Skeletal muscle myostatin mRNA expression is fiber-type specific and increases during hindlimb unloading

American Journal of Physiology - Regulatory Integrative and Comparative Physiology

Volumn 277, Issue 2 46-2, 1999, Pages

  Carlson, Christian J ^a   Booth, Frank W ^a   Gordon, Scott E ^a  

^a UNIVERSITY OF TEXAS MEDICAL SCHOOL   (United States)

Author keywords

Atrophy; Mice; Myosin heavy chain isoforms

Indexed keywords

MESSENGER RNA; MYOSIN HEAVY CHAIN; MYOSTATIN;

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; FAST MUSCLE; FEMALE; GASTROCNEMIUS MUSCLE; GENE EXPRESSION; HINDLIMB; MOUSE; MUSCLE MASS; NONHUMAN; PLANTARIS MUSCLE; PRIORITY JOURNAL; PROTEIN EXPRESSION; SKELETAL MUSCLE; SLOW MUSCLE; SOLEUS MUSCLE;

EID: 0032832616     PISSN: 03636119     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpregu.1999.277.2.r601     Document Type: Article

References (25)

1. Allen, R. E., and L. K. Boxhorn. Inhibition of skeletal muscle satellite cell differentiation by transforming growth factor-beta. J. Cell. Physiol. 133: 567-572, 1987.
2. Allen, R. E., and L. K. Boxhorn. Regulation of skeletal muscle satellite cell proliferation and differentiation by transforming growth factor-beta insulin-like growth factor and fibroblast growth factor. J. Cell. Physiol. 138: 311-315, 1989.
3. Babij, P., and F. W. Booth. α-Actin and cytochrome c mRNAs in atrophied adult rat skeletal muscle. Am. J. Physiol. 254 (Cell Physiol. 23): C651-C656, 1988.
4. Chin, E. R., E. N. Olson, J. A. Richardson, Q. Yang, C. Humphries, J. M. Shelton, H. Wu, W. Zhu, R. Bassel-Duby, and R. S. Williams. A calcineurin-dependent transcriptional pathway controls skeletal muscle fiber type. Genes Dev. 12: 2499-2509, 1998.
5. Chomczynski, P., and N. Sacchi. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162: 156-159, 1987.
6. Cresci, S., L. D. Wright, J. A. Spratt, F. N. Briggs, and D. P. Kelly. Activation of a novel metabolic gene regulatory pathway by chronic stimulation of skeletal muscle. Am. J. Physiol. 270 (Cell Physiol. 39): C1413-C1420, 1996.
7. Criswell, D. S., F. W. Booth, F. DeMayo, R. J. Schwartz, S. E. Gordon, and M. L. Fiorotto. Overexpression of IGF-I in skeletal muscle of transgenic mice does not prevent unloading-induced atrophy. Am. J. Physiol. 275 (Endocrinol. Metab. 38): E373-E379, 1998.
8. Darr, K. C., and E. Schultz. Hindlimb suspension suppresses muscle growth and satellite cell proliferation. J. Appl. Physiol. 67: 1827-1834, 1989.
9. Gibson, M. C., and E. Schultz. The distribution of satellite cells and their relationship to specific fiber types in soleus and extensor digitorum longus muscles. Anat. Rec. 202: 329-337, 1982.
10. Gonzalez-Cadavid, N. F., W. E. Taylor, K. Yarasheski, I. Sinha-Hikim, K. Ma, S. Ezzat, R. Shen, R. Lalani, S. Asa, M. Mamita, G. Nair, S. Arver, and S. Bhasin. Organization of the human myostatin gene and expression in healthy men and HIV-infected men with muscle wasting. Proc. Natl. Acad. Sci. USA 95: 14938-14943, 1998.
11. Gossett, L. A., D. J. Kelvin, E. A. Sternberg, and E. N. Olson. A new myocyte-specific enhancer-binding factor that recognizes a conserved element associated with multiple muscle-specific genes. Mol. Cell. Biol. 9: 5022-5033, 1989.
12. Grobet, L., L. J. R. Martin, D. Poncelet, D. Priottin, B. Brouwers, J. Riquet, A. Schoeberlein, S. Dunner, F. Menisseir, J. Massabandam, R. Fires, R. Hanset, and M. Georges. A deletion in the bovine myostatin gene causes the double-muscled phenotype in cattle. Nat. Genet. 17: 71-74, 1997.
13. Gulati, A. K. The effect of X-irradiation on skeletal muscle regeneration in the adult rat. J. Neurol. Sci. 78: 111-120, 1987.
14. Haida, N., W. M. Fowler, Jr., R. T. Abresch, D. B. Larson, R. B. Sharman, R. G. Taylor, and R. K. Entrikin. Effect of hind-limb suspension on young and adult skeletal muscle. I. Normal mice. Exp. Neurol. 103: 68-76, 1989.
15. Ji, S., R. L. Losinski, S. G. Cornelius, G. R. Frank, G. M. Willis, D. E. Gerrard, F. F. S. Depreux, and M. E. Spurlock. Myostatin expression in porcine tissues: tissue specificity and developmental and postnatal regulation. Am. J. Physiol. 275 (Regulatory Integrative Comp. Physiol. 44): R1265-R1273, 1998.
16. Kambadur, R., M. Sharma, T. P. L. Smith, and J. J. Bass. Mutations in myostatin (GDF-8) in double-muscled belgian blue and piedmontese cattle. Genome Res. 7: 910-915, 1997.
17. McCarthy, J. J., A. M. Fox, G. L. Tsika, L. Gao, and R. W. Tsika. β-MHC transgene expression in suspended and mechanically overloaded/suspended soleus muscle of transgenic mice. Am. J. Physiol. 272 (Regulatory Integrative Comp. Physiol. 41): R1522-R1561, 1997.
18. McPherron, A. C., A. M. Lawler, and S.-J. Lee. Regulation of skeletal muscle mass in mice by a new TGF-β superfamily member. Nature 387: 83-90, 1997.
19. McPherron, A. C., and S.-J. Lee. Double muscling in cattle due to mutations in the myostatin gene. Proc. Natl. Acad. Sci. USA 94: 12457-12461, 1997.
20. Pette, D., and R. S. Staron. Mammalian skeletal muscle fiber type transitions. Int. Rev. Cytol. 170: 143-223, 1997.
21. Rosenblatt, J. D., and D. J. Parry. Gamma irradiation prevents compensatory hypertrophy of overloaded mouse extensor digitorum longus muscle. J. Appl. Physiol. 73: 2538-2543, 1992.
22. Schultz, E., K. C. Darr, and A. Macius. Acute effects of hindlimb unweighting on satellite cells of growing skeletal muscle. J. Appl. Physiol. 76: 266-270, 1994.
23. Snow, M. H. A quantitative ultrastructural analysis of satellite cells in denervated fast and slow muscles of the mouse. Anat. Rec. 207: 593-604, 1983.
24. Talmadge, R. J., and R. R. Roy. Electrophoretic separation of rat skeletal muscle myosin heavy chain isoforms. J. Appl. Physiol. 75: 2337-2340, 1993.
25. Thomason, D. B., and F. W. Booth. Atrophy of the soleus muscle by hindlimb unweighting. J. Appl. Physiol. 68: 1-12, 1990.