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Divisions of 1 Endocrinology,
Using sodium dodecyl sulfate-polyacrylamide
gel electrophoresis (SDS-PAGE), we have developed a simple method to
isolate myosin heavy chain (MHC) and actin from small (60-80 mg)
human skeletal muscle samples for the determination of their fractional
synthesis rates. The amounts of MHC and actin isolated are adequate for the quantification of
[13C]leucine abundance
by gas chromatography-combustion-isotope ratio mass spectrometry
(GC-C-IRMS). Fractional synthesis rates of mixed muscle protein (MMP),
MHC, and actin were determined in six healthy young subjects (27 ± 1 yr) after they received a 14-h intravenous infusion (prime = 7.58 µmol/kg body wt, constant infusion = 7.58 µmol · kg body
wt
1 · h1)
of [1-13C]leucine. The
fractional synthesis rates of MMP, MHC, and actin were found to be
0.0468 ± 0.0048, 0.0376 ± 0.0033, and 0.0754 ± 0.0078%/h,
respectively. Overall, the synthesis rate of MHC was 20% lower
(P = 0.012), and the synthesis rate of
actin was 61% higher (P = 0.060, not
significant) than the MMP synthesis rate. The isolation of these
proteins for isotope abundance analysis by GC-C-IRMS provides important
information about the synthesis rates of these specific contractile
proteins, as opposed to the more general information provided by the
determination of MMP synthesis rates.
muscle protein synthesis; amino acid metabolism; protein metabolism; stable isotope tracers; mass spectrometry
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