期刊
JOURNAL OF PHYSIOLOGY-LONDON
卷 563, 期 1, 页码 203-211出版社
WILEY
DOI: 10.1113/jphysiol.2004.077180
关键词
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资金
- NIAMS NIH HHS [R01 AR049869, AR49869] Funding Source: Medline
- NICHD NIH HHS [HD 01459, K12 HD001459] Funding Source: Medline
- NIDDK NIH HHS [DK 56341, P30 DK056341] Funding Source: Medline
in many animals the rate of protein synthesis is higher in slow-twitch, oxidative than fast-twitch, glycolytic muscles. To discover if muscles in the human body also show such differences, we measured [C-13]leucine incorporation into proteins of anatomically distinct muscles of markedly different fibre-type composition (vastus lateralis, triceps, soleus) after an overnight fast and during infusion of a mixed amino acid solution (75 mg amino acids kg(-1) h(-1)) in nine healthy, young men. Type- I fibres contributed 83 +/- 4% (mean +/- S.E.M.) of total fibres in soleus, 59 +/- 3% in vastus lateralis and 22 +/- 2% in triceps. The basal myofibrillar and sarcoplasmic protein fractional synthetic rates (FSR, % h(-1)) were 0.034 +/- 0.001 and 0.064 +/- 0.001 (soleus), 0.031 +/- 0.001 and 0.060 +/- 0.001 (vastus), and 0.027 +/- 0.001 and 0.055 +/- 0.001 (triceps). During amino acid infusion, myofibrillar protein FSR increased to 3-fold, and sarcoplasmic to 2-fold basal values (P < 0.001). The differences between muscles, although significant statistically (triceps versus soleus and vastus lateralis, P < 0.05), were within similar to 15%, biologically probably insignificant. The rates of collagen synthesis were not affected by amino acid infusion and varied by < 5% between muscles and experimental conditions.
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