Brief Summary of Minutes of Annual Meeting

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 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.

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