Effects of dietary vitamin B6 on the skeletal muscle protein metabolism of growing rabbits
G. Y. Liu A , Z. Y. Wu A , Y. L. Zhu A , L. Liu A and F. C. Li A B
+ Author Affiliations
- Author Affiliations
A College of Animal Science and Technology, Shandong Agricultural University, Tai’an 271018, P. R. China.
B Corresponding author. Email: chlf@sdau.edu.cn
Animal Production Science 57(10) 2007-2015 https://doi.org/10.1071/AN15807
Submitted: 13 November 2015 Accepted: 15 July 2016 Published: 26 September 2016
Abstract
This study aimed to evaluate the effects of dietary vitamin B6 on the skeletal muscle protein metabolism and expression of transcription and growth factor of growing rabbits. Two hundred, healthy, rabbits with similar bodyweights were randomly assigned to one of five dietary groups with 40 animals per group. The dietary groups consisted of the following different vitamin B6 supplementation levels: 0, 5, 10, 20 and 40 mg/kg. The feeding trial lasted 60 days. The results showed that dietary vitamin B6 elicited significant effects on the fore and hind leg muscle ratio (the fore and hind leg muscle weight/the liveweight; P < 0.05) and on serum total amino acids (T-AA), blood urea and insulin-like growth factor 1 (IGF1) content (P < 0.05). Additionally, expression of IGF1, myogenic determination factor (MYOD) and myogenin (MYOG), myocyte regulation factor 5 (MYF5), myostatin (MSTN) and WW domain-containing E3 proteasome ubiquitin ligase 1 (WWP1) mRNA in the loin (M. longissimus dorsi) were affected by vitamin B6 in diets (P < 0.05). The immunoblot analysis revealed that dietary vitamin B6 elicited significant effects on IGF1, MYOG and WWP1 expression in the loin (P < 0.05). Our results indicate that the addition of dietary vitamin B6 can significantly alter the protein metabolism of growing rabbits and that an appropriate vitamin B6 supplementation level is 20 mg/kg for 3–5-month-old growing rabbits (the basic diet vitamin B6 content was 4.51 mg/kg).
Additional keywords: serum constituents, slaughter performance.
References
Albektsen S, Waabgo R, Sandes K (1998) Tissue vitamin B6 concentration and aspartate aminotransferase activity in Atlantic salmon (Salmo salar) fed graded dietary levels of vitamin B6. Fik Dir Skr Ser Ernaring 6, 21–34.AOAC International (1995) ‘Official methods of analyses.’ 16th edn. (Association of Official Analytical Chemists: Arlington, VA)
AOAC International (2000) ‘Official methods of analyses.’ 17th edn. (Association of Official Analytical Chemists: Washington, DC)
AOAC International (2005) ‘Official methods of analyses.’ 18th edn. (Association of Official Analytical Chemists: Rockville, MD)
Bailey P, Tamara H, Andrew BL (2001) The origin of skeletal muscle stem cells in the embryo and the adult. Current Opinion in Cell Biology 13, 679–689.
| The origin of skeletal muscle stem cells in the embryo and the adult.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3MXotFWhsbY%3D&md5=154e8647442deabc2ffab05c8f768fb6CAS | 11698183PubMed |
Blasco A, Ouhayoun J (1996) Harmonization of criteria and terminology in rabbit meat research. World Rabbit Science 4, 93–99.
Brameld JM (1997) Molecular mechanisms involved in the nutritional and hormonal regulation of growth in pigs. The Proceedings of the Nutrition Society 56, 607–619.
| Molecular mechanisms involved in the nutritional and hormonal regulation of growth in pigs.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK2sXlsVCjt7s%3D&md5=8a1cb52879f367f14654b0246d2c4cc8CAS | 9264111PubMed |
Breier BH (1999) Regulation of protein and energy metabolism by the somatotropic axis. Domestic Animal Endocrinology 17, 209–218.
| Regulation of protein and energy metabolism by the somatotropic axis.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK1MXmsVWmtrY%3D&md5=2da8b693200b66cddc46b61a920d6cc1CAS | 10527124PubMed |
Buonomo FC, Baile CA (1990) The neurophysiological regulation of growth hormone secretion. Domestic Animal Endocrinology 7, 435–450.
| The neurophysiological regulation of growth hormone secretion.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK3MXktVSqsro%3D&md5=2718d46ef31eddcdf596e9650b2b3faeCAS | 1979764PubMed |
Buonomo FC, Baile CA (1991) Influence of nutritional deprivation on insulin-like growth factor I, somatotropin, and metabolic hormones in swine. Journal of Animal Science 69, 755–760.
Chinese Academy of Agricultural Sciences (2009) Tables of feed composition and nutritive values in China. 20th edn, Institute of Animal Science of CAAS. (Chinese Academy of Agricultural Sciences)
Clayton PT (2006) B6 responsive disorders: a model of vitamin dependency. Journal of Inherited Metabolic Disease 29, 317–326.
| B6 responsive disorders: a model of vitamin dependency.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD28XlsV2ltb0%3D&md5=2af33e4030174e1b96af85dbace7cde4CAS | 16763894PubMed |
Cobos A, de la Hoz L, Cambero MI, Ordonez JA (1995) Sugar-beet pulp as an alternative ingredient of barley in rabbit diets and its effect on rabbit meat. Meat Science 39, 113–121.
| Sugar-beet pulp as an alternative ingredient of barley in rabbit diets and its effect on rabbit meat.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK2MXit1Wiurw%3D&md5=13cb7a6292de8da6a6dece0b5beb36a0CAS | 22059768PubMed |
Coma J, Carrion D, Zimmerman DR (1995) Use of plasma urea nitrogen as a rapid response criterion to determine the lysine requirement of pigs. Journal of Animal Science 73, 472–481.
Coma J, Zimmerman DR, Carrion D (1996) Lysine requirement of the lactating sow determined by using plasma urea nitrogen as a rapid response criterion. Journal of Animal Science 74, 1056–1062.
Costelli P, Muscaritoli M, Bossola M, Moore-Carrasco R, Crepaldi S, Grieco G, Autelli R, Bonelli G, Pacelli F, Lopez-Soriano FJ, Argilés JM, Doglietto GB, Baccino FM, Rossi Fanelli F (2005) Skeletal muscle wasting in tumor-bearing rats is associated with MyoD down-regulation. International Journal of Oncology 26, 1663–1668.
Costelli P, Muscaritoli M, Bossola M, Penna F, Reffo P, Bonetto A, Busquets S, Bonelli G, Lopez-Soriano FJ, Doglietto GB, Baccino FM, Rossi Fanelli F (2006) IGF-I is downregulated in experimental cancer cachexia. American Journal of Physiology, Regulatory, Integrative and Comparative Physiology 291, R674–R683.
| IGF-I is downregulated in experimental cancer cachexia.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD28XhtVSks7zF&md5=569940dafd23abf28e8fc293723719edCAS | 16614058PubMed |
Dalle Zotte A, Szendrõ Z (2011) The role of rabbit meat as functional food. Meat Science 88, 319–331.
| The role of rabbit meat as functional food.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3MXjvVejsro%3D&md5=d4e865eced578454ab3c9526330b58d8CAS | 21392894PubMed |
Dasarathy S, Muc S, Hisamuddin K, Edmison JM, Dodig M, McCullough AJ, Kalhan SC (2007) Altered expression of genes regulating skeletal muscle mass in the portacaval anastomosis rat. American Journal of Physiology. Gastrointestinal and Liver Physiology 292, G1105–G1113.
| Altered expression of genes regulating skeletal muscle mass in the portacaval anastomosis rat.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2sXks1Kjtrc%3D&md5=12bebcc65f4dee5526c80e09fcf3f8edCAS | 17185634PubMed |
Duclos MJ (2005) Insulin-like growth factor-I (IGF-I) mRNA levels and chicken muscle growth. Journal of Physiology and Pharmacology 56, 25–35.
Florini JR, Ewton DZ, Coolican SA (1996) Growth hormone and the insulin-like growth factor system in myogenesis. Endocrine Reviews 17, 481–517.
Gilson H, Schakman O, Combaret L, Lause P, Grobet L, Attaix D, Ketelslegers JM, Thissen JP (2007) Myostatin gene deletion prevents glucocorticoid-induced muscle atrophy. Endocrinology 148, 452–460.
| Myostatin gene deletion prevents glucocorticoid-induced muscle atrophy.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2sXjsFShtw%3D%3D&md5=14ca6dce5f70b2110679b1952ce69ef2CAS | 17038559PubMed |
Giri NA, Teshima SI, Kanazawa A, Ishikawa M (1997) Effects of dietary pyridoxine and protein levels on growth, vitamin B6 content and free amino acid profile of juvenile, Penaeus japonicus. Aquaculture 157, 263–275.
| Effects of dietary pyridoxine and protein levels on growth, vitamin B6 content and free amino acid profile of juvenile, Penaeus japonicus.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK2sXns1Wmt70%3D&md5=f84896b4870b04c8929247af92737affCAS |
Glass DJ (2003) Signalling pathways that mediate skeletal muscle hypertrophy and atrophy. Nature Cell Biology 5, 87–90.
| Signalling pathways that mediate skeletal muscle hypertrophy and atrophy.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3sXot12rtw%3D%3D&md5=16ad6fb86b2dd3ae898d1df9983845edCAS | 12563267PubMed |
Glass DJ (2005) Skeletal muscle hypertrophy and atrophy signaling pathways. The International Journal of Biochemistry & Cell Biology 37, 1974–1984.
| Skeletal muscle hypertrophy and atrophy signaling pathways.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2MXpsVWmsrY%3D&md5=64ba6bb9af58bc7f822db9d3aa23c7ceCAS |
Kambadur R, Sharma M, Smith TP, Bass JJ (1997) Mutations in myostatin (GDF8) in double-muscled Belgian Blue and Piedmontese cattle. Genome Research 7, 910–916.
Karppanen H, Mervaala E (2006) Sodium intake and hypertension. Progress in Cardiovascular Diseases 49, 59–75.
| Sodium intake and hypertension.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD28Xht1emtLbJ&md5=26124d635fdfe31ec3ce1ced9a89395eCAS | 17046432PubMed |
Knapp JR, Davie JK, Myer A, Meadows E, Olson EN, Klein WH (2006) Loss of myogenin in postnatal life leads to normal skeletal muscle but reduced body size. Development 133, 601–610.
| Loss of myogenin in postnatal life leads to normal skeletal muscle but reduced body size.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD28Xis1Cltb0%3D&md5=f01a0a777c0fc191f7d754b316463974CAS | 16407395PubMed |
Lee SJ, McPherron AC (2001) Regulation of myostatin activity and muscle growth. Proceedings of the National Academy of Sciences of the United States of America 98, 9306–9311.
| Regulation of myostatin activity and muscle growth.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3MXlvFSrsL0%3D&md5=29efc999740e1c67bfc74daeac5016f8CAS | 11459935PubMed |
Liu G, Zhao N, Zhu Y, Liu L, Liang C, Li F (2015) Effects of dietary vitamin B6 supplemental level on growth performance and vitamin B6 metabolism of growing Rex rabbits. Chinese Journal of Animal Nutrition 27, 2291–2299.
Ma K, Mallidis C, Bhasin S, Mahabadi V, Artaza J, Gonzalez-Cadavid N, Arias J, Salehian B (2003) Glucocorticoid-induced skeletal muscle atrophy is associated with upregulation of myostatin gene expression. American Journal of Physiology. Endocrinology and Metabolism 285, E363–E371.
| Glucocorticoid-induced skeletal muscle atrophy is associated with upregulation of myostatin gene expression.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3sXmsVahsb8%3D&md5=c99ca3b078df686b94fd659ccb5c2c02CAS | 12721153PubMed |
Malmolf K (1998) Amino acid in farm animal nutrition metabolism, partition and consequences of imbalance. Swedish Journal of Agricultural Research 4, 191–193.
Matsumoto H, Maruse H, Inaba Y, Yoshizawa K, Sasazaki S, Fujiwara A, Nishibori M, Nakamura A, Takeda S, Ichihara N, Kikuchi T, Mukai F, Mannen H (2008) The ubiquitin ligase gene (WWP1) is responsible for chicken muscular dystrophy. FEBS Letters 582, 2212–2218.
| The ubiquitin ligase gene (WWP1) is responsible for chicken muscular dystrophy.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD1cXnt1Ogurs%3D&md5=0cf194de88c93948fb4f2cb982c98e06CAS | 18501710PubMed |
Mauricio M, Cuskelly GJ, Williamson J, Toth JP, Gregory JF (2000) Vitamin B6 deficiency in rats reduces hepatic serine hydroxymethyl transferase and cystathionine β-synthase activities and rates of in vivo protein turnover, homocysteine remethylation and transsulfuration. Nutrition (Burbank, Los Angeles County, Calif.) 130, 1115–1123.
McFarland DC, Velleman SG, Pesall JE, Liu C (2007) The role of myostatin in chicken (Gallus domesticus) myogenic satellite cell proliferation and differentiation. General and Comparative Endocrinology 151, 351–357.
| The role of myostatin in chicken (Gallus domesticus) myogenic satellite cell proliferation and differentiation.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2sXkt1aiurw%3D&md5=251a4e8f3901f08242a1ead507733704CAS | 17362950PubMed |
McFarlane C, Plummer E, Thomas M, Hennebry A, Ashby M, Ling N, Smith H, Sharma M, Kambadur R (2006) Myostatin induces cachexia by activating the ubiquitin proteolytic system through an NF-kappaB-independent, FoxO1-dependent mechanism. Journal of Cellular Physiology 209, 501–514.
| Myostatin induces cachexia by activating the ubiquitin proteolytic system through an NF-kappaB-independent, FoxO1-dependent mechanism.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD28XhtVClu7fL&md5=82cbf1ad175412adaee17b8a7c6cd821CAS | 16883577PubMed |
McPherron AC, Lee SJ (1997) Double muscling in cattle due to mutations in the myostatin gene. Proceedings of the National Academy of Sciences of the United States of America 94, 12457–12461.
| Double muscling in cattle due to mutations in the myostatin gene.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK2sXns1ylsbk%3D&md5=44a0df4a9d72d6b24592c6b9dc9b25cfCAS | 9356471PubMed |
McPherron AC, Lawler AM, Lee SJ (1997) Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member. Nature 387, 83–90.
| Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK2sXivFygur0%3D&md5=c6d98d623a4ec5ffe01eafcefa22d2a2CAS | 9139826PubMed |
Miyake M, Hayashi S, Sato T, Taketa Y, Watanabe K, Hayashi S, Tanaka S, Ohwada S, Aso H, Yamaguchi T (2007) Myostatin and MyoD family expression in skeletal muscle of IGF-1 knockout mice. Cell Biology International 31, 1274–1279.
| Myostatin and MyoD family expression in skeletal muscle of IGF-1 knockout mice.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2sXnslWlsLs%3D&md5=bf068e29bd3c970eaa41a55ddb8eace1CAS | 17590360PubMed |
Nishi M, Yasue A, Nishimatu S, Nohno T, Yamaoka T, Itakura M, Moriyama K, Ohuchi H, Noji S (2002) A missense mutant myostatin causes hyperplasia without hypertrophy in the mouse muscle. Biochemical and Biophysical Research Communications 293, 247–251.
| A missense mutant myostatin causes hyperplasia without hypertrophy in the mouse muscle.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD38XksVGitLc%3D&md5=713f976e7e5ab1f18e6e9753e55be991CAS | 12054591PubMed |
NRC (1977) Nutrient requirements of domestic animals, no. 9. Nutrient requirements of rabbits, 2nd revised edn. (National Academy of Science, National Research Council: Washington, DC)
Peiretti PG, Meineri G (2008) Effects on growth performance, carcass characteristics,and the fat and meat fatty acid profile of rabbits fed diets with chia (Salvia hispanica L.) seed supplements. Meat Science 80, 1116–1121.
| Effects on growth performance, carcass characteristics,and the fat and meat fatty acid profile of rabbits fed diets with chia (Salvia hispanica L.) seed supplements.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD1cXhtFOqsrbM&md5=686c1196fb0a7209f51fc75dfdee0e2aCAS | 22063845PubMed |
Pell JM, Saunders JC, Gilmour RS (1993) Differential regulation of transcriptional initiation from insulin-like growth factor-I (IGF1) leader exons and of tissue IGF1 expression in response to changed growth hormone and nutritional status in sheep. Endocrinology 132, 1797–1807.
Pickart CM, Eddins MJ (2004) Ubiquitin: structures, functions, mechanisms. Biochimica et Biophysica Acta 1695, 55–72.
| Ubiquitin: structures, functions, mechanisms.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2cXhtVantbzO&md5=0dd3f62aa7d6f56abd28bcb435465587CAS | 15571809PubMed |
Rudnicki MA, Schnegelsberg PN, Stead RH, Braun T, Arnold HH, Jaenisch R (1993) MyoD or Myf-5 is required for the formation of skeletal muscle. Cell 75, 1351–1359.
| MyoD or Myf-5 is required for the formation of skeletal muscle.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK2cXhtVaqtbk%3D&md5=390715362b5506744973a8842894376fCAS | 8269513PubMed |
Sacheck JM, Ohtsuka A, McLary SC, Goldberg AL (2004) IGF1 stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1. American Journal of Physiology. Endocrinology and Metabolism 287, E591–E601.
| IGF1 stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2cXptVyitL0%3D&md5=47a5a85c9d5cebcf13ba10d940675719CAS | 15100091PubMed |
Sampson DA, Young LA, Kretsh MJ (1988) Marginal intake of vitamin B-6: effects on protein synthesis in liver, kidney and muscle of the rat. Nutrition Research (New York, N.Y.) 8, 309–319.
| Marginal intake of vitamin B-6: effects on protein synthesis in liver, kidney and muscle of the rat.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaL1cXhvVGmt7w%3D&md5=a4f917d58069684c7ad1b02b0641b350CAS |
Schuelke M, Wagner KR, Stolz LE, Hubner C, Riebel T, Komen W, Braun T, Tobin JF, Lee SJ (2004) Myostatin mutation associated with gross muscle hypertrophy in a child. The New England Journal of Medicine 350, 2682–2688.
| Myostatin mutation associated with gross muscle hypertrophy in a child.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2cXltFGns7c%3D&md5=a755f560f5eb645628abacadf48ffb90CAS | 15215484PubMed |
Schulze PC, Gielen S, Adams V, Linke A, Möbius-Winkler S, Erbs S, Kratzsch J, Hambrecht R, Schuler G (2003) Muscular levels of proinflammatory cytokines correlate with a reduced expression of insulin like growth factor-I in chronic heart failure. Basic Research in Cardiology 98, 267–274.
Smith JM, van Amburgh ME, Díaz MC, Lucy MC, Bauman DE (2002) Effect of nutrient intake on the development of the somatotropic axis and its responsiveness to GH in Holstein bull calves. Journal of Animal Science 80, 1528–1537.
Sohlstrom A, Katsman A, Kind KL, Grant PA, Owens PC, Robinson JS, Owens JA (1998) Effects of acute and chronic food restriction on the insulin-like growth factor axis in the guinea pig. The Journal of Endocrinology 157, 107–114.
| Effects of acute and chronic food restriction on the insulin-like growth factor axis in the guinea pig.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK1cXisFShtr4%3D&md5=f91f415f0770e4d2604961a2acd919aaCAS | 9614364PubMed |
Soliman AT, Hassan AE, Aref MK, Hintz RL, Rosenfeld RG, Rogol AD (1986) Serum insulin-like growth factors I and II concentrations and growth hormone and insulin responses to arginine infusion in children with protein-energy malnutrition before and after nutritional rehabilitation. Pediatric Research 20, 1122–1130.
| Serum insulin-like growth factors I and II concentrations and growth hormone and insulin responses to arginine infusion in children with protein-energy malnutrition before and after nutritional rehabilitation.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaL2sXjtFOqtA%3D%3D&md5=efad0ae63f92e4fc47d884fbe5cc729bCAS | 3099250PubMed |
Stick DA, David ME, Loerch SC, Simmen RC (1998) Relationship between blood serum insulin-like growth factor I concentration and post weaning feed efficiency of crossbred cattle at three levels of dietary intake. Journal of Animal Science 76, 498–505.
Straus DS, Takemoto CD (1990) Effect of dietary protein deprivation on insulin-like growth factor IGF1 and -II, IGF binding protein-2, and serum albumin gene expression in rat. Endocrinology 127, 1849–1860.
| Effect of dietary protein deprivation on insulin-like growth factor IGF1 and -II, IGF binding protein-2, and serum albumin gene expression in rat.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK3cXlvFSiu7o%3D&md5=b304223c7239e948bfc8511c368ddc04CAS | 1698149PubMed |
Takahashi S, Kajikawa M, Umezawa T, Takahashi S, Kato H, Miura Y, Taek JN, Noguchi T, Naito H (1990) Effect of dietary proteins on the plasma immunoreactive insulin-like growth factor-1/somatomedin C concentration in the rat. British Journal of Nutrition 63, 521–534.
| Effect of dietary proteins on the plasma immunoreactive insulin-like growth factor-1/somatomedin C concentration in the rat.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK3cXktVGjtLg%3D&md5=069de3575576045501c3092eb3fc8172CAS | 2383530PubMed |
Valente LM, Bower NI, Johnston IA (2012) Postprandial expression of growth related genes in Atlantic salmon (Salmo salar L.) juveniles fasted for 1 week and fed a single meal to satiation. British Journal of Nutrition 108, 2148–2157.
| Postprandial expression of growth related genes in Atlantic salmon (Salmo salar L.) juveniles fasted for 1 week and fed a single meal to satiation.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC38XhvVCltrjN&md5=5de19e54a3a35d432156e2313135aab1CAS | 22464448PubMed |
Vance ML, Hartman ML, Thorner MO (1992) Growth hormone and nutrition. Hormone Research 38, 85–88.
| Growth hormone and nutrition.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK3sXpsVCntA%3D%3D&md5=0a6555ff208a6dbb9f5b5d9e0e4c17c1CAS | 1295819PubMed |
Weller PA, Dauncey MJ, Bates PC, Brameld JM, Buttery PJ, Gilmour RS (1994) Regulation of porcine insulin-like growth factor I and growth hormone receptor mRNA expression by energy status. The American Journal of Physiology 266, E776–E785.
Yang W, Wang K, Chen Y, Zhang Y, Huang B, Zhu DH (2003) Functional characterization of recombinant myostatin and its inhibitory role in chicken muscle development. Acta Biochimica et Biophysica Sinica 35, 1016–1022.
