goll, Darrel (darrel.goll@arizona.edu)-Arizona;
Kim, Yong Soo (ykim@hawaii.edu)-Hawaii;
Hill, Rodney (rodhill@uidaho.edu)-Idaho;
Killefer, John (jkillef@uiuc.edu)-Illinois;
Grant, Alan (agrant@purdue.edu)-Indiana;
Huiatt, Ted (twhuiatt@iastate.edu)- Iowa;
Ernst, Catherine (ernstc@msu.edu)-Michigan;
Dayton, Bill (wdayton@umn.edu)-Minnesota;
White, Michael (mwhite@umn.edu)-Minnesota;
Velleman, Sandra (velleman.1@osu.edu)-Ohio

Brief Summary of Minutes

Members Not Attending:
Brad Johnson - Kansas; Charles Carpenter - Utah; David Gerrard, Darl Swartz - Indiana; Matthew Doumit - Michigan; Neil Forsberg - Oregon; Richard Robson - Iowa; Marcia Hathaway - Minnesota; Marion Greaser - Wisconsin; Douglas McFarland - South Dakota; Michael Dodson - Washington; Steven Jones, Mike Zeece - Nebraska; Paul Mozdziak - North Carolina; Ron Allen - Arizona; Sally Johnson - Florida

Guests:

Halina Zaleski - Hawaii; Sungwkwon Park, Amanda Weaver, Caiyun Zeng - Indiana

The annual meeting of the NC-1131 technical committee was held in Honolulu, Hawaii on November 2-3, 2006. The meeting was called to order by committee chair, Yong soo Kim.

The group was welcomed to the University of Hawaii by Dr. Halina Zaleski, Chair of the Department of Human Nutrition, Food and Animal Sciences.

Each of the stations prepared a brief written report and presented this information to the group in attendance. Dr. Min Du of the University of Wyoming presented their work and requested admission to the NC-1131 project. Dr. Du was approved by consensus of the Technical Committee during the Business Meeting.

In the business meeting, Alan Grant (Administrative Advisor) reported that the NC-131 Termination Report required significant shortening prior to its final submission and that we are now into our second year as NC-1131. Dr. Debora Hamernik (USDA-CSREES, National Program Leader) provided programmatic updates on personnel and the USDA Strategic Plan. Dr. Hamernik also provided insight into successful grantsmanship and funding opportunities.

It was decided that the next year meeting would be held in Champaign, Illinois and that John Killefer would serve as Chair. Dr. Goll agreed to serve as Secretary of NC-1131 for 2007 and to host the NC-1131 meeting in Arizona in 2008. The Business Meeting was adjourned and presentations of remaining Station Reports resumed.

Accomplishments

Insulin-like growth factor binding protein (IGFBP)-3 binds IGFs with high affinity and affects their biological activity. IGFBP-3 that is not bound to IGF also affects cells via mechanisms involving binding to specific cell surface receptors and/or transport into the cell. IGFBP-3 is produced by porcine embryonic myogenic cell (PEMC) cultures. Additionally, IGFBP-3 facilitates the proliferation-suppressing actions of TGF-²1 and myostatin in PEMC cultures via mechanisms that do not involve IGF binding. Results suggest that translocation of IGFBP-3 into the nucleus of PEMC could play a role in mediating the proliferation-suppressing action of TGF-²1. Additionally, it was reported that exogenous and endogenous IGFBP-3 affect proliferation and differentiation of L6 myogenic cells in a similar way, and that endogenously produced IGFBP-3 must first be secreted before it is internalized. Inhibitors of arginine-specific mono-ADP-ribosylation reversibly block proliferation and differentiation of myoblasts in cell culture. Additionally, ADP-ribosylation of the muscle intermediate filament (IF) protein desmin by a purified muscle arginine-specific mono-ADP-ribosyltransferase (ART) blocks the ability of desmin to assemble into 10-nm Ifs. Research findings provided additional evidence to support a role for ADP-ribosylation in the regulation of myogenesis. Research demonstrated that synemin could provide critical linkages between myofibrils and costameres, and provided support for the hypothesis that synemin is an important linker between IFs and other cytoskeletal components. Studies during the past year have added to the information on activation of muscle satellite cells, and how the hepatocyte growth factor functions in concert with nitric oxide and metalloproteinases in response to growth stimuli such as stretching. Ability to assay the calpains and calpastatin in small, biopsy samples will make it possible to determine the properties of the calpain system in living animals. The role of proteoglycans in the regulation of muscle growth is not well understood at this time. It is clear that muscle cells especially the satellite cells are responsive to growth factors like fibroblast growth factor 2 (FGF2) and transforming growth factor ² (TGF-²). The regulation of muscle cell responsiveness to each of these growth factors is critical in the muscle growth and regeneration processes. Research to address the role of extracellular matrix in muscle growth and development included generation of glypican site directed mutants, development of transfection assays to measure the effect of the different site direct mutants for the heparan sulfate glycosaminoglycan attachment sites on satellite cell proliferation and FGF2 responsiveness, and initiating initial studies on the TGF-²-decorin-²1 integrin signal transduction pathways. Research was conducted to examine the differences in myogenic cell populations during various developmental timepoints during prenatal and postnatal development. Research was also conducted to examine the effects of myostatin on embryonic myogenesis. Results indicated that the anti-myostatin antibodies produced by maternal immunization against myostatin in mice did not suppress the biological activity of myostatin, and probably do not modulate skeletal muscle growth. It was demonstrated that Myostatin Knock Out (MKO, a model of extreme muscle hyperplasia and hypertrophy) mice do respond, and may be more responsive than Wild Type mice to, Beta-adrenergic agonist (BAA) treatment . BAA administration to MKO mice resulted in increased muscle mass and decreased fat deposition. A second insulin gene in zebrafish was discovered and described, and the sequence has been deposited with Genbank. Understanding the developmental roles of insulin in teleosts (zebrafish model) is forming the groundwork for future studies of insulin effects in teleost muscle. It was reported that BAA exerts a distinct muscle- and muscle fiber type-specific hypertrophy that is preferentially restricted to fast-twitch fibers. Moreover, pharmacologically or genetically attenuating extracellular signal-regulated kinase (ERK) signaling in muscle fibers resulted in decreases in fast but not slow fiber type-specific reporter gene expressions in response to BAA exposure. These data suggest fast myofibers are pivotal in the adaptation of muscle to environmental cues and that the mechanism underlying this change is partially mediated by the MAPK signaling cascade.

Publications

Referreed Papers: Arizona: Katsuki, Y., R. Tatsumi, M. Yamada, J. Ishizaki, W. Mizunoya, Y. Ikeuchi, A. Hattori, H. Shimokawa, K. Sungawa,, and R.E. Allen. 2006. Low-pH preparation of skeletal muscle satellite cells can be used to study activation in vitro. Int. J. Biochem. Cell Biol. 38:1678-1685. Tatsumi, R., X. Liu, A. Pulido, M. Morales, T. Sakata, S. Dial, A. Hattori, Y. Ikeuchi, and R.E. Allen. 2006. Satellite cell activation in stretched skeletal muscle and the role of nitric oxide and hepatocyte growth factor. Am. J. Physiol. Cell Physiol. 290:C1487-94. Yamada, M., R. Tatsumi, T. Kikuri, S. Okamoto, S. Nonoshita, W. Mizunoya, Y. Ikeuchi, H. Shimokawa, K. Sunagawa, and R.E. Allen. 2006. Matrix metalloproteinases are involved in mechanical stretch-induced activation of skeletal muscle satellite cells. Muscle Nerve 34:313-319. Saido, M., H. Li, V.F. Thompson, N. Kunisaki, and D.E. Goll. 2007. Purification and characterization of calpain and calpastatin from rainbow trout, Oncorhynchus mykiss. Comp. Biochem. Physiol. (in press). Florida: Li, J. & Johnson, S. E. 2006. ERK2 is required for efficient terminal differentiation of skeletal myoblasts. Biochem. Biophys. Res. Commun. 345(4):1425-1433. Reed, S.A., Ouellette, S.E., Liu, X., Allen, R.E. & Johnson, S.E. 2006. E2F5 and LEK1 translocation to the nucleus is an early event demarcating myoblast quiescence. J. Cell Biochem. Submitted. Hawaii: Y.S. Kim, N.K. Bobilli, K.S. Paek and H.J. Jin. 2006. In-ovo administration of monoclonal anti-myostatin antibody improves post-hatch chicken growth and muscle mass. Poultry Science 85:1062-1071. Idaho: Papasani, M.R., Robison, B.D., Hardy, R. W. and Hill R.A. (2006). Early developmental expression of two insulins in zebrafish. Physiological Genomics 27:79-85. Baker, S.D., Szasz, J.I., Klein, T.A., Kuber, P.S., Hunt, C.W., Glaze Jr., J.B., Falk, D., Richard, R., Miller, J.C., Battaglia, R.A. and Hill, R.A. (2006). Residual Feed Intake of Purebred Angus Steers: Effects on Meat Quality and Palatability. Journal of Animal Science 84:938-945. Strat, A.L., Kokta, T.A., Dodson, M.V., Gertler, A., Wu, Z. and Hill, R.A. (2005). Early Signaling Interactions between the Insulin and Leptin Pathways in Bovine Myogenic Cells. Biochimica et Biophysica Acta 1744:164-175. Fernyhough, M.E., Helterline, D.L.,Vierck, J.L., Hausman, G.J., Hill, R.A. and Dodson, M.V. (2005). Dedifferentiation of mature adipocytes to form adipofibroblasts: 1. More than just a possibility Adipocytes 1:17-24. Kinkel, A.D., Fernyhough, M.E., Helterline, D.L., Vierck, J.L., Oberg, K.S., Vance, T.J., Hausman, G.J., Hill, R.A. and Dodson, M.V. (2005) Oil red-O stains non-adipogenic cells: A precautionary note. Cytotechnology.46:1-8. Indiana: Wang, X., G.H. Hockerman, H.W. Green, C.F. Babbs, S.I. Mohammad, D.E. Gerrard, M.A. Latour, B. London, K.M. Hannon and A.L. Pond. 2006. Merg1a K+ channel induces skeletal muscle atrophy by activating the ubiquitin-proteasome pathway. FASEB J. 20(9):1531-1533. Guo, Q, B.T. Richert, J.R. Burgess, D.D. Hall, D.M. Webel, D.E. Orr, Jr., M. Blair, G. Fitzner, A. L. Grant and D.E. Gerrard. 2006. Effects of dietary vitamin E and fat supplementation on pork quality J. Anim. Sci. 84: 3071-3078. Guo, Q., B.T. Richert, J.R. Burgess, D. Webel, D. Orr, M. Blair, A.L. Grant and D.E. Gerrard. 2006. Effect of dietary vitamin E supplementation and feeding period on pork quality J. Anim. Sci. 84: 3089-3099. Copenhafer, T.L., B.T. Richert, A.P. Schinckel, A.L. Grant, and D.E. Gerrard. 2006. Augmented postmortem glycolysis does not occur early postmortem in AMPK³3-mutated porcine muscle of halothane positive pigs. Meat Sci. 73(4) 590-599. Swartz, D.R., Z. Yang, A. Sen, S.B. Tikunova and J.P. Davis. 2006. Myofibrillar troponin exists in three states and there is signal transduction along skeletal myofibrillar thin filaments. J. Mol. Biol. 361:420-435. Gunawan, A.M., S.K. Park, J.M. Pleitner, L. Feliciano, A.L. Grant and D.E. Gerrard. Contractile protein content reflects myosin heavy chain isoform gene expression. J. Anim. Sci. (accepted). Gunawan, A.M., B.T. Richert, A.P. Schinckel, A.L. Grant and D.E. Gerrard Ractopamine induces differential gene expression in porcine skeletal muscles. J. Anim. Sci. (accepted). Xia, J., A.D. Weaver, D.E. Gerrard and G. Yao. 2006. Monitoring sarcomere structure changes in whole muscle with diffuse light reflectance. Optics Letters (In Press). Eddinger, T.E., J.D. Schiebout, and D.R. Swartz. Adherens junction associated protein distribution differs in smooth muscle tissue and acutely isolated cells. Am. J. Physiol. GI and Liver Physiology (In Press). Shi, H., A. Ricome, K.M. Hannon, A.L. Grant and D.E. Gerrard. Beta-adrenergic receptor agonist-induced skeletal muscle hypertrophy is fiber type-specific through differential involvement of the MAPK signaling pathway Am. J. Physiol. (submitted). Iowa: Bhosle, R. C., D. E. Michele, K. P. Campbell, Z. Li and R. M. Robson. 2006. Interactions of intermediate filament protein synemin with dystrophin and utrophin. Biochem. Biophys. Res. Commun. 346:768-777. Uyama, N., L. Zhao, E. Van Rossen, Y. Hirako, H. Reynart, D. H. Adams, Z. Xue, Z. Li, R. Robson, M. Pekny and A. Geerts. 2006. Hepatic stellate cells express synemin, a protein bridging intermediate filaments to focal adhesions. Gut 55: 1276-1289. Michigan: Allison, C.P., A.L. Marr, N.L. Berry, D.B. Anderson, D.J. Ivers, L.F. Richardson, K. Keffaber, R.C. Johnson and M. E. Doumit. 2006. Effects of halothane sensitivity on mobility status and blood metabolites of HAL-1843-normal pigs following rigorous handling. J.Anim. Sci. 84:1015-1021. Minnesota: Xi, G., E. Kamanga-Sollo, M. R. Hathaway, W. R. Dayton, and M. E. White. 2006. Effect of constitutive expression of porcine IGFBP-3 on proliferation and differentiation of L6 myogenic cells. Domest. Anim Endocrinol. 31:35-51. Xi. G., M. R. Hathaway, M. E. White and W. R. Dayton. 2006. Localization of insulin-like growth factor (IGFBP)-3 in cultured porcine embryonic myogenic cells before and after TGF-²1 treatment. Domest. Anim. Endocrinol. doi:10.1016/j.domaniend.2006.08.006 Xi, G., M.R., Hathaway, W.R. Dayton, and M.E., White. 2006. Growth factor mRNA expression during differentiation of porcine embryonic myogenic cells. J. Anim. Sci. (in press) Nebraska: Schulz, J.S., N. Palmer, J. Steckleberg, S.J. Jones, and M. Zeece. 2006. Microarray profiling of skeletal muscle sarcoplasmic reticulum proteins. Biochim. Biophysic. Acta. 1764:1429-1435. Ohio: Liu, C., McFarland, D.C., and Velleman, S.G. 2005. Effect of selection on MyoD and myogenin expression in turkeys with different growth rates. Poult. Sci. 84:376-384. Velleman, S.G., and Mozdziak, P.E. 2005. Effects of posthatch feed deprivation on heparan sulfate proteoglycan, syndecan-1, and glypican expression: Implications for muscle growth potential in chickens. Poult. Sci. 84:601-606. Velleman, S.G., and Nestor, K.E. 2005. Effect of genetic increases in egg production, age, and sex on muscle development in turkeys. Poult Sci. 84:1347-1349. Nestor, K.E., Anderson, J.W., and Velleman, S.G. 2005. Genetic variation in pure lines and crosses of large-bodied turkey lines. 3. Growth-related measurements on live birds. Poult Sci. 84:1341-1346. Nestor, K. E., Anderson, J. W., Hartzler, D., and Velleman, S.G. 2005. Genetic variation in pure lines and crosses of large-bodied turkeys. 4. Body shape and carcass traits. Poult. Sci. 84:1825-1834. Li, X., McFarland, D.C., and Velleman, S.G. 2006. Effect of transforming growth factor beta on decorin and beta 1 integrin expression during muscle development in chickens. Poult. Sci 85:326-332. Liu, C., McFarland, D.C., and Velleman, S.G. 2006. Membrane-associated heparan sulfate proteoglycans are differentially expressed in the skeletal muscle of turkeys with different growth rates. Poult. Sci. 85:422-428. Velleman, S.G., Liu, C., Coy, C.S., and McFarland, D.C. 2006. Effects of glypican-1 on turkey skeletal muscle cell proliferation, differentiation, and fibroblast growth factor 2 responsiveness. Dev. Growth Diff. 48:271-276. McFarland, D.C., Velleman, S.G., Pesall, J.E., and Liu, C. 2006. Effect of myostatin on turkey myogenic satellite cells and embryonic myoblasts. Comp. Biochem. Physiol. Pt A 144:501-508. Nestor, K.E., Anderson, J.W., Patterson, R.A., and Velleman, S.G. 2006. Genetics of growth and reproduction in the turkey. 16. Effect of repeated backcrossing of an egg line to a commercial sire line. Poult. Sci. 85:1550-1554. Velleman, S.G., and Nestor, K.E. 2006. Inheritance of breast muscle morphology in a line of turkeys selected long term for increased egg production, its randombred control line, and reciprocal crosses among them. Poult. Sci. (In press). South Dakota: Velleman, S. G., C. Liu, C. S. Coy, and D. C. McFarland. 2006. Effects of Glypican-1 on Turkey Skeletal Muscle Cell Proliferation, Differentiation, and Fibroblast Growth Factor 2 Responsiveness. Development, Growth and Differentiation. Development Growth & Differentiation 48:271-276. Liu, Caini, Douglas C. McFarland, Karl E. Nestor, and Sandra G. Velleman. 2006. Differential Expression of Membrane-associated Heparan Sulfate Proteoglycans in the skeletal muscle of turkeys with different growth rates. Poultry Science 85:422-428. Li, X., D. C. McFarland, and S. G. Velleman. 2006. Effect of Transforming Growth Factor Beta on Decorin and Beta 1 Integrin Expression during Muscle Development in Chickens. Poultry Science 85:326-332 McFarland, Douglas C., Sandra G. Velleman, Jane E. Pesall, and Caini Liu. 2006. Effect of Myostatin on Turkey Myogenic Satellite Cells and Embryonic Myoblasts. Comparative Biochemistry and Physiology 144(4): 501-508. Velleman, S. G., X. Li, C. S. Coy, C. Liu, and D. C. McFarland. Association of membrane-associated heparan sulfate proteoglycan expression and fibroblast growth factor-2 in turkey muscle satellite cells. (Submitted) McFarland, Douglas C., Sandra G. Velleman, Jane E. Pesall, and Caini Liu. The role of myostatin in chicken (Gallus domesticus) myogenic satellite cell proliferation and differentiation. General and Comparative Endocrinology (submitted) Wisconsin: Greaser, M.L., P.R. Krzesinski, C.M. Warren, B. Kirkpatrick, K.S. Campbell, and R. L. Moss. 2005. Developmental changes in rat cardiac titin/connectin: transitions in normal animals and in mutants with a delayed pattern of isoform transition. J. Mus. Res. & Cell Motil 26:325-332. Duan, Y., J. G. DeKeyser, D. Srinivasan, and M.L. Greaser. 2006. Studies on titin PEVK peptides and their interaction. Arch. Biochem. Biophys. 454:16-25. Dissertations: Illinois: Holmer, S.F. Effects of feeding regimen and enhancement on quality characteristics of muscles from beef cull cows. Master Thesis. University of Illinois. 2005. Kutzler, L.W. Effects of Feeding Regimens on Animal Growth, Longissimus Muscle DNA and Protein Concentration, Gene Expression and Protein Degradation in Beef Cull Cows. Masters Thesis. University of Illinois. 2006 Indiana: Guo Qinghai. Control of postmortem muscle metabolism in pigs. Ph.D., Purdue University, West Lafayette, IN. 2006. Iowa: Brooks, B. D. 2006. M.S. Thesis. Expression of ADP-ribosylation enzymes in mouse embryos and musle cell cultures. Iowa State University, Ames. 89p. Abstracts: Arizona: Camou, J.P., J.A. Marchello, and D.E. Goll. 2006. Effects of postmortem storage on µ- and m-calpain in bovine skeletal muscle. J. Anim. Sci. 84: Suppl. 1, 38. Camou, J.P., J.A. Marchello, S. Mares, R. Vasquez, and D.E. Goll. 2006. Effect of pH and temperature on activity of µ- and m-calpain. FASEB J. 20: A50. Mares, S.W., V.F. Thompson, and D.E. Goll. 2006. Degradation of myofibrillar proteins by µ- and m-calpain. FASEB J. 20: EB54. Neti. G., S. Mares, V.F. Thompson, and D.E. Goll. 2006. Easily releasable myofilaments and myofibrillar protein turnover. FASEB J. 20: A50. Rhoads, R. P., X. Liu, T. Cardinal, S. Sheehan, M. Morales, R. Cheatham, J. Hoying, and R. Allen. 2006.Aging impairs the ability of satellite cells to induce angiogenesis in vitro. FASEB J. 20: EB34. Taylor, M.D., V.F. Thompson, W. Wei, L.Z. Stern, and D.E. Goll. 2006. The calpain system in muscular dystrophy. FASEB J. 20: A50. Wendt, A., V.F. Thompson, S.W. Mares, and D.E. Goll. 2006. Role of phosphorylation on catalytic properties of m-calpain. FASEB J. 20: EB52. Hawaii: N.K. Bobbili, Y.K. Lee and Y.S. Kim. 2006. Production of a polyclonal antibody against unprocessed chicken myostatin and the effects of in-ovo administration of the antibody on post-hatch broiler growth and muscle mass. J. Anim. Sci. 84(suppl. 1):30 Y.S. Kim, Y.C. Huh and C.J. Kim. 2006. Maternal immunization against myostatin enhances post-hatch broiler growth and muscle mass. J. Anim. Sci. 84(suppl. 1):30 Idaho: Papasani, M.R., Halterman, K. and Hill, R.A. (2007). Defining the promoter region of a second insulin gene in zebrafish. Society of Integrative and Comparative Biology Meeting, Phoenix AZ. Stone, D.A.J., Hill, R.A. and Hardy, R.W. (2007). Strain differences in carbohydrate utilization by freshwater rainbow trout Oncorhynchus mykiss: Investigation of new molecular tools for genetic selection. World Aquaculture Society Meeting, San Antonio TX. Amberg, J.J., Rønnestad, I., Rust, M.B., Hill, R.A. and Hardy, R.W. (2007). Prey type and rearing density affects expression of the intestinal oligopeptide transporter, pept1, in larval cod Gadus morhua. World Aquaculture Society Meeting, San Antonio TX. Choi, J.M., Papasani, M.R. and Hill, R.A. (2006). Effect of linoleic and oleic acids on lipid accumulation and adipogenesis in 3T3-L1 cells. The Endocrine Society's 88th Annual Meeting. Papasani M.R., Robison, B.D., Hardy, R.W. and Hill, R.A. (2006). Temporal and spatial expression of two zebrafish insulin genes during early development. The Endocrine Society's 88th Annual Meeting. Amberg, J.J., Papasani, M.R., Cook, M.A., Hardy, R.W., Rust, M.B., Anderson, C.L. and Hill, R.A. (2006). An intestinal peptide transporter, pept1-like, identified in altricial larval fishes: beginning to understand the importance of intestinal peptide uptake in larval fishes. World Aquaculture Society Meeting, Las Vegas, NE. Papasani, M.R., Kokta, T.A., Strat, A.L., Gertler, A. and Hill, R.A. (2005) Regulation of gene expression in Sol8 myogenic cells in response to leptin. The Endocrine Society's 87th Annual Meeting, (accepted). Kokta, T.A., Strat, A.L., Papasani, M.R., Szasz, J.I., Dodson, M.V., and Hill, R.A. (2005) Regulation of Lipid Accumulation in 3T3-L1 cells: effects of Oleic and Linoleic Acids and Insulin. The Endocrine Society's 87th Annual Meeting, (accepted). Illinois: Kutzler, L.W., S.F. Holmer, C.M. Leick, F.K. McKeith and J. Killefer. Effects of Feeding Regimes on Animal Growth, Longissimus muscle DNA and Protein Concentration and Gene expression in Beef Cull Cows. Reciprocal Meat Conference. 2006 Iowa: Sun, N., Z. Li, D. Paulin, D. R. Critchley and R. M. Robson. 2005. Interactions of two isoforms of mammalian synemin with vinculin and metavinculin. Mol. Biol. Cell 16:85a. Veneziano, S. E., R. C. Bhosle, Z. Li, D. Paulin and R. M. Robson. 2005. Interaction between the intermediate filament protein synemin and ±-actinin in mammalian and avian muscle cells. Mol. Biol. Cell 16:85a. Sun, N. and R. M. Robson. 2006. Interactions of a novel intermediate filament protein with two costameric proteins in muscle cells. J. Anim. Sci. 84 (Suppl. 2);59. Veneziano, S. E., R. C. Bhosle and R. M. Robson. 2006. Unique interaction of intermediate filaments with ±-actinin in skeletal muscle cells. J. Anim. Sci. 84 (Suppl. 2):60. Michigan: Edwards, D.B., C.W. Ernst, N.E. Raney, M.E. Doumit, M.D. Hoge and R.O. Bates. 2006. QTL mapping in an F2 Duroc x Pietrain resource population: II. Carcass and meat quality traits. J.Anim. Sci. 84(Suppl. 2):49. Edwards, D.B., C.W. Ernst, N.E. Raney, R.J. Tempelman, M.D. Hoge and R.O. Bates. 2006. QTL mapping in an F2 Duroc x Pietrain resource population: I. Growth traits. 84(Suppl. 2):108. Helman, E.E., C.S. Quinlan, N.L. Berry, C.S. Abney, C.P. Allison, S.R. Rust, W.N. Osburn and M.E. Doumit. 2006. Qualitative characteristics of beef value cuts from Holstein and Angus cattle. Proc. Reciprocal Meat Conf. 59:13. Wiedmann, R., M. Doumit, L. Matukumalli, T. Sonstegard, L. Coutinho, D. Nonneman and T. Smith. 2006. Expression profiles of micro-RNAs in swine muscle development. Intl. Soc. Anim. Gen. (in press). Minnesota: X Gang, E. I. Kamanga-Sollo, M. R. Hathaway, M. E. White*, M. S. Pampusch, and W. R. Dayton. 2006. Localization of IGFBP-3 and IGFBP-5 in cultured porcine embryonic myogenic cells. J. Anim. Sci 84: suppl. 1 X. Gang, M. R. Hathaway, M. E. White, E. I. Kamanga-Sollo, M. S. Pampusch, and W. R. Dayton. 2006. Use of RNA interference (RNAi) to silence IGFBP-3 and IGFBP-5 expression in porcine embryonic myogenic cell cultures. J. Anim. Sci 84:suppl 1 South Dakota: Smith, C., D. C. McFarland, H. N. Oliveira, G. J. M. Rosa, A. M. Sanborn, S. J. Lindblom, J. Pesall, and A. J. M. Rosa. 2006. Gene expression analysis of differentiating avian myogenic satellite cells. Proceedings of the VIII World Congress on Genetics Applied to Livestock Production. Belo Horizonte, MG. Brazil. Wisconsin: Greaser, M.L. 2006. Developmental changes in cardiac and skeletal muscle titin PEVK in normal and mutant rats. Biophys. J. 90:259a

Impact Statements

Substantial contributions toward understanding the extracellular signals, intracellular signal transduction pathways, and nuclear mechanisms that govern myogenic cell activity.
Identification of differentially expressed genes during muscle development.
Progress to understand muscle protein characteristics, and the extracellular matrix on the regulation of myofibrillar assembly and disassembly.
Identification of possibilities for pharmacological intervention or targets for genetic selection to increase muscle growth.
Provide a foundation for the development of novel strategies to improve muscularity, increase the rate and efficiency of muscle growth, or improve meat quality.

Date of Annual Report: 12/03/2007

Report Information

Annual Meeting Dates: 10/04/2007 - 10/05/2007
Period the Report Covers: 10/01/2006 - 09/01/2007

Participants

Participants:
" Rhoads, Robert (rhoadsr@email.arizona.edu) -Arizona
" Goll, Darrel E. (darrel.goll@arizona.edu) -Arizona
" Kim, Yong Soo (ykim@hawaii.edu) -Hawaii
" Killifer, John (jkillef@uicu.edu) -Illinois
" Grant, Allan ( agrant@purdue.edu) -Indiana- Administrative Advisor
" Swartz, Darl (drsswartz@purdue.edu)- Indiana
" Dayton, William R. (wdayton@umn.edu) -Minnesota
" White, Michael (mwite@umn.edu) -Minnesota
" Mozdziak, Paul E. (pemozdzi@unity.ncsuedu) -North Carolina
" Velleman, Sandra (velleman.1@osu.edu) -Ohio
" Douglas McFarland (douglas.mcfarland@sdstate.edu) -South Dakota
" Penny K. Riggs (riggs@tamu.edu) -Texas
" Geaser, Marion (mgreaser@ansci.wisc.edu) -Wisconsin
" Du, Min (mindu@uwyo.edu) -Wyoming

Brief Summary of Minutes

Brief Summary of Minutes of Annual Meeting:

Members not attending: Ronald E. Allen-Arizona; Sally E. Johnson-Florida; Rod Hill-Idaho; David E. Gerrard-Indiana; Ted. Huiatt-Iowa; Richard M. Robson-Iowa; Bradley J Johnson-Kansas; Mathew E. Doumit-Michigan State; Catherine W. Ernst-Michigan State; Marcia R. Hathaway-Minnesota; Jane A. Boles-Montana; Steven J. Jones-Nebraska; Michael G. Zeece-Nebraska; Michael Dodson-Washington State University;

Guests: Dustin Boler, Anna Dilger, Savannah Gabiel, Sean Holmer, Lou Kutzler, Christine Leick, Stacy Scramlin, and Chad Souza, all from the University of Illinios.

The annual meeting of the NC-1131 technical committee meeting was held at the University of Illinois, Urbana on 4-5 October, 2007 and hosted by Dr. John Killefer, Department of Animal Sciences, University of Illinois. The group was welcomed by Dr. Neal Merchen, head of the Department of Animal Science, University of Illinois. Dr. Merchan summarized the student numbers and other properties of the University of Illinois and of the Department of Animal Science at the University of Illinois.

This year, many stations sent their annual reports electronically to the University of Illinois before the meeting date, so copies were printed at the meeting and made available to those who attended.

Following Dr. Merchans welcome, the remainder of the first day to 4:00pm was filled by oral station reports summarizing each stations contributions to the objectives of the NC-1131 project.

The business meeting, chaired by the Administrative Advisor, Dr. Alan Grant, began at 4:00pm. Dr. Grant reminded the committee that a mid-term review report summarizing the activities of the NC-1131 committee since the renewal of the project in 2005 was due by 15 December, 2007. Dr. Grant will contact those stations who had not sent a representative to the annual meeting of NC-1131 committee for several years to inquire about their intention to continue to participate. Two individuals, Dr. Peggy Riggs from Texas A & M University and Dr. Robert Rhoads from the University Arizona petitioned to be admitted as members of the NC-1131 committee. Both gave presentations at the meeting and after hearing descriptions of their research programs, the committee elected both individuals to membership. Dr.Debora Hamernik, the USDA-CSREES representative was unable to attend the meeting but sent material summarizing recent personnel changes in the USDA-CSREES, describing the 2007 Farm Bill, Investing in Research to Advance Agriculture, and listing the National Program Leaders and Program Specialists along with a summary of the funding data for the National Research Initiative.

Next years annual meeting of the NC-1131 committee will be held at the University of Arizona, Tucson, Arizona at a date yet to be determined. Dr. Min Du, University of Wyoming, was elected as secretary for the 2007-08 year with the expectation that the 2009 meeting will be held in Laramie, Wyoming. The business meeting ended the day, and station reports resumed the next morning. The meeting adjourned at 11:45am the following morning to allow participants time to return home that day.

Accomplishments

Accomplishments It is now well-established, to a considerable extent because of previous work by members of this committee, that satellite cells are crucial to postnatal growth of skeletal muscle in addition to being important contributors to skeletal muscle repair following injury. Without proper vascularization, myogenic cells do not survive. A co-culture of satellite and microvascular fragments has been developed and has been used to show that satellite cells can secrete angiogenic factors such as VEGF and that the satellite-derived VEGF will induce angiogenesis in the co-cultures. The studies indicate that a heretofore unknown aspect of satellite cells is their ability to initiate pro-angiogenic signals. Studies by other stations have shown that HGF (hepatocyte growth factor) induces a cell cycle-arrest of satellite cells, and that this cell cycle arrest requires MEK (MAP kinase kinase) activity. The level of nutrition and muscle type also affect satellite cells. Higher levels of nutrition increase the rate of proliferation of satellite cells obtained from turkey pectoralis thoracicus muscle. Satellite cells obtained from rat soleus muscle had higher numbers of Pax7, myoD, and myogenin-positive nuclei than satellite cells from rat externsor longus digitorum muscle, suggesting that the satellite cells from rat soleus muscle were posed for differentiation. Other studies have measured level of phosphorylation of MAP kinase (ERK 1/2 kinase) to learn whether phosphorylation of this kinase could be used as a marker to objectively measure the response of satellite cells to growth factor stimuli. The results indicated that the degree of phosphorylation of MAP kinase varied in response to different growth factors, although the responses did not correlate with proliferation rates of the individual clones. It is clear from the research done by committee members during the past year that skeletal muscle satellite cells are responsive to a number of external stimuli, but how these stimuli relate to differentiation and proliferation are still unclear. Some preliminary studies suggest that the phospholipid content of satellite cell plasma membranes may be involved in this responsiveness. Future studies by committee members will focus on the signaling pathways involved in satellite cell response to growth factor stimulants. The Arizona, Florida, North Carolina, and South Dakota stations are collaborating on this aspect of the regional project. Postnatal skeletal muscle growth can be altered by administration of either anabolic steroids such as estradiol or ²-adrenergic agonists such as clenbuterol or trenbolone acetate (TBA). Clenbuterol administration to mice during lactation resulted in an increased rate of muscle growth of the offspring, but such administration during gestation had no effect on rate of muscle accumulation of the offspring. Studies on bovine animals indicated that estradiol implants increased the rate of muscle growth by increasing satellite cell proliferation and subsequent fusion with the adjacent muscle fiber, whereas TBA implants increased rate of skeletal muscle growth by altering the rates of muscle protein synthesis and degradation. Other studies showed that estradiol and TBA implants increase the IGF-1 mRNA levels in longissimus muscle of steers but did not affect myostatin, IGFBP-3(IGF binding protein 3), or hepatocyte mRNA levels in the same muscle. If IGFBP-3 is removed from serum by immunoaffinity chromatography, estradiol and TBA both increased 3H-thymindine incorporation into cultures of bovine satellite cells by ~ 50% but did not affect IGF-1 mRNA levels. The use of agents that block binding to the estradiol receptor and the androgen receptor suggested that these two steroids are exerting their effects on proliferation by binding to their respective receptors. Zilpaterol, another ²-adrenergic agonist, also did not affect the rate of proliferation in cultures of satellite cells, but altered rates of protein synthesis and degradation. Hence the two agents seem to work by different mechanisms and may be expected to have synergistic effects of rates of postnatal muscle growth. The Illinois, Kansas, and Minnesota stations are collaborating on this part of the regional project. The NC-1131 committee also is working the role of the extracellular matrix in skeletal muscle growth. This work has focused on the role of the heparin sulfate proteoglycans, syndecan and glypican, in skeletal muscle development. Because so little is known about the role of the extraxcellular matrix in skeletal muscle growth and development, the experiments have been largely at the observation stage thus far. The cDNAs for glypican-1 and syndecan-4 have been cloned and some of the glycosylation sites on these clones have been mutated to determine the effects of glycosylation on muscle differentiation. Overexpression of glypican-1 in turkey satellite cells increased the FGF2 responsiveness of these cells during proliferation, whereas inhibition of glypican-1 expression with RNAi techniques decreased satellite cell proliferation, differentiation,and FGF2 responsiveness. Mutating three Ser residues that are glycosaminoglycan (GAG) sites reduced the effects of glypican on the proliferation and differentiation of the satellite cells, suggesting that glycosylation has an important role in the effects of glypican-1 on satellite cell differentiation. Overexpression of syndecan-4 decreased satellite cell proliferation and differentiation. Experiments using syndecan mutants have not been completed yet, but the results thus far suggest that glycosylation has little effect on the role of syndecan on satellite cell differentiation. The results indicate that the extracellular matrix has important effects on muscle cell growth and differentiation, although the area remains understudied. The Ohio station is taking the lead on this part of the regional project with assistance from the South Dakota station. The IGF-binding proteins (IGFBP) have received increasing attention in muscle growth and differentiation as recent results have shown that they have varied, important, and complex roles in skeletal muscle. Of the family of IGF-binding proteins that have been identified, IGFBP-3 is the principal IGFBP in skeletal muscle. IGFBP-3 is involved in facilitating the proliferation-suppressing effects of myostatin and TGF-² on cultured myoblasts, but studies using an IGFBP-3 antibody indicated that IGFBP-3 does not exert its effects through PSmad2, PSmad3, p38, MAP kinase, SnoN, of cyclin because expression of these signaling molecules did not change in the presence of anti-IGFBP-3 even though the ability of myostatin and TGF-² to inhibit proliferation of porcine embryonic myogenic cells (PEMC) was suppressed. Treatment of PEMC with TGF-² results in IGFBP-3 being translocated to the nucleus. Recent studies indicate that the low-density lipoprotein receptor-related protein 1 is involved in the mechanism by which IGFBP-3 facilitates the proliferation-suppressing effects of myostatin and TGF-² on cultured myoblasts. The Minnesota station is leading the efforts in learning how the IGFBPs function in skeletal muscle growth. The Ohio station is also investigating the effects of TGF-² on Samd2/3 phosphorylation and MD and myogenin expression in a different cell system, satellite cells. Although is has been well-documented that turnover of skeletal muscle protein has important effects on both rate and efficiency of skeletal muscle growth in domestic animals, the mechanism by which muscle proteins are turned over metabolically has not been studied. It is difficult to understand how myofibrillar proteins turnover because the myofibrillar structure must remain intact if the muscle is to preserve its contractile function. Yet, the myofibrillar proteins constitute 55-60% of all muscle protein, and it is clear that they turnover metabolically at different rates depending on the physiological state of the animal. At present, there seem to be two possible mechanisms for turnover of myofibrillar proteins: removal of the outer layer of filaments leaving the remainder of the myofibril intact and functional or exchange of individual proteins in the myofiril with newly synthesized or newly released individual myofibrillar proteins in the muscle cell cytoplasm. The NC-1131 committee is working on both possibilities. It is possible to remove ~ 0.1-0.5 % of the myofibrillar protein fraction by gently shearing myofibrils in the presence of ATP. These easily releasable myofilaments (ERMs) are identifiable entities in muscle because once they have been removed, additional ERMs cannot be obtained by shearing the residual myofibrils in the presence of ATP. Gentle treatment with purified calpain increases the amount of ERMs by 5-10-fold, suggesting that the calpains may initiate myofibrillar protein turnover as was first proposed over 30 years ago. Turning over myofibrillar proteins via ERMs, however, cannot explain how different isoforms of the myofibrillar proteins can be exchanged during muscle development. Other studies by NC-1131 members have shown that the subunits of the troponin complex in solution can exchange with troponin subunits in intact myofibrils and that this exchange can be quantitated by measuring rates of binding and dissociation. The extent to which these two mechanisms are used to turnover myofibrillar proteins in living muscle is still unclear, but it seems likely that both are involved. These studies involve a collaboration between the Indiana and Arizona stations. Studies on the role of signaling via the AMP-activated protein kinase (AMPK) in skeletal muscle growth has shown that AMPK signaling is linked to intracellular Ca2+ concentration by a mechanism involving Ca2+/ calmodulin-dependent protein kinase kinase; activity of the latter enzyme is dependent on Ca2+ as its name implies, and this enzyme, once activated by Ca2+, then phosphorylates AMPK to activate it. AMPK activity is decreased during hind limb unloading, a procedure that results in pronounced muscle wasting. AMPK activity is also necessary for expression of GLUT4, the principal glucose transporter in skeletal muscle. Other preliminary studies on AMPK indicate that it has a crucial role in adipogenesis in developing muscle. These studies involve the Indiana and Wyoming stations. Studies on titin and on the response of muscle to eccentric contractions (ECs) have discovered that a rat strain that has an autosomal mutation that alters titin isoform expression expresses a very large polypeptide of ~ 3,900-kDa; this is significantly larger than the native titin polypeptide of 3,000-kDa. The mutation is in chromosome 1 of the rat and not on chromosome 3 where the titin gene is located. A knockout mouse that lacks all three of the muscle ankyrin repeat proteins has a greater degree of torque loss after a bout of ECs than muscle from control mice but recovered at the same or even slightly faster rate than muscle from control mice (Wisconsin station). Modern biology is heavily dependent on new technologies, and several stations are working on developing technologies/procedures that can be used by the other stations in the studies described in the preceding paragraphs. Work has been done to develop a proteomics approach that can be used to characterize expression of different proteins (as opposed to mRNAs for these proteins) in response to different treatments or during different stages of muscle development/growth. This proteomics approach has thus far used protein microarrays and two-dimensional electrophoresis (Nebraska station). Microarrays have also be used to compare mRNA levels in normal and a transgenic mouse that expresses an inhibitor of myostatin activity. Fifty-one different genes are overexpressed in the transgenic mouse compared with the normal mouse. Verification of these genes and their identification are currently underway (Hawaii station). Other microarray studies are comparing expression of genes at different stages of development (57, 70, 90, 105 days of gestation and 1-,3-, 5- and 7-days postnatally) in the pig (Michigan station). A real-time PCR procedure for rapid quantitation of the message levels of different myosin heavy chains has been developed and a procedure for accurate quantitation of the different myosin heavy chains at the protein level is being developed, so mRNA expression and protein expression can be compared on the same sample (Illinois station). This is important because quantitation of mRNAs is becoming increasingly widespread, and some results have suggested that levels of mRNA and levels of actual protein are poorly related in many instances. Other research has focused on developing a technique to enrich cell suspensions for use in implantation into developing embryos. These studies have used chicken cells and fluorescence-activated cell sorting (FACS). Chimeric chickens have been obtained (North Carolina station). Studies on adipocytes have found that subcutaneous-derived mature adipocytes will dedifferentiate to form proliferative-competent adipofibroblasts, but that subsequent redifferentation is incomplete and that perimuscular-derived adipofibrioblasts behave differently than the subcutaneous-derived cells (Washington station). The physiological significance of these results awaits further analysis, but thus far, it seems that subcutaneous-derived adipocytes are programmed to follow a pathway different from perimusular-derived adipocytes.

Publications

Refereed Publications Barash, I., M.-L. Bang, L. Mathew, M. L. Greaser, J. Chen, and R. L. Lieber. 2007. Structural and regulatory roles of the muscle ankyrin repeat protein family in skeletal muscle. Am.J. Physiol. Cell Physiol. 293:C218-C217 Brown, K. R., R. D. Goodband, M. D. Tokach, S. S. Dritz, J. L. Nelssen, J. E. Minton, J. J. Higgins, J. C. Woodworth, and B. J. Johnson. 2007. Growth characteristics, blood metabolites, and IGF system components in maternal tissues from gilts fed L-carnitine through day 70 of gestation J. Anim. Sci. 85:1687-1694. Christensen, V.L., Ort, D.T., Nestor, K.E., Velleman, S.G., and Havenstein, G.B. 2007. Genetic control of neonatal growth and intestinal maturation in turkeys. Poult. Sci. 86:476-487. Davis, J.D., C. Alionte, T. Kobayashi, R.J. Solaro, D.R. Swartz, and S. Tikunova. 2007. Effects of thin and thick filament proteins on calcium binding and exchange with cardiac troponin C. Biophys. J. 92: 3195-3206. Dodson, M.V. 2006. Career check-up, rather than check-out. NACTA J. 50:67-70. Dodson, M.V. 2006. Scholars or bankers? NACTA J. 50:102. Dodson, M.V. 2007. In order to recruit animal sciences students into the university, you need to teach them about animal science jobs. NACTA J. 51:72-73. Dodson, M.V. 2007. Codger and computers: to "unplug" or not to "unplug?" NACTA J. 51:72. Dodson, M.V., M.E. Fernyhough and B.B. Holman. 2006. Advising graduate students: Mentor or tormentor? NACTA J. 50:39-43 Dodson, M.V., M.E. Fernyhough and J.L Vierck. 2006. Work environments are critical for maximum productivity in teaching and research efforts in animal sciences. NACTA J. 50:64-67 Du, M., Q. W. Shen, M. J. Zhu, and S. P. Ford. 2007. Leucine stimulates mTOR signalling in C2C12 myoblast cells through inhibition of AMP-activated protein kinase. J. Anim. Sci. 85: 919-927. Eash, J., A. Olsen, G. Breur, D. Gerrard and K. Hannon. 2007. FGFR1 inhibits skeletal muscle atrophy associated with hindlimb suspension. BMC Musculoskelet Disord. 8:32. Eddinger, T.E., J.D. Schiebout, and D.R. Swartz. 2007. Adherens junction associated protein distribution differs in smooth muscle tissue and acutely isolated cells. Am. J. Physiol. 292:G684-697. Fernyhough, M.E., J.L. Vierck and M.V. Dodson. 2006. Assessing a non-traditional view of adipogenesis: adipocyte dedifferentiation mountains or molehills? Cells, Tissues, Organs (formerly ACTA Anatomica; 287 libraries worldwide) 182: 226-228 Fraser, J. N., B. L. Davis, K. A. Skjolaas, T. E. Burkey, S. S. Dritz, B. J. Johnson, and J. E. Minton, 2007. Effects of feeding Salmonella enterica serovar Typhimurium or serovar Choleraesuis to weaned pigs on growth performance and circulating insulin-like growth factor-I, tumor necrosis factor alpha, and interleukin-1 beta. J. Anim. Sci. 85:1161-1167. Gunawan, A.M., B.T. Richert, A.P. Schinckel, A.L. Grant and D.E. Gerrard. 2007. Ractopamine induces differential gene expression in porcine skeletal muscles. J. Anim. Sci. 85(9):2115-24. Kim, Y.S., N.K. Bobbili, Y.K. Lee and M. Dunn. 2007. Production of a polyclonal antibody against unprocessed chicken myostatin and the effects of in-ovo administration of the antibody on post-hatch broiler growth and muscle mass. Poult. Sci. 86:1196-1205 Lee, S.B., Y.S. Kim and H.J. Jin. 2007. Characterization and expression pattern of myostatin in the rockfish, Sebastes schlegeli. J. Fisheries Sci. Technol. 10:60-67. Li, X., McFarland, D.C., and Velleman, S.G. 2006. Effect of transforming growth factor beta on decorin and beta 1 integrin expression during muscle development in chickens. Poult. Sci 85:326-332. Liu, C., McFarland, D.C., and Velleman, S.G. 2006. Membrane-associated heparan sulfate proteoglycans are differentially expressed in the skeletal muscle of turkeys with different growth rates. Poult. Sci. 85:422-428. McFarland, D.C., Velleman, S.G., Pesall, J.E., and Liu, C. 2006. Effect of myostatin on turkey myogenic satellite cells and embryonic myoblasts. Comp. Biochem. Physiol. Pt A 144:501-508. McFarland, D.C., Velleman, S.G., Pesall, J.E., and Liu, C. 2007. The role of myostatin in chicken (Gallus domesticus) myogenic satellite cell proliferation and differentiation. Gen. Comp. Endocrinol. 151:351-357. Meeson AP, Shi X, Alexander MS, Williams RS, Allen RE, Jiang N, Adham IM, Goetsch SC, Hammer RE, Garry DJ. (2007). Sox15 and Fhl3 transcriptionally coactivate Foxk1 and regulate myogenic progenitor cells. EMBO J. 26:1902 12. Mei J. Zhu, S. P. Ford, W. J. Means, B. W. Hess, P. W. Nathanielsz, and M. Du. (2006) Maternal nutrient restriction affects muscle fiber number and composition in skeletal muscle of offspring. J. Physiol. 575: 241-250. Nestor, K.E., Anderson, J.W., Patterson, R.A., and Velleman, S.G. 2006. Genetics of growth and reproduction in the turkey. 16. Effect of repeated backcrossing of an egg line to a commercial sire line. Poult. Sci. 85:1550-1554. Reed SA, Ouellette SE, Liu X, Allen RE, Johnson SE. (2007). E2F5 and LEK1 translocation to the nucleus is an early event demarcating myoblast quiescence. J Cell Biochem.101:1394 408. Rilington, V.D., N.E. Raney and C.W. Ernst. 2006. Radiation hybrid mapping of 24 porcine skeletal muscle expressed sequence tags. Anim. Genet. 37:302-304. Saito, M., H. Li, V.F.Thompson, N. Kunisaki, and D.E. Goll. 2007. Purification and characterization of calpain and calpastatin from rainbow trout, Oncorhynchus mykiss. Comp. Biochem. Physiol. 146: 445-455. Scheffler, T.L. and D.E. Gerrard. 2007. Mechanisms controlling pork quality development: The biochemistry controlling postmortem energy metabolism. Meat Sci. 77(1):7-16. Shen, Q. W., W. J. Means, S. A. Thompson, K. R. Underwood, M. J. Zhu, R. J. McCormick, S. P. Ford, and M. Du. 2006. Pre-slaughter transport, AMP-activated protein kinase, glycolysis, and quality of pork loin. Meat Sci. 74:388-395. Shen, Q. W., W. J. Means, S. A. Thompson, K. R. Underwood, M. J. Zhu, R. J. McCormick, S.P. Ford, and M. Du. (2006). Early AMP-activated protein kinase (AMPK) activation leads to PSE meat in pork. J. Agric.Food Chem. 54: 5583-5589. Shen, Q. W., K. R. Underwood, W. J. Means, R. J. McCormick, and M. Du. 2007. Halothane gene, energy metabolism, AMP-activated protein kinase, and glycolysis in postmortem pig longissimus dorsi muscle. J. Anim. Sci. 85: 1054-1061. Shi, H., C. Zeng A. Ricome, K.M. Hannon, A.L. Grant and D.E. Gerrard. 2007. Extracellular signal regulated kinase pathway is differentially involved in beta-agonist-induced hypertrophy in slow and fast muscles. Am. J. Physiol. Cell Physiol. 292: C1681-C1689. Sissom, E. K., C. D. Reinhardt, J. P. Hutcheson, W. T. Nichols, D. A. Yates, R. S. Swingle, and B. J. Johnson. 2007. Response to ractopamine-HCl in heifers is altered by implant strategy across days on feed. J. Anim. Sci. 85:2125-2132. Sissom, E. K., C. D. Reinhardt, and B. J. Johnson. 2006. Melengestrol acetate alters carcass composition in feedlot heifers through changes in muscle cell proliferation. J. Anim. Sci. 84:2950-2958. (published after last years meeting) Velleman, S.G. 2007. Muscle development in the embryo and hatchling. Poult. Sci. 86:1050-1054. Velleman, S.G., Coy, C.S., and McFarland, D.C. 2007. Effect of syndecan-1, syndecan-4, and glypican-1 on turkey muscle satellite cell proliferation, differentiation, and responsiveness to fibroblast growth factor 2. Poult. Sci. 86:1406-1413. Velleman, S.G., Liu, C., Coy, C.S., and McFarland, D.C. 2006. Effects of glypican-1 on turkey skeletal muscle cell proliferation, differentiation, and fibroblast growth factor 2 responsiveness. Dev. Growth Diff. 48:271-276. Velleman, S.G., and Nestor, K.E. 2006. Inheritance of breast muscle morphology in a line of turkeys selected long term for increased egg production, its randombred control line, and reciprocal crosses among them. Poult. Sci. 85:2130-2134. Xia, J., A. Weaver, D.E. Gerrard and G. Yao. 2008. Heating induced optical property changes in beef muscle. J. Food Eng. 84: 75-81. Walker, D. K., E. C. Titgemeyer, E. K. Sissom, K. R. Brown, J. J. Higgins, and B. J. Johnson. 2007. Effects of steroidal implantation and ractopamine-HCl on nitrogen retention, blood metabolites, and longissimus mRNA expression of IGF-I in Holstein steers. J. Anim. Physiol. Anim. Nutr. 91:439-447. Winterholler, S. J., G. L. Parsons, C. D. Reinhardt, J. P. Hutcheson, W. T. Nichols, D. A. Yates, R. S. Swingle, and B. J. Johnson. 2007. Response to ractopamine-hydrogen chloride is similar in yearling steers across days on feed. J. Anim. Sci. 85:413-419. Xi, G., M. R. Hathaway, W. R. Dayton, and M. E. White. 2007. Growth factor messenger ribonucleic acid expression during differentiation of porcine embryonic myogenic cells. J. Anim Sci. 85:143-150. Zhang, X., Liu, C., Nestor, K.E., McFarland, D.C., and Velleman, S.G. 2007. The effect of glypican-1 glycosaminoglycan chains on turkey myogenic satellite cell proliferation, differentiation, and fibroblast growth factor 2 responsiveness. Poult. Sci. 86:2020-2028. Genebank Submission Kimzey, J. M. and M. Du. 2007. Ovis aries AMP-activated protein kinase a2 subunit cDNA complete coding sequence. Genebank accession number: EU131097. In Press Arnett, A. M., M. E. Dikeman, C. W. Spaeth, B. J. Johnson, and B. Hildabrand. 2007. Effects of vitamin A supplementation in young lambs on performance, serum lipid, and longissimus muscle lipid composition. J. Anim. Sci. 85: (in press). Brown, K. R., R. D. Goodband, M. D. Tokach, S. S. Dritz, J. L. Nelssen, J. E. Minton, J. J. Higgins, X. Lin, J. Odle, J. C. Woodworth, and B. J. Johnson. 2007. Effects of feeding L-carnitine to gilts through day 70 of gestation on litter traits and the expression of insulin-like growth factor system components and L carnitine concentration in foetal tissues. J. Anim. Physiol. Anim. Nutr. (In press, DOI: 10.1111/j.1439- 0396.2007.00762.x) Chester-Jones, H., and S.G. Velleman. 2007. Growth and development symposium: Transcriptional factors and cell mechanisms for regulation of growth and development with application to animal agriculture. J. Anim. Sci. (in press). Collier, R.J., J.L. Collier, R.P. Rhoads, and L.H. Baumgard. 2007. Genes involved in the bovine heat stress response. (in press). Dayton, W. R. and White, M. E. 2007. Cellular and molecular regulation of muscle growth and development in meat animals. J. Animal Sci. (in press, PMID: 17709769) Elwakeel, E. A., E. C. Titgemeyer, B. J. Johnson, C. K. Armendariz, and J. E. Shirley. 2007. Fibrolytic enzymes to increase nutritive value of dairy feedstuffs. J. Dairy Sci. (in press). Fernyhough, M.E., E. Okine, G. Hausman, J.L. Vierck and M.V. Dodson. 2007. Invited review: PPAR-gamma and GLUT-4 expression as differentiation markers for preadipocyte conversion to become an adipocyte. Domestic Anim. Endocrin. (in press). Goll, D.E., G. Neti, S.W. Mares, and V.F. Thompson. 2007. Myofibrillar protein turnover: the proteasome and the calpains. J. Anim. Sci: 85: (in press). Han, B., Junfeng Tong, C. Ma, M. J. Zhu, and M. Du. 2007. Insulin-like growth factor-1 (IGF-1) and leucine stimulate mammalian target of rapamycin (mTOR) signaling in pig myogenic satellite cells. Mol. Reprod. Develop. (in press). Han, B., M. J. Zhu, J. Tong, C. Ma, and M. Du. 2007. Rat hindlimb unloading induces down-regulation of insulin like growth factor-1 signaling and AMP-activated protein kinase, and severe atrophy of Soleus muscle. Appl. Physiol. Nutr. Metabol. (in press). Hoekstra, K.A., and Velleman, S.G. 2007. Brain microvascular and intracranial artery resistance to atherosclerosis is associated with heme oxygenease ferritin. Mol. Cell. Biochem. (in press). Mir, P.S., K. Schwartzhoph-Genswein, E. Okine, and M.V. Dodson. 2007. Effect of a short duration feed withdrawal followed by full feeding on marbling fat in beef carcasses. Livestock Sci. (in press). Shen, Q.W., D.E. Gerrard, and M. Du. 2007. Compound C, an inhibitor of AMP-activated protein kinase, inhibits glycolysis in mouse longissimus dorsi postmortem Meat Sci. In press. Shen, Q. W., M. J. Zhu, J. Tong, J. Ren, and M. Du. 2007. Ca2+/calmodulin-dependent protein kinase kinase is involved in AMP-activated protein kinase activation by a-lipoic acid in C2C12 myotubes. Am. J. Physiol.-Cell Physiol. (in press). Tatsumi, R. and Allen, R.E. 2007. Mechano-biology of resident myogenic stem cells: molecular mechanism of stretch-induced activation of satellite cells. (in press). Underwood K.R., J. Tong, M. J. Zhu, Q. W. Shen, W. J. Means, S. P. Ford, S. I. Paisley, B. W. Hess, and M. Du. (2007). Relationship between kinase phosphorylation, muscle fiber typing and glycogen accumulation in longissimus dorsi muscle of beef cattle with high and low intramuscular fat. J. Agri. Food Chem. (in press). Xi, G., M. R. Hathaway, M. E. White, and W. R. Dayton. 2007. Localization of insulin-like growth factor (IGFBP)-3 in cultured porcine embryonic myogenic cells before and after TGF-beta(1) treatment. Domest. Anim. Endocrinol. (in press, PMID: 17049199) Zhou, X., D. F. Li, J. D. Yin, J. J. Ni, B, Dong, J. X. Zhang, and M. Du. 2007. Conjugated linoleic acid differently regulates adipogenesis in stromal vascular cells from subcutaneous adipose tissue and skeletal muscle of neonatal pigs. J. Lipid Res. (in press). Abstracts Brazle, A. E., T. Rathbun, B. J. Johnson, and D. Davis. 2007. Omega-3 fatty acid supplementation and the IGF system in early pregnancy in pigs. J. Anim. Sci. 85 (Suppl. 1):88. Camou, J.P., S.W. Mares, J.A. Marchello, R. Vazquez, M.D. Taylor, V.F. Thompson, and D.E. Goll. 2007. Isolation and characterization of µ-calpain, m-calpain, and calpastatin from postmortem muscle. I. Initial steps. J. Anim. Sci. 85: Suppl.1, 281. Coy, C.S., Nestor, K.E., and Velleman, S.G. 2007. Effect of selection for increased egg production, age, and sex on turkey breast muscle development. Poult. Sci. 86 (suppl. 1): W53. Dilger, A. C., R. N. Dilger, L.W.Kutzler, and J. Killefer. (2007). Effect of juvenile clenbuterol exposure on growth in mice. J. Anim. Sci. 85 (Suppl. 1): 280. Dilger, A. C. and J. Killefer (2007). Clenbuterol increases muscle mass in myostatin knockout mice. FASEB J. 21(6): A944-d-945. Du, M., B. Han, M. J. Zhu, P. W. Nathanielsz, S. P. Ford. 2007. Insulin signaling and AMP-activated protein kinase are down-regulated in skeletal muscle of overnourished, obese pregnant sheep. Ann. Meeting Soc. Study Reprod. San Antonio, Texas, July 21 to July 25. Du, M., B. Han, M. J. Zhu, P. W. Nathanielsz, S. P. Ford. 2007. Down-regulation of AMP-activated protein kinase in fetal muscle of obese, overnourished pregnant sheep. Ann. Meeting Soc. Study Reprod. San Antonio, Texas, July 21 to July 25. Goll, D.E., G.Neti, S.W. Mares, and V.F. Thompson. 2007. The non-lysosomal Ca2+-dependent protein degradation pathway: the calpains, proteasome, and myofibrillar protein turnover. J. Anim. Sci. 85: Suppl. 1, 445. Goll, D.E., A.S.Wendt, V.F. Thompson, S.W. Mares, and R. Vazquez. 2007. Phosphorylation of the calpains. FSEB Summer Research Conference, Biology of the Calpains in Health and Disease. p. 5. Greaser, M.L. and W. Guo. 2007. Messenger RNA changes in a rat strain with altered cardiac titin isoform expression. Biophys. J. (in press). Han, B., C. W. Ma, M. J. Zhu, Q. W. W. Shen, and M. Du. (2007) Leucine supplementation mitigates atrophy of non-weight-bearing skeletal muscle in rats. FASEB J. 21: A1205-A1205. Harborth, K. W., T. T. Marston, J. A. Unruh, and B. J. Johnson. 2007. Effects of ractopamine HCl and steroid implants on feedlot performance and carcass characteristics of cull beef cows. J. Anim. Sci. 85 (Suppl. 1):547. Harborth, K. W., T. T. Marston, J. A. Unruh, and B. J. Johnson. 2007. Effect of age on feedlot performance and carcass characteristics of cull beef cows. J. Anim. Sci. 85 (Suppl. 1):547. Johnson, B. J. 2007. Application of cellular mechanisms to growth and development of food producing animals. J. Anim. Sci. 85 (Suppl. 1):638. Kutzler, L. W., A. C. Dilger, P.J.Rincker, and J. Killefer. (2007). Integrity of porcine myosin heavy chain mRNA collected up to 72 hours postmortem. FASEB J. 21(6): A1308. Li, J., S.A. Reed and S.E. Johnson. 2007. Hepatocyte growth factor induces cell cycle withdrawal in satellite cells in a MAPK-dependent manner. Mol. Biol. Cell 18: Li, X., McFarland, D.C., and Velleman, S.G. 2007. Reduction in cell responsiveness to transforming growth factor-beta by decorin overexpression increases satellite cell proliferation and differentiation. Poult. Sci. 86 (suppl. 1): 458. Mares, S.W., V.F. Thompson, G. Beinbreck, and D.E. Goll. Do the calpains degrade actin, ±-actinin, and myosin? FASEB J. 21: A647. Mares, S.W., V.F. Thompson, G. Beinbreck, and D.E. Goll. 2007. Do the calpains degrade actin, ±-actinin, or myosin? FASEB Summer Research Conference, Biology of the Calpains in Health and Disease. Abstract #10, McFarland, D. C. and J. E. Pesall. 2007. Phospho-MAPK as a marker of myogenic satellite cell responsiveness to growth factors. J. Anim. Sci. 85, suppl. 1:47. Miller, W. F., B. J. Johnson, E. C. Titgemeyer, J. F. Smith, J. E. Shirley, and T. G. Nagaraja. 2007. Effect of cane molasses on ruminal absorptive capacity of dairy cows during the periparturient period. J. Anim. Sci. 85 (Suppl. 2):88. Parsons, G. L., K. A. Harborth, M. J. Quinn, T. T. Marston, J. S. Drouillard, and B. J. Johnson. 2007. Effects of combined trenbolone acetate and estradiol implant and/or ractopamine-HCl administration on circulating insulin-like growth factor-I and skeletal muscle gene expression in cull cows. Proc. Plains Nutrition Spring Conference. Pub. AREC 07-20. Texas A & M Research and Extension Center, Amarillo. p. 104. Price, P.L., M. Du, S.I. Paisley, V. Nayigihugu, J.D. Hess, and B.W. Hess. 2007. Beef cow performance in response to early through mid-gestational nutrient restriction and provision of supplementary ruminally undegradable protein. Western Section ASAS Meeting, Moscow, Idaho, June 20-22. Scheffler. J. M., A.K. Batie, and S.J. Jones, 2007, Lysophosphatidic acid stimulates increases in ERK-1/2 and proliferation of C2C12 cells but does not result in a significant increase in total DNA. J. Anim. Sci. Vol. 85, Suppl 1:46. Sissom, E. K., D. A. Yates, J. L. Montgomery, W. T. Nichols, M. N. Streeter, J. P. Hutcheson, and B. J. Johnson. Effect of zilpaterol on cultured bovine satellite cells. J. Anim. Sci. 85 (Suppl. 1):295. Shen, Q. W., and M. Du. 2007. Ca2+/calmodulin-dependent protein kinase kinases are involved in AMP-activated protein kinase activation by alpha-lipoic acid in C2C12 myotubes. 2007 Graduate Student Symp. April 3-4. Shen, Q.W.W., J. Ren, and M. Du. (2007) Ca2+/calmodulin-dependent protein kinase kinases are mainly responsible for AMP-activated protein kinase activation by alpha-lipoic acid in C2C12 myotubes. FASEB J. 21: A1204-A1205. Taylor, M., V.F. Thompson, and D.E., Goll. 2007. The calpain system in human muscular dystrophy. FASEB Summer Research Conference, Biology of the Calpains in Health and Disease. Abstract #15. Tong, C.W., Powers, P.A., Greaser, M.L., Dunning, S.B., Hacker, T.A., Wu, X., Muthuchamy, M., and R. L. Moss. 2006. Modulation of cardiac function by phosphorylation of myosin binding protein C. Amer. Heart Assoc. Abstr. Tong, C., P. Powers, M. Greaser, T. Hacker, and R. Moss. 2007. Phosphorylation of myosin binding protein-C enhances in vivo cardiac contractility. Biophys. J. Suppl., POS-L177 . Tong, J., K. R. Underwood, J. M. Kimsey, M. J. Zhu, W. J. Means, and M. Du. 2007. Myosin type IIb isoform is absent in the longissimus dorsi muscle of beef cattle. 60th Reciprocal Meat Conf. Brookings, South Dakota. June 17-20. Underwood, K. R., and M. Du. 2007. AMP activated protein kinase is negatively associated with intramuscular fat in beef cattle. 2007 Graduate Student Symp. April 3-4. Underwood, K. R., W. J. Means, and M. Du. (2007) Caspase-3 is not activated in postmortem beef and lamb muscle. Midwest Soc. Anim. Sci. Ann. Meeting, Des Moines, Iowa, March 19-21. Underwood, K. R., J. Zhu, W. J. Means, and M. Du. 2007. AMP-activated protein kinase is negatively associated with marbling in beef cattle. 60th Reciprocal Meat Conf. Brookings, South Dakota. June 17-20. Wallace, J. O., W. F. Miller, C. D. Reinhardt, and B. J. Johnson. 2007. Adaptation of feedlot cattle by limit-feeding a high-concentrate diet may alter nutrient absorption. J. Anim. Sci. 85 (Suppl. 2):80. Wallace, J. O., W. F. Miller, C. D. Reinhardt, and B. J. Johnson. 2007. Limit-feeding a high-concentrate diet may alter nutrient absorption. Proc. Plains Nutrition Spring Conference. Pub. AREC 07-20. Texas A & M Research and Extension Center, Amarillo. Page 110. Winterholler, S. J., A. S. Webb, G. L. Parsons, D. K. Walker, M. J. Quinn, J. S. Drouillard, and B. J. Johnson. 2007. Effects of combined trenbolone acetate and estradiol implant and/or ractopamine-HCl administration versus natural beef production in finishing steers. Proc. Plains Nutrition Spring Conference. Pub. AREC 07-20. Texas A & M Research and Extension Center, Amarillo. p.113. Zhang, X., Liu, C., Nestor, K.E., McFarland, D.C., and Velleman, S.G. 2007. The role of glypican-1 glycosaminoglycan chains in myogenic satellite cell proliferation, differentiation, and fibroblast growth factor 2 responsiveness. Poult. Sci. 86 (suppl. 1):457. Zhu, M. J., M. Du, B.W. Hess, P.W. Nathanielsz, and S.P. Ford. 2007. Localization of key growth signaling proteins in placentomes of overfed ewes. Soc. Gynecologic Invest. Reno, Nevada, March 14-17. Zhu, M. J., S. P. Ford, and M. Du. 2007. Androgen enhances both Akt/mTOR and MAPK signaling in C2C12 myoblast cells. FASEB J. 21: A1205-A1205. Zhu, M.J., J. M. Kimsey, J. Tong, S. P. Ford, P. W. Nathanielsz, and M. Du. 2007. Enhanced adipogenesis and decreased AMPK activity in fetal muscle of obese, overnourished pregnant sheep. Aspen Perinatal Biol. Symp. The Given Institute, Aspen, Colorado, August 25 to 28. Zhu, M. J., J. Tong, K. R. Underwood, and M. Du. 2007. Activation of AMP-activated protein kinase inhibits adipogenesis in 3T3 cells. 60th Reciprocal Meat Conf. Brookings, South Dakota. June 17-20. Book Chapters Johnson, B. J., and K. Y. Chung. 2007. Alterations in the physiology of growth of cattle with growth-enhancing compounds. In: Vet. Clin. Food Anim. 23:321-332. Reinhardt, C. D., and B. J. Johnson. 2007. Growth Promotants for Beef Production - Anabolic Steroids: Performance responses and Mode of Action. Current Veterinary Therapy. D.U. Thomson, Ed. (in press). Velleman, S.G. and C. Liu. 2006. "Structure and Function of Cell Associated and Pericellular Heparan Sulfate Proteoglycans," in Chemistry and Biology of Heparin and Heparan Sulfate. eds. H. G. Garg, R.J. Linhardt, and C.A. Hales, Elsevier Publishing, 29-54 . Theses Bobbili, Naveen. Effects of maternal immunization against myostatin on skeletal muscle mass of offspring in mice. M.S. Thesis,University of Hawaii. Neary, Kathy. In vitro comparison of satellite cells isolated from normal and callipyge sheep exposed to growth promoting hormones. M.S. Thesis, Montana State University. Scheffler J.M. 2007 Lysophosphatidic acid but neither clenbuterol nor salbutamol, stimulates increases in ERK-1/2 phosphorylation which is not associated with an appreciable increase in proliferation. Ph.D. Dissertation, University of Nebraska. Shi, Hao. Modulation of skeletal muscle fiber growth and specialization by mitogen-activated protein kinase pathways. Ph.D. Dissertation, Purdue University. Weaver, A.D. Sarcomere length influences proteolysis. Ph.D. Dissertation, Purdue University. Please visit and contribute to OUR NC-1131 web site: http://ars.sdstate.edu/nc131/main.htm

Impact Statements

Dr. S. Velleman (co-chair Dr. H. Chester-Jones) organized a symposium on growth and development at the 2007 Joint Annual Meeting of the American Dairy Science Association, the Poultry Science Association, the Asociación Mexicana de Producción Animal, and the American Society of Animal Science held in San Antonio, TX from 8-12 July. Three of the 4 speakers were NC-1131 members; Drs. M. Doumit, W. Dayton, and B. Johnson. The presentations were selected for publication in the Journal of Animal Science; one of only a few of the symposia held at the meeting that were selected.
Committee members were invited to give over 25 oral presentations at national scientific and livestock meetings during the past year. The presentations covered a wide range of topics from basic laboratory results to applying this basic knowledge to the animal industry. The number of invited presentations and variety of audiences testify to the quality of work and impact that this committee has on muscle growth in domestic animals.
Procedures have been developed for expressing two important extracellular matrix (ECM )proteins in muscle cells and then having the expressed proteins transported out of the cell and assemble in a functional manner in the extracellular milieu. Availability of these procedures will allow for the first time mechanistic studies of the role of the ECM in skeletal muscle development and growth, something that has been impossible up to now.
Microarray analysis has identified 51 genes that are overexpressed in transgenic mice that express an inhibitor of myostatin. Because myostatin has important effects on skeletal muscle growth, verification and identification of the genes whose expression is affected by its inhibition has potentially very important implications and raises the possibility that new genes having important roles in postnatal muscle growth may be identified.
Research by the committee on the effects of growth promotants such as anabolic steroids has progressed beyond the administer and observe stage to determining the signaling pathways in muscle cells that are involved in the response to these steroids. This new effort will undoubtedly reveal a complex and initially bewildering array of signaling molecules, pathways, and interactions, but eventually could lead to an understanding that will permit rational approaches to significantly increasing the rate of skeletal muscle growth.

Date of Annual Report: 11/08/2008

Report Information

Annual Meeting Dates: 11/07/2008 - 11/08/2008
Period the Report Covers: 10/01/2007 - 09/01/2008

Participants

Participants:
" Robert Rhoads (rhoadsr@email.arizona.edu) -Arizona
" Ronald. E. Allen (rallen@ag.arizona.edu)
" Sally E. Johnson (sjohnson@animal.ufl.edu) -Florida
" John Killefer (jkillef@uicu.edu) -Illinois
" Alan Grant ( agrant@purdue.edu) -Indiana- Administrative Advisor
" David E. Gerrard (dgerrard@purdue.edu) -Indiana
" Shihuan Kuang (skuang@purdue.edu) - Indiana
" Steven J. Jones (sjones1@unl.edu) - Nebraska
" Catherine W. Ernst (ernstc@msu.edu) -Michigan
" William R. Dayton (wdayton@umn.edu) -Minnesota
" Michael White (mwite@umn.edu) -Minnesota
" Sandra Velleman (velleman.1@osu.edu) -Ohio
" Penny K. Riggs (riggs@tamu.edu) -Texas
" Marion Geaser (mgreaser@ansci.wisc.edu) -Wisconsin
" Min Du (mindu@uwyo.edu) -Wyoming

Brief Summary of Minutes

Brief Summary of Minutes of Annual Meeting:
Members not attending: Rod Hill-Idaho; Mathew E. Doumit-Idaho; Marcia R. Hathaway-Minnesota; Jane A. Boles-Montana; Michael G. Zeece-Nebraska; Michael Dodson-Washington State;
The annual meeting of the NC-1131 technical committee meeting was held at the University of Arizona, Tucson on 7-8 November, 2008 and hosted by Dr. Robert Rhoads, Department of Animal Sciences, University of Arizona. The group was welcomed by Dr. Ronald Allen, head of the Department of Animal Science, and Dr. Colin Kaltenbach, the director of Arizona Agricultural Experimental Station. Dr. Kaltenbach gave an overview of agriculture in Arizona and presented problems and opportunities for Arizona agriculture.
Following Dr. Kaltenbach's welcome, the remainder of the first day to 4:00pm was filled by oral station reports summarizing each station's contributions to the objectives of the NC-1131 project. After 4:00 pm, there was a special session---remembering Dr. Darrel Goll. In addition to all attending NC1131 members, many faculty members and colleagues of Dr. Goll at University of Arizona also attended the session.
The business meeting was held on the next day, chaired by the Administrative Advisor, Dr. Alan Grant. Dr. Grant proposed to form a committee to write the project renewal proposal, which is composed of Drs. Killefer, Riggs and Kuang. Dr. Killefer will take charge of the writing with the assistance from Drs. Riggs and Kuang. The objectives for the renewal were also revised. The new objectives are:
1) Characterize the signal transduction pathways that regulate skeletal muscle growth and metabolism. (TX, IN, NE, AZ, OH, WI, IL, SD, WY, MN, HI, ID)
2) Characterize the cellular and molecular basis of myogenesis. (IN, MN, IL, MI, AZ, SD, OH, WA, NC, WY, FL, ID, HI)
3) Characterize mechanisms of protein assembly and degradation in skeletal muscle. (WI, NE, IN, IL)
Dr.Debora Hamernik, the USDA-CSREES representative also introduced the name changes of USDA-CREES to USDA-National Institute for Food and Agriculture (NIFA), and the funding situation and regulations of USDA.
Next year's annual meeting of the NC-1131 committee will be held at the University of Wyoming, Laramie, Wyoming at a date yet to be determined. Dr. Penny Riggs, Texas A&M University, was elected as secretary for the 2008-09 year with the expectation that the 2010 meeting will be held in College Station, Texas. Following the business, station reports resumed to the noon. The meeting adjourned at noon to allow participants time to return home that day.

Accomplishments

The Arizona Station reported their progress in satellite cell research. Myogenesis is driven by resident stem cells termed satellite cells (SC) whereas angiogenesis arises from endothelial cells and perivascular cells of pre-existing vascular segments and the collateral vasculature. Without proper revascularization of damaged muscle, myogenic cells do not survive and myogenesis ceases. Communication between myogenic and angiogenic cells seems plausible, especially given the number of growth factors produced by SC. To characterize these interactions, they developed an in vitro co-culture model composed of SC and microvascular fragments (MVF). In this system, isolated MVF suspended in collagen gel are cultured over a rat SC monolayer culture. In the presence of SC, MVF exhibit greater indices of angiogenesis than MVF cultured alone. A positive dose-dependent effect of SC conditioned medium (CM) on MVF growth was observed suggesting that SC secrete soluble-acting growth factor(s). Next, they specifically blocked VEGF action in SC CM and this was sufficient to abolish satellite cell-induced angiogenesis. Finally, hypoxia inducible factor-1alpha (HIF-1±), a transcriptional regulator of VEGF gene expression, was found to be expressed in cultured SC and in putative SC in sections of stretch-injured muscle. This data indicates that satellite cell-derived VEGF and HGF play an important role in satellite cell mediated angiogenic processes. Another progress in Arizona Station is to examine the role of environmental influences on skeletal muscle growth, metabolism and physiology. A large proportion of an animal's mass is comprised of skeletal muscle which can have a profound impact on whole-animal energy metabolism and nutrient homeostasis especially during periods of heat stress. They have initiated a series of studies to understand how environmental factors influence the set points of several metabolic pathways within skeletal muscle. Skeletal muscle (semimembranosus) biopsies were obtained from beef cattle during thermal comfort conditions and again after exposure to heat stress conditions. Total RNA was isolated for DNA microarray (GeneChip® Bovine Genome Arrays, Affymetrix, Inc.). Data demonstrated the differential expression of 251 genes based on an adjusted p value of less than 0.005. Interrogation of the data by pathway analysis has revealed dramatic changes in the skeletal muscle transcriptional profile relating to mitochondrial function. It appears that during heat stress bovine skeletal muscle may experience mitochondrial dysfunction leading to impaired cellular energy status. Arizona station also updated their research in calpain system. The calpain system is generally accepted as being responsible for postmortem tenderization of meat. It has been suggested that µ-calpain is responsible for the proteolytic degradation that occurs, however, most of the µ-calpain activity is gone after 3 d of postmortem storage. On the other hand, m-calpain activity can be detected even 14 d postmortem. Both calpastatin and µ-calpain are extensively degraded after 14 d of postmortem storage. In order to better characterize the extent of degradation of these 3 proteins, they have attempted to purify calpains from 12-14 d postmortem bovine semimembranosus. They have identified 5 fractions: 2 fractions of calpastatin activity, CAST I and CAST II, 2 fractions of µ-calpain, and 1 fraction of m-calpain. Purification of m-calpain in postmortem muscle yielded a single fraction with intact 80-kDa and 28-kDa subunits with purity similar to that of at-death purified m-calpain. The specific activity was slightly less (~ 25% lower) than at-death purified m-calpain and total m-calpain protein recovered was much less than for at-death m-calpain. The calcium concentration required for half-maximal activity was the same for both at-death and postmortem m-calpain. The Hawaii station analyzed global gene expression in hypertrophic skeletal muscles induced by clenbuterol and myostatin suppression. In a previous study, they examined the difference in skeletal muscle gene expression between wild type and transgenic mice overexpressing myostatin prodomain (MSTN-pro) using microarray analysis. They observed an overexpression of many myofibrillar protein genes as well as changes in genes involved in various cellular processes were in the transgenic mice. The most significant change in gene expression was the 32-fold overexpression of metallothionein 3 gene in transgenic mice. As a continuation of the previous study, they have examined the global gene expression of hypertrophic muscles induced by beta-adrenergic agionist treatment (clenbuterol) both in wild type and MSTN-pro transgenic mice. Female B6SJL F1 mice were mated to heterozygous MSTN-pro transgenic male mice to produce heterozygous MSTN-pro transgenic mice and wild type (WT) littermate. Pups were weaned at 28 days, then males and females were housed separately and genotype was determined by PCR analysis. At 35 days of age, both MSTN-pro and WT male mice were randomly divided into two groups. The two groups were received 0 ppm or 20 ppm clenbuterol in drinking water for three days, then sacrificed by CO2 asphyxiation, and gastrocnemius, plantaris, soleus, and extensor digitorum longus (EDL) muscles of the lower hind leg were rapidly dissected out, weighed, snap-frozen in liquid nitrogen and stored at -80°C until analysis. Regardless of genotype, clenbuterol significantly increased the weights of the above skeletal muscles. No significant interaction of clenbuterol and genotype effect on skeletal muscle was observed. RNA samples of the gastrocnemius muscle from the clenbuterol-fed WT and clenbuterol-treated MSTN-pro groups were subjected to microarray analysis using the Affymetrix GeneChip Mouse 430-2.0 platform (four chips in each group). Currently, microarray data are being analyzed to identify genes or gene groups differentially expressed by the treatment of beta agonist, clenbuterol and myostatin suppression. The Illinois Station presented their studies in myostatin null mice receiving clenbuterol (clen) treatment. They used clenbuterol mixed in water with 20 ppm clen to male mice for 14 days. Mice were sacrificed at 7 weeks of age for dissection and proximate composition determinations. There was a significant (P<0.05) effect of both clen treatment and genotype but no significant interaction, meaning that wild type and Mstn null mice responded similarly to clen treatment. Body weight, average daily gain, and empty carcass (without skin, head, tail, and viscera) weight were all increased with clen treatment and were greater in Mstn null mice than wild type. Carcass protein percentage was increased with clen treatment and was greater in Mstn null mice, while both visceral and carcass fat percentages were decreased with clen treatment and in Mstn null mice compared with wild type. Furthermore, weights of the retroperitoneal and epididymal fat pads were decreased in Mstn null mice compared with wild type. Epididymal fat pad weight was also decreased by clen treatment. Therefore, they concluded that Mstn null mice do respond to clen treatment and the effects of the Mstn null mutation (increased muscle mass, decreased fat mass) are additive to the effects of clen treatment (increased muscle mass, decreased fat mass). Another project is high fat diet-induced obesity in myostatin null mice. Alterations in myostatin function (Mstn null, transgenic overexpression of Mstn propeptide) result in decreased adiposity and resistance to fat gain. Combining the Mstn null mutation with either the leptin ob/ob mutation or the Agouti yellow mutation reduced obesity and normalized glucose levels. In their study, they fed high (60% calories from fat) or a low (10% calories from fat) diets to wild type and Mstn null mice from 4-16 weeks of age. At 16 weeks of age, were sacrificed and dissected and tissues were saved for further analysis. Body weight, measured weekly, differed by dietary treatment starting in week 1 of the study and by genotype starting in week 2 of the study. At week 6, the interaction of genotype and dietary treatment was trending towards significance (P = 0.15). Blood glucose levels following glucose bolus differed by dietary treatment but not genotype. Genotype and dietary treatment significantly impacted carcass weight, weights of several fat pads and muscles. The Indiana Station studied the regulation of satellite cell function by notch signaling in the skeletal muscle. The group is particularly interested in the signaling pathways that regulate the cell fate choice between self-renewal and differentiation in activated satellite cells. To this end, they have a mouse model to investigate the regulation of satellite cell fate by an evolutionary conserved signaling transduction pathway-the Notch signaling. In this transgenic mouse model, the Notch signaling can be visualized as it exhibits green fluorescence (GFP). The self-renewal and differentiation of satellite cells were dissected using in vitro single myofiber culture and in vivo muscle regeneration models, in which self-renewal and differentiating progenies can be readily identified with specific markers. They discovered an unexpected heterogeneity and dynamics in Notch activation in both quiescent and activated satellite cells. They have also established a strategy to purify satellite cells exhibiting Notch signaling and analyzed their gene expression profiles. Phenotypic heterogeneities have been documented in satellite cells derived from slow and fast muscles. However, the intrinsic molecular mechanisms are unknown due to technical difficulties in isolating fiber type-specific satellite cells. The group has initiated a project to explore the intrinsic molecular mechanisms that program the developmental fate of satellite cells and restrict them to a specific muscle fiber type. They have established unique mouse models that express cyan and red fluorescent proteins in the type I slow and type IIa fast fibers, respectively. These mice provide an unprecedented opportunity to isolate fresh satellite cells from these specific cohorts of fibers and investigate their unique gene expression patterns by high throughput microarray or illumina array analysis. This project will form a foundation for their long-term goal of understanding the molecular regulation of muscle development and growth. Another project is to assess the role of AMPK in metabolism of growing pigs. The purpose of this study was to determine the effect of long-term administration of 5-aminoimidazole-4-carboxamide-1-D-ribofuranoside (AICAR), a known activator of the energy sensor 5'-AMP-activated protein kinase (AMPK), on energy metabolism and myosin heavy chain (MyHC) isoform expression in growing pigs. AICAR treatment caused a significant decrease in mRNA and protein levels of type IIa MyHC isoform and a concomitant increase in type IIx fibers. Consistent with MyHC isoform shift from IIa to IIx, muscles from pigs treated with AICAR showed increased expression and activity of lactate dehydrogenase (LDH), which is an enzyme responsible for anaerobic glycolysis. However, AICAR administration did not alter expression of PPAR³ coactivator (PGC)-1±, fatty acid translocase (FAT/CD36), citrate synthase, or the activity of cytochrome c oxidase (COX). Overall, these results suggest that activation of AMPK by AICAR increases glycolytic capacity by increasing MyHC IIx isoform and increasing LDH activity. The signal transduction cascades that maintain muscle mass remain somewhat obscure but important to animal growth. They have been investigating the extracellular signal-regulated kinase 1/2 (ERK1/2) signaling and have shown that inhibition of this pathway in vitro decreases myotube size and protein content after 3d treatment with a MEK inhibitor. Neither p38 nor JNK inhibitors had any effect on myotube size or morphology. ERK1/2 inhibition also up-regulated gene transcription of atrogin-1 and MuRF-1, and down-regulated the phosphorylation of Akt and its downstream kinases. Forced expression of EGFP-tagged MAPK phosphatase-1 (MKP1) in soleus and gastrocnemius muscles decreased both fiber size and reporter activity. This atrophic effect of MKP1 was time-dependent. Analysis of the reporter activity in vivo revealed that the activities of nuclear factor kappa B (NF-kB) and 26S ribosome were differentially activated in slow and fast muscles, suggesting muscle type-specific mechanisms may be utilized. Together, these findings suggest that MAPK signaling is necessary for the maintenance of skeletal muscle mass as inhibition of these signaling cascades elicits muscle atrophy in vitro and in vivo. Skeletal troponin (Tn) exchange is a good model to use to develop methods to study protein dissociation kinetics from the isolated myofibril. The group showed that troponin's dissociation rate is regulated by calcium and strong (rigor) crossbridges. These different rates fit well with the three-state model (B<->C<->M) of the thin filament for regulation of contraction and are well explained by changes in Tn domain interactions within Tn and between Tn domains and actin-tropomyosin. More recently, they investigated the difference between cardiac and fast skeletal Tn isoforms (in skeletal myofibrils) by measuring the Tn dissociation rate and the pCa-ATPase relationship. They observe three different dissociation rates for both isoforms, but there are large differences in the rates between the two isoforms. In general, the cardiac isoform has a faster dissociation rate under all conditions, is more sensitive but less cooperative in terms of calcium enhanced Tn dissociation rate, and is less in the B or off state in the absence of calcium. The observed differences in the pCa-ATPase activity relationship further support these observations. These studies suggest that three-state equilibrium of the thin filament is dependent upon Tn isoform. Their current studies use ionic strength to alter the equilibrium between the three states. Biochemical studies using reconstituted thin filaments and myosin S1 suggested that low ionic strength, in the absence of free calcium, shifts the equilibrium away from the B or off state and into the C and/or M state. They measured Tn dissociation rate and ATPase activity of myofibrils at different ionic strengths to determine if these conditions influence the three-state equilibrium in a more physiologically intact system. Low ionic strength (25- 50 mM) increases Tn dissociation rate and ATPase activity in the absence of calcium. Also, the ATPase activity is more sensitive and cooperative to activation by calcium at low compared to high ionic strength. Studies to define the molecular mechanism use myofibrils with TnIT exchanged for Tn to give a constitutive B or off state myofibril. Preliminary data suggest that the low ionic strength effects are only partially (30%) mediated by TnI. Addition of TnC to the TnIT myofibrils suggests that TnC is required for the full, low ionic strength effects on the thin filament. Future studies will investigate structural protein dissociation rates to determine if they limit protein turnover rates. The Ohio Station updated their research on the role of the extracellular matrix in avian skeletal muscle development. Current research efforts are focused on understanding the mechanism of how the heparan sulfate family of proteoglycans may be involved in the regulation of muscle growth properties. Fibroblast growth factor 2 (FGF2) is a potent stimulator of muscle cell proliferation and a strong inhibitor of muscle cell differentiation. Heparan sulfate proteoglycans function as a low affinity receptor for FGF2 thus permitting a high affinity interaction of FGF2 with its receptor. Their research is focused on the heparan sulfate proteoglycan syndecan and glypican families. By using a site directed mutagenesis approach the glycosaminoglycan attachment sites were mutated to create a series of site directed mutants for glypican-1 and syndecan-4. For glypican-1, the GAG attachment sites at Ser483, Ser485, and Ser487 were mutated to threonine to obtain 1-chain and no-chain mutants. A similar approach was done for syndecan-4 mutating serine sites 38, 65, and 67. The various constructs of syndecan-4 and glypican-1 were transfected into turkey satellite cells to assay the effect of the GAG chains on the proliferation, differentiation, and responsiveness to FGF2. The data obtained for glypican-1 suggests that glypican-1 function requires the GAG chain attachment sites for myogenic satellite cell FGF2 responsiveness during proliferation and to affect the process of differentiation. In contrast syndecan-4 may affect satellite cell behavior independent of the attached GAG chains and function in a manner independent of FGF2. Also attached to the proteoglycan core protein are N-glycosylation chains. The function of the glycosylated chains has not been well studied to date. To begin to address the function of the N-glycosylation chains a site directed mutagenesis approach was used to create all possible N-glycan chain combinations and a no-chain construct. Preliminary data for both glypican-1 and syndecan-4 suggests that the N-glycan chains do not affect satellite cell proliferation, but differentiation is affected by the absence of the N-glycan chains attached to the core protein. The absence of the N-glycan chains increases differentiation for glypican-1 and in contrast differentiation is decreased by the absence of N-glycan chains for syndecan-4. The second project in Ohio station is the role of transforming growth factor beta1 signaling. Transforming growth factor-beta1 (TGF-beta1) induces apoptosis in many cell types. The cell adhesion receptor, beta1 integrin subunit, prevents apoptosis and may be involved in TGF-beta1-induced muscle cell apoptosis. Chicken primary satellite cells were used to investigate the apoptotic effect of TGF-beta1 on muscle cells. The data showed that the addition of exogenous TGF-beta1 reduced beta1 integrin expression and altered its localization. Treatment of the satellite cells with TGF-beta1 increased the number of apoptotic cells and increased the number of caspase positive cells. Expression of the anti-apoptotic gene Bcl-2 was significantly reduced by TGF-beta1. These data suggest that the apoptotic effect of TGF-beta1 on satellite cells was likely associated with a beta1 integrin-mediated signaling pathway. The Minnesota station studied the roles of IGF-I and the estrogen, androgen and IGF-I receptors in estradiol-17beta and trenbolone acetate- stimulated proliferation of cultured bovine satellite cells. A combined estradiol 17beta (E2)/trenbolone acetate (TBA) implant causes a significant increase in muscle IGF-I mRNA and both E2 and TBA stimulate a significant increase in IGF-I mRNA level in bovine satellite cell (BSC) cultures in media containing 10% fetal bovine serum (FBS). Consequently, increased IGF-I expression may play a role in anabolic steroid enhanced muscle growth. However, even though treatment of cultured BSC with E2 or TBA in media containing 1% IGFBP-3-free swine serum (SS) results in increased proliferation there is no effect on IGF-I mRNA expression, suggesting that increased IGF-I expression may not be responsible for anabolic steroid enhanced BSC proliferation. To further examine the role of estrogen, androgen and IGF-I receptors and their respective ligands in E2 and TBA-stimulated BSC proliferation, the Minnesota group assessed the effects of specific inhibitors on E2 or TBA-stimulated proliferation of BSC. Both ICI 182 780 (an estrogen receptor blocker) and flutamide (an inhibitor of androgen receptor) suppressed (p<0.05) E2 and TBA-stimulated BSC proliferation, respectively. JB1 (a competitive inhibitor of IGF-I binding to type I IGF receptor) reduced (p<0.05) both E2 and TBA-stimulated proliferation in BSC cultures. Both the Raf-1/MAPK kinase (MEK)1/2/ERK1/2, and the phosphatidylinositol 3-kinase (PI3K)/Akt pathways play significant roles in the actions of IGF-I on proliferation and differentiation of myogenic cells. PD98059, an inhibitor of the MAPK pathway, and wortmannin, and inhibitor of the PI3K pathway, both suppressed (p<0.05) E2 and TBA-stimulated proliferation of cultured BSC. Their data suggest that IGF-I plays a role in E2 and TBA stimulated proliferation of cultured BSC even in the absence of increased IGF-I expression. The second project in this station is to study the potential role of G-protein-coupled receptor 30 (GPR30) in estradiol-17beta-stimulated IGF-I mRNA expression in bovine satellite cell cultures. Androgenic and estrogenic steroids enhance muscle growth in animals and humans. Estradiol-17beta (E2) and trenbolone acetate (TBA) (a synthetic testosterone analog increased IGF-I mRNA expression in bovine muscle satellite cell (BSC) cultures. The goal of this study was to evaluate the mechanisms responsible for this increase by evaluating the effects of ICI 182 780 (an E2 receptor antagonist), flutamide (an androgen receptor inhibitor), G1 (a GPR30 agonist), and BSA-conjugated E2 on E2 and/or TBA-stimulated IGF-I mRNA expression in BSC cultures. Flutamide completely suppressed TBA-stimulated IGF-I mRNA expression in BSC cultures. ICI 182 780 did not suppress E2-stimulated IGF-I mRNA expression and 100 nM ICI 182 780 enhanced (93%, p < 0.05) IGF-I mRNA levels in BSC cultures. G1 (100 nM) stimulated IGF-I mRNA expression (100%, p < 0.05) but had no effect on proliferation in BSC cultures. E2-BSA, which cannot cross the cell membrane, stimulated IGF-I mRNA expression (approximately 100%, p < 0.05) in BSC but even at extremely high concentrations had no effect on proliferation. In summary, their data indicate the E2-stimulation of proliferation and E2-stimulation of IGF-I mRNA expression in BSC cultures occur via different mechanisms. Stimulation by ICI 182 780, G1 and E2-BSA suggests the E2-stimulated IGF-I mRNA expression in BSC cultures is mediated through the GPR30 receptor. The third project is to examine the effects of trenbolone acetate (TBA), estradiol (E2) and combined TBA/E2 implants on muscle IGF-I, IGF-I receptor, estrogen receptor-± and androgen receptor mRNA levels in feedlot steers. They have previously shown that a combined trenbolone acetate (TBA)/ estradiol-17beta (E2) implant significantly increases IGF-I mRNA levels in longissimus dorsi (LD) muscles of feedlot steers by 28 days after implantation. Here they compare the effects of E2 (25.7 mg), TBA (120 mg) and combined /TBA (120 mg)/ E2 (24 mg) implants on IGF-I, IGF-I receptor (IGFR-1), estrogen receptor (ER)-± and androgen receptor (AR) mRNA levels in the LD muscles of steers implanted for 28 days. Five yearling steers per group were implanted with each implant and 5 control steers received no implant. Steers were weighed weekly starting on d 0 and muscle biopsy samples were taken from each steer on d 0 (prior to implantation), d 7, d 14 and d 28. RNA was prepared from each sample and real-time RT-PCR was used to determine the levels of IGF-I, IGFR-1, ER-± and AR mRNA. Body weight of implanted steers tended (P = 0.09) to be greater than that of CTL steers. On d 7 and 28 IGF-I mRNA levels were higher (58% and 78%, respectively) (p < 0.009) in E2 implanted animals than in control steers. Similarly, on d 28 the LD muscle IGF-I mRNA level was 65% higher (P = 0.017) in TBA/E2 implanted steers than in control animals. In contrast, the TBA implant did not increase LD muscle IGF-I mRNA levels after 28 days of implantation. These data suggest that E2 is responsible for the increased muscle IGF-I mRNA level observed in steers implanted with a combined TBA/E2 implant. The Texas Station utilizes a unique cattle population for investigation of differential gene expression and signal transduction in skeletal muscle resulting from inheritance of Bos taurus or Bos indicus alleles. This project uses microarray, quantitative realtime RT-PCR, and proteomic analyses of skeletal muscle from steers to characterize the Brahman influence on carcass traits and meat characteristics. In addition, expression profiles will be correlated to extensive phenotype, SNP and QTL data from this population of animals. Genetic mechanisms influencing these complex traits remain poorly understood. One objective of the McGregor Genomics Project is to identify potentially valuable QTL for use in breeding programs for a variety of these traits. Approximately 180 F2 Nellore-Angus steers were assessed for feed efficiency as determined by computation of model predicted residual consumption (MPRC). Animals with the greatest positive or smallest negative MPRC values were identified as least efficient or most efficient, respectively. The Texas group extracted RNA from skeletal muscle from the 14 most efficient and 14 least efficient animals for microarray analysis. They used data generated from Agilent bovine oligo microarrays to identify candidate genes for further study. Among differentially expressed genes verified between the two groups, ±-actinin 3 (ACTN3), was expressed nearly 3-fold higher in the inefficient group when compared to the efficient group. ACTN3 is expressed only in fast twitch muscle fibers. Actinins are myofilament proteins essential to Z-line attachment for actin fibers, and have been shown to bind factors relating to myofiber differentiation as well as muscle contraction. The Washington station characterized selected signal transduction pathways that regulate skeletal muscle growth and differentiation. Skeletal muscle is composed of a variety of cells, including adipocytes. For a considerable number of years the Washington station have been interested in the mechanism of intercellular communication between muscle cells and intramuscular adipocytes. During an attempt to develop a defined co-culture system, it was obvious that 3T3-L1 cells and stromal vascular cells were not sufficiently defined to use as the adipocyte cell component of the defined co-culture system. As such, they looked for an alternative adipocyte, which could be used in our developing system. The group devised repeatable methods to isolate mature adipocytes from beef cattle and to generate progeny cultures of adipofibroblasts for use in a variety of studies. Whereas beef-derived (mature) adipocytes retained lipid and divided in an asymmetric or symmetric manner, similar cells from pigs had to physically extrude lipid from the cell prior to proliferation. Another project is to determine molecular mechanisms that control gene expression in skeletal muscle. The group has previously shown that mature lipid-filled beef-derived adipocytes possess the ability to return to a proliferative-competent state and produce progeny cells. Such progeny cells have been tested for numerous properties, and compared to 3T3-L1 and stromal vascular cells. Bovine-specific oligo microarrays and qRT-PCR were used to determine differentially expressed genes in purified progeny cultures of dedifferentiated beef-derived (mature) adipocytes and to validate selected genes considered closely associated with adipogenesis. The same methods were used to compare differentially expressed genes in subcutaneous adipose tissues of beef steers with different backfat thickness. A variety of intrinsic factors were different between proliferative vs redifferentiative adipofibroblasts, and between individuals of the same breed (developmental study) and between two cattle crossbreds (direct comparison study). The Wisconsin Station characterized a mutation that affects alternative splicing of titin. An autosomal dominant mutation that dramatically alters the alternative splicing pattern of titin has been described (Greaser et al., J. Mus. Res. & Cell Motil 26:325-332, 2005). In spite of the dramatic change in titin size, the animals remain visibly healthy. Electron micrographs of homozygous mutant ventricles showed occasional regions of myofibrillar disarray. The mutants also contained unusual clustering of mitochondria and often had very wide myofibrils. Changes in cardiac muscle transcriptional levels from mutant compared to normal rat ventricular were determined using Affymetrix Rat 230 2.0 microarrays. Results showed that 433 genes (from a total of 31099) were differentially expressed in mutant compared to normal rats. 239 genes were down-regulated and 194 genes were differentially up-regulated. Genes that exhibited the largest increase in expression were sarcomeric proteins and regulation of muscle contraction, G-protein signaling and calcium regulation in cardiac cells. The other project is to study the role of phosphorylation in myosin binding protein C function. Normal cardiac function requires dynamic modulation of contraction. Beta1-adrenergic-induced protein kinase A (PKA) phosphorylation of cardiac myosin binding protein (cMyBP)-C may regulate crossbridge kinetics to modulate contraction. The group tested this idea with mechanical measurements and echocardiography in a mouse model lacking 3 PKA sites on cMyBP-C, ie, cMyBP-C(t3SA). They developed the model by transgenic expression of mutant cMyBP-C with Ser-to-Ala mutations on the cMyBP-C knockout background. Western blots, immunofluorescence, and in vitro phosphorylation combined to show that non-PKA-phosphorylatable cMyBP-C expressed at 74% compared to normal wild-type (WT) and was correctly positioned in the sarcomeres. Similar expression of WT cMyBP-C at 72% served as control, ie, cMyBP-C(tWT). Skinned myocardium responded to stretch with an immediate increase in force, followed by a transient relaxation of force and finally a delayed development of force, ie, stretch activation. The rate constants of relaxation, k(rel) (s-1), and delayed force development, k(df) (s-1), in the stretch activation response are indicators of crossbridge cycling kinetics. cMyBP-C(t3SA) myocardium had baseline k(rel) and k(df) similar to WT myocardium, but, unlike WT, k(rel) and k(df) were not accelerated by PKA treatment. Reduced dobutamine augmentation of systolic function in cMyBP-C(t3SA) hearts during echocardiography corroborated the stretch activation findings. Furthermore, cMyBP-C(t3SA) hearts exhibited basal echocardiographic findings of systolic dysfunction, diastolic dysfunction, and hypertrophy. Conversely, cMyBP-C(tWT) hearts performed similar to WT. Thus, PKA phosphorylation of cMyBP-C accelerates crossbridge kinetics and loss of this regulation leads to cardiac dysfunction. The Wyoming Station continues their work on AMPK and skeletal muscle growth and growth. The group studied the role of AMPK in the regulation of skeletal muscle development. They found that AMPK controls the skeletal muscle development through sensitizing the insulin/insulin-like growth factor-1 signaling. In C2C12 myoblast cell culture, they also demonstrated that Ca2+/calmodulin-dependent protein kinase kinase is involved in the activation of AMPK, linking calcium signaling, AMPK and skeletal muscle growth. Currently, they are further investigating the role of AMPK in skeletal muscle growth by employing RN- pigs which carries a mutation in muscle-specific AMPK g3 subunit. They are also investigating the role of AMPK in muscle growth and development using a transgenic mice which carry a R225Q mutation in AMPKg3 subunit, corresponding to the mutation in RN- pigs. In addition, the group is investigating the role of AMPK in fetal muscle development. Since meat animals spend one third to half of their lives in utero, muscle development during fetal stage is essential for growth performance of offspring. Therefore, studies on the association between maternal nutrition and fetal skeletal muscle development are very important. Another project is to define the role of AMPK in the marbling of beef cattle. AMPK has a key role in the regulation of marbling. AMPK activity in skeletal muscle is negatively associated with marbling in beef cattle. Data suggested that nutrition during fetal stage is closely associated with marbling in beef cattle and lamb. The group showed that nutrient supplementation during gestation in the dam enhanced marbling in fetal muscle. They are currently studying the myogenesis and adipogenesis from mesenchymal stem cells. Their studies show that AMPK is involved in muscle growth, postmortem glycolysis and marbling. It is known that selection of animals for enhanced muscle growth increases incidence of PSE meat, and also reduces marbling in livestock. But the underlying mechanisms remain undefined. Their studies suggest that AMPK participates in all these three aspects providing a possibly explanation for such negative association between muscle growth and meat quality.

Publications

Allen, D. L., and M. Du. 2008. Comparative functional analysis of the cow and mouse myostatin genes reveals novel regulatory elements in their upstream promoter regions. Comparative Biochemistry and Physiology, 150: 432-439. Bobbili, N.K., Y.S. Kim, M.A. Dunn, J, Yang and A.Ong. 2008. Effects of maternal immunization against myostatin on postnatal growth and skeletal muscle mass of offspring in mice. Food and Agricultural Immunology 19:93-106. Chen, J., M. Guridi, M.E. Fernyhough, Z. Jiang, L.L. Guan, E. Okine, G,J, Hausman and M.V. Dodson. (submitted). Lipid extrusion prior to pig-derived mature adipocyte dedifferentiation. Histochemistry and Cell Biology Chen, J., M. Guridi, M.E. Fernyhough, Z. Jiang, L.L. Guan, E. Okine, G,J, Hausman and M.V. Dodson. (submitted). The process of adipogenesis needs to include mature adipocyte dedifferentiation. Biochemistry and Cell Biology Chester-Jones, H., and S.G. Velleman. 2008. Growth and development symposium: Transcriptional factors and cell mechanisms for regulation of growth and development with application to animal agriculture. J. Anim. Sci. 86:E205-206E. Collier, R.J., J.L. Collier, R.P. Rhoads, and L.H. Baumgard. 2008. Genes involved in the bovine heat stress response. J. Dairy Sci. 91(2):445-54. Dayton, W. R., and M. E. White. 2008. Cellular and molecular regulation of muscle growth and development in meat animals. J. Anim. Sci. 86(14 Suppl):E217-25. Dodson, M.V. 2008. Research paper citation record keeping: It is not for wimps. Journal of Animal Science 86:2795-2796 Dodson, M.V. and M.E. Fernyhough. 2008. Mature adipocytes: Are there still novel things that we can learn from them? Tissue & Cell 40:307-308 Dodson, M.V., A. Kinkel, J.L. Vierck, K. Cain, M. Wick, and J. Ottobre. 2008. Undefined cells reside in fish skeletal muscle. Cytotechnology 56:171-178 Dodson, M.V., Z. Jiang, J. Chen, G.J. Hausman, L.L. Guan, J. Novakofski, D. Thompson, C. Lorenzen and M.E. Fernyhough. (submitted). Thinking outside the beef cow or pig: Applying cell/molecular biology observations with adipocytes to the end-point of altering red meat quality. Meat Science Fernandez-Duenas, D.M, A.J. Myers, S.M. Scramlin, C.W. Parks, S.N. Carr, J. Killefer, and F.K. McKeith. 2008. Carcass, meat quality, and sensory characteristics in heavy weight pigs fed ractopamine (Paylean). J. Anim. Science. (Sep. 2 E-Pub) Fernyhough, M.E., G.J. Hausman and M.V. Dodson. 2008. Progeny from dedifferentiated adipocytes display protracted adipogenesis. Cells, Tissues, Organs 188:359-372 Fernyhough, M.E., G.J. Hausman, L.L. Guan, E. Okine, S.S. Moore and M.V. Dodson. 2008. Mature adipocytes may be a source of stem cells for tissue engineering. Biochemical Biophysical Research Communications 368(3):455-457 Forhead, A.J., C. A. Lamb, K. L. Franko, D. M. O'Connor, F. B. P. Wooding, R. L. Cripps, S. Ozanne, D. Blache, Q. W Shen, M. Du, and A. L. Fowden. 2008. Role of leptin in the regulation of growth and carbohydrate metabolism in the ovine fetus during late gestation. Journal of Physiology, 586: 2393-2403. Goll, D.E., G. Neti, S.W. Mares, and V.F. Thompson. 2008. Myofibrillar protein turnover: the proteasome and the calpains. J. Anim. Sci: 86: E19-E35. Greaser, M.L., and D.R. Swartz. 2008. High efficiency blotting of high-molecular weight proteins. In Methods in Molecular Biology, 3rd Ed., J. M. Walker, ed., Humana Press (in press). Greaser, M.L., C. M. Warren, K. Esbona, W. Guo,Y. Duan, A. M. Parrish, P. R. Krzesinski, H. S. Norman, S. Dunning, D. P. Fitzsimons, and R. L. Moss. 2008. Mutation that dramatically alters rat titin isoform expression and cardiomyocyte passive tension. J. Molec. Cellul. Cardiol. 44:982-991. Gunn, P.J., A.D. Weaver, R.P. Lemenager, D.E. Gerrard, M.C. Claeys and S.L. Lake. Effects of dietary fat and crude protein on feedlot performance, carcass characteristics, circulating plasma metabolites, and meat quality in steers fed differing levels of distiller's dried grains with solubles. J. Anim. Sci (submitted). Han, B. , Junfeng Tong, C. Ma, M. J. Zhu, and M. Du. 2008. Insulin-like growth factor-1 (IGF-1) and leucine stimulate mammalian target of rapamycin (mTOR) signaling in pig myogenic satellite cells. Molecular Reproduction and Development, 75: 810-817. Hausman, G.J., M.V. Dodson, K. Ajuwon, M. Azain, K. Barnes, L.L. Guan, Z. Jiang, S. Poulos, R.D. Sainz, S. Smith, M. Spurlock, J. Novakofski, M.E. Fernyhough, and W.G. Bergen. 2008. Board Invited/Sponsored Review: Domestic animal carcass composition: The biology and regulation of preadipocytes and adipocytes. Journal of Animal Science [*participated equally] doi: 10.2527 Holmer, S.F., J. W. Homm, L. L. Berger, M. S. Brewer, F.K. McKeith, and J. Killefer. 2008. Realimentation of cull beef cows. I. Live performance, carcass traits, and muscle characteristics. J. Muscle Foods. (In Press) Ibrahim, R.M., D. E. Goll, J. A. Marchello, G. C. Duff, V. F. Thompson, S. W. Mares, and H. A. Ahmad. 2008. Effect of two dietary concentrate levels on tenderness, calpain and calpastatin activities, and carcass merit in Waguli and Brahman steers. J Anim Sci. 86(6):1426-33. Iglay, H.B., J.W. Apolzan, D.E. Gerrard, J.K. Eash, J.C. Anderson and W.W. Campbell. 2008. Moderately increased protein intake predominately from egg sources does not influence whole body, regional, or muscle composition responses to resistance training in older people. The Journal of Nutrition, Health & Aging. (In press). Kamanga-Sollo, E., M. E. White, K. Y. Chung, B. J. Johnson, and W. R. Dayton. 2008. Potential role of G-protein-coupled receptor 30 (GPR30) in estradiol-17beta- stimulated IGF-I mRNA expression in bovine satellite cell cultures. Domestic Anim. Endocrinol. 35:254-262. Kamanga-Sollo, E., M. E. White, M. R. Hathaway, K. Y. Chung, B. J. Johnson, and W. R. Dayton. 2008. Roles of IGF-I and the estrogen, androgen and IGF-I receptors in estradiol-17beta and trenbolone acetate- stimulated proliferation of cultured bovine satellite cells. Domestic Anim. Endocrinol. 35:88-97. Kokta, T.A., A.L. Strat, M.R. Papasani, J. Szasz, M.V. Dodson and R.A. Hill. 2008. Regulation of lipid accumulation in 3T3-L1 cells: Insulin-independent and combined effects of fatty acids and insulin. Animal 2(1):92-99 Kuang S, Gillespie M, Rudnicki MA. 2008. Niche regulation of muscle satellite cell self-renewal and differentiation. Cell Stem Cell 2: 22-31. Kuang S, Rudnicki MA. 2008. Emerging biology of satellite cells and their therapeutic potentials. Trends Mol Med 14: 82-91. Lee, S.B., Y.S. Kim, M. Yoon, S.K. Kim, I.W. Jang, H.J. Lim and H.J. Jin. 2007. Characterization and expression pattern of the partial myostatin cDNA in shrimp, Fenneropenaeus Chinensis. Journal of Marine Bioscience and Biotechnology 2:224-229. Li, X., and S.G. Velleman. 2008 Effect of transforming growth factor-beta1 on decorin expression and muscle morphology during chicken embryonic and posthatch growth and development. Poult. Sci. (In press). Li, X., D.C. McFarland, and S. G. Velleman. 2008. Effect of smad3-mediated transforming growth factor-beta1 signaling on satellite cell proliferation and differentiation in chickens. Poult. Sci. 87:1823-1833. Li, X., D.C. McFarland, and S.G. Velleman. 2008. Extracellular matrix proteoglycan decorin-mediated myogenic satellite cell responsiveness to transforming growth factor-beta during satellite cell proliferation and differentiation. Dom. Anim. Endocrinol. 35:263-273. Li, X., D.C. McFarland, and S.G.Velleman. 2008.Transforming Growth Factor-beta1 Induces Satellite Cell Apoptosis by beta1 Integrin-Mediated Focal Adhesion Kinase Activation. (Submitted). Mir, P.S., K. Schwartzhoph-Genswein, E. Okine and M.V. Dodson. 2008. Effect of a short duration feed withdrawal followed by full feeding on marbling fat in beef carcasses. Livestock Science 116:22-29 Neti, G., S. M. Novak, V. F. Thompson, and D. E. Goll. 2009. Properties of easily releasable myofilaments (ERMs): are ERMs the first step in myofibrillar protein turnover? J. Physiol. (Manuscript in preparation). Novak, S. W., J. P. Camou, V. F. Thompson, R. Vazquez, J. A. Marchello, and D. E. Goll. 2009. Isolation and characterization of µ-calpain, m-calpain, and calpastatin from postmortem bovine muscle. ii. Purification of m-calpain and characterization of calpastatin. J. Anim. Sci. (Manuscript in preparation). Pampusch MS, White ME, Hathaway MR, Baxa TJ, Chung KY, Parr SL, Johnson BJ, Weber WJ, Dayton WR.. 2008. Effects of implants of trenbolone acetate, estradiol, or both, on muscle IGF-I, IGF-I receptor, estrogen receptor-{alpha} and androgen receptor mRNA levels in feedlot steers. J Anim Sci. doi:10.2527/jas.2008-1085 [Epub ahead of print]. PMID: 18676717 (in press). Park, S., T.L. Scheffler, A.M. Gunawan, H. Shi, C. Zeng, K.M. Hannon, A.L. Grant and D.E. Gerrard. 2008. Disruption of calcium homeostasis blocks AMPK-induced GLUT4 expression in skeletal muscle. Amer. J. Physiol. (In press). Park, S.K, A. M. Gunawan, T. L. Scheffler, A. L. Grant and D. E. Gerrard. Myosin heavy chain isoform content and energy metabolism can be uncoupled in pig skeletal muscle J. Anim. Sci (In press). Park, S.K., T. L. Sheffler, M. E. Spurlock, A. L. Grant and D. E. Gerrard Chronic activation of 5'-AMP-activated protein kinase changes myosin heavy chain expression in growing pigs J. Anim. Sci (submitted). Pearson, D.S., D.R. Swartz and M.A. Geeves. 2008. Fast pressure jumps can perturb calcium and magnesium binding to troponin C F29W. Biochemistry (10.1021/bi801150w, in press). Qu, A., R.P. Rhoads, and C.H. Stahl. 2009. Cholecalciferol affects the differentiation and proliferation of satellite cells isolated from young pigs. (Manuscript in preparation). Rhoads, R., M.E. Fernyhough, S. Velleman, D.C. McFarland, X. Liu, G.J. Hausman and M.V. Dodson. Invited Review: Extrinsic regulation of domestic animal-derived myogenic satellite cells II. Domestic Animal Endocrinology [*participated equally] (submitted). Rhoads, R.P., R.M. Johnson, C.R. Rathbone, X. Liu, C. Temm-Grove, S.M. Sheehan, J.B. Hoying and R.E. Allen. 2008. Satellite cell mediated angiogenesis coincides with a functional hypoxia-inducible factor (HIF) pathway. (in review). Riggs, P. K. 2008. Functional genomics and proteomics of cattle. Beef Cattle Research in Texas. (submitted) Riggs, P.K., and C.A. Gill. 2008. Molecular mapping and marker assisted breeding for meat quality. In Applied Muscle Biology and Meat Science, Du M, McCormick RJ, eds. CRC Press (submitted). Ritter, M.J., M. Ellis, D.B. Anderson, S.E. Curtis, K.K. Keffaber, J. Killefer, F.K. McKeith, C.M. Murphy, and B.A. Peterson. 2008. Effects of multiple concurrent stressors on rectal temperature, blood acid-base status, and longissimus muscle glycolytic potential in market weight pigs. J. Animal Science (Aug.1, E-Pub) Seale P, Bjork B, Yang W, Kajimura S, Chin S, Kuang S, Scime A, Devarakonda S, Conroe H, Erdjument-Bromage H, Tempst P, Rudnicki MA, Beier DR, Spiegelman BM. 2008. PRDM16 Controls a Brown Fat/Skeletal Muscle Switch. Nature, 454:961-7. Shen, Q. W. D. E. Gerrard, and M. Du. 2008. Compound C, an inhibitor of AMP-activated protein kinase, inhibits glycolysis in mouse longissimus dorsi postmortem. Meat Science, 78: 323-330. Shen, Q.W., D.E. Gerrard and M. Du. 2008. Compound C, an inhibitor of AMP-activated protein kinase, inhibits glycolysis in mouse Longissimus Dorsi postmortem. Meat Sci. 78(3) p. 323-330. Shi, H., J.M. Pleitner, J.M. Scheffler, C. Zeng K.M. Hannon, A.L. Grant and D.E. Gerrard. 2008. Modulation of skeletal muscle fiber type by mitogen-activated protein kinase signaling. FASEB J. 22(8):2990-3000. Shi, H., J.M. Pleitner, J.M. Scheffler, C. Zeng K.M. Hannon, A.L. Grant and D.E. Gerrard. Mitogen-activated protein kinase signaling is necessary for the maintenance of muscle mass. FASEB Journal (In press) Taniguchi, M., L. Guan, J. Basarab, M.V. Dodson and S.S. Moore. 2008. Comparative analysis of gene expression profiles in subcutaneous fat tissues of beef cattle. Comparative Biochemistry and Physiology (Part D; Genomics and Proteomics) 3(4):3:251-256 Taniguchi, M., L.L. Guan, B. Zhang, M.V. Dodson, E. Okine and S.S. Moore. 2008. Gene expression patterns of bovine perimuscular adipocytes during adipogenesis. Biochemical Biophysical Research Communications 366:346-351 Taniguchi, M., L.L. Guan, B. Zhang, M.V. Dodson, E. Okine and S.S. Moore. 2008. Adipogenesis of bovine perimuscular adipocytes. Biochemical Biophysical Research Communications 366:54-59 Tong, C.W., J. E. Stelzer, M. L. Greaser, P.A. Powers, and R. L. Moss. 2008. Acceleration of crossbridge kinetics by protein kinase A phosphorylation of cardiac myosin binding protein C modulates cardiac function. Circ. Res 103:974-82. Tong, J., M. J. Zhu, K. R. Underwood, B. W. Hess, S. P. Ford, and M. Du. 2008. AMP-activated protein kinase negatively regulates adipogenesis in sheep fetal skeletal muscle and 3T3 cells. Journal of Animal Science, 86: 1296-1305. Underwood K. R. , W. J. Means, M. J. Zhu, S. P. Ford, B. W. Hess, and M. Du. 2008. AMP-activated protein kinase is negatively associated with intramuscular fat content in longissimus dorsi muscle of beef cattle. Meat Science, 79: 394-402. Underwood K.R. , W.J. Means, and M. Du. 2008. Caspase 3 is not involved in the postmortem tenderization of beef. Journal of Animal Science, 86: 960-966. Vaughn, RN, Kochan KJ, Amen TS, Abbey CA, Gill CA, Sanders JO, Herring AD, Lunt DK, Sawyer JE, Riggs PK. 2009. Association of alpha-actinin 3 gene expression with bovine feed efficiency. 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Impact Statements

Significant progress has been made in understanding the role of satellite cells in muscle growth and development.
Cell signaling pathways regulating skeletal muscle growth and development was further defined.
Our knowledge on the role of extracellular matrix in regulation of muscle growth has been enhanced.
The association between myofibrillar protein structure and function was further studied.
AMP-activated protein kinase has been proposed to have important roles in regulating muscle growth and meat quality.

Date of Annual Report: 04/15/2010

Report Information

Annual Meeting Dates: 10/23/2009 - 10/24/2009
Period the Report Covers: 10/01/2008 - 09/01/2009

Participants

Brief Summary of Minutes

Minutes Attachment:

Attachment

Accomplishments

Publications

Impact Statements

Date of Annual Report: 01/03/2010

Report Information

Annual Meeting Dates: 11/12/2010 - 11/13/2010
Period the Report Covers: 10/01/2009 - 09/01/2010