Abstract
These experiments provide evidence that creatine, an end product of contraction unique to muscle, is involved in the control of muscle-protein synthesis. Skeletal muscle cells formed both in vitro and in vivo synthesize myosin heavy chain faster when supplied creatine in vitro. The response is apparent within four hours after addition of creatine to the culture medium, and is dependent on concentration over a range of 10-100 μM creatine. The effect seems to be selective for cell-specific proteins(s), since the rate of total protein synthesis is unaffected.
Keywords: cell culture, chick embryo, heavy chain, protein synthesis, DNA synthesis
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- BURTON K. A study of the conditions and mechanism of the diphenylamine reaction for the colorimetric estimation of deoxyribonucleic acid. Biochem J. 1956 Feb;62(2):315–323. doi: 10.1042/bj0620315. [DOI] [PMC free article] [PubMed] [Google Scholar]
- DREYFUS J. C., KRUH J., SCHAPIRA G. Metabolism of myosin and life time of myofibrils. Biochem J. 1960 Jun;75:574–578. doi: 10.1042/bj0750574. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Fitch C. D., Shields R. P. Creatine metabolism in skeletal muscle. I. Creatine movement across muscle membranes. J Biol Chem. 1966 Aug 10;241(15):3611–3614. [PubMed] [Google Scholar]
- Hauschka S. D., Konigsberg I. R. The influence of collagen on the development of muscle clones. Proc Natl Acad Sci U S A. 1966 Jan;55(1):119–126. doi: 10.1073/pnas.55.1.119. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Hinegardner R. T. An improved fluorometric assay for DNA. Anal Biochem. 1971 Jan;39(1):197–201. doi: 10.1016/0003-2697(71)90476-3. [DOI] [PubMed] [Google Scholar]
- McManus I. R., Mueller H. The metabolism of myosin and the meromyosins from rabbit skeletal muscle. J Biol Chem. 1966 Dec 25;241(24):5967–5973. [PubMed] [Google Scholar]
- O'Neill M. C., Stockdale F. E. A kinetic analysis of myogenesis in vitro. J Cell Biol. 1972 Jan;52(1):52–65. doi: 10.1083/jcb.52.1.52. [DOI] [PMC free article] [PubMed] [Google Scholar]
- O'Neill M., Strohman R. C. Changes in DNA polymerase activity associated with cell fusion in cultures of embryonic muscle. J Cell Physiol. 1969 Feb;73(1):61–68. doi: 10.1002/jcp.1040730109. [DOI] [PubMed] [Google Scholar]
- O'Neill M., Strohman R. C. Studies of the decline of deoxyribonucleic acid polymerase activity during embryonic muscle cell fusion in vitro. Biochemistry. 1970 Jul 7;9(14):2832–2839. doi: 10.1021/bi00816a012. [DOI] [PubMed] [Google Scholar]
- Paterson B., Strohman R. C. Myosin structure as revealed by simultaneous electrophoresis of heavy and light subunits. Biochemistry. 1970 Oct 13;9(21):4094–4105. doi: 10.1021/bi00823a010. [DOI] [PubMed] [Google Scholar]
- Reporter M. 3-methylhistidine metabolism in proteins from cultured mammalian muscle cells. Biochemistry. 1969 Sep;8(9):3489–3496. doi: 10.1021/bi00837a001. [DOI] [PubMed] [Google Scholar]
- STOCKDALE F. E., HOLTZER H. DNA synthesis and myogenesis. Exp Cell Res. 1961 Sep;24:508–520. doi: 10.1016/0014-4827(61)90450-5. [DOI] [PubMed] [Google Scholar]
- Sender P. M. Muscle fibrils: Solubilization and gel electrophoresis. FEBS Lett. 1971 Sep 15;17(1):106–110. doi: 10.1016/0014-5793(71)80575-6. [DOI] [PubMed] [Google Scholar]
- Tonomura Y., Appel P., Morales M. On the molecular weight of myosin. II. Biochemistry. 1966 Feb;5(2):515–521. doi: 10.1021/bi00866a017. [DOI] [PubMed] [Google Scholar]