Protein synthesis rates in human muscles: neither anatomical location nor fibre-type composition are major determinants

B. Mittendorfer*, J.L. Anderson, P. Plomgaard, B. Saltin, J.A. Babraj, K. Smith, M.J. Rennie

*Corresponding author for this work

Research output: Contribution to journalArticle

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Abstract

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 [13C]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 -1 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 approximately 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.
Original languageEnglish
Pages (from-to)203-211
Number of pages9
JournalThe Journal of Physiology
Volume563
Issue number1
Early online date20 Dec 2004
DOIs
Publication statusPublished - 7 Feb 2005
Externally publishedYes

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protein synthesis
muscles
amino acids
myofibrillar proteins
leucine
collagen
proteins
synthesis
animals

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Mittendorfer, B. ; Anderson, J.L. ; Plomgaard, P. ; Saltin, B. ; Babraj, J.A. ; Smith, K. ; Rennie, M.J. / Protein synthesis rates in human muscles : neither anatomical location nor fibre-type composition are major determinants. In: The Journal of Physiology. 2005 ; Vol. 563, No. 1. pp. 203-211.
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Protein synthesis rates in human muscles : neither anatomical location nor fibre-type composition are major determinants. / Mittendorfer, B.; Anderson, J.L.; Plomgaard, P.; Saltin, B.; Babraj, J.A.; Smith, K.; Rennie, M.J.

In: The Journal of Physiology, Vol. 563, No. 1, 07.02.2005, p. 203-211.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Protein synthesis rates in human muscles

T2 - neither anatomical location nor fibre-type composition are major determinants

AU - Mittendorfer, B.

AU - Anderson, J.L.

AU - Plomgaard, P.

AU - Saltin, B.

AU - Babraj, J.A.

AU - Smith, K.

AU - Rennie, M.J.

PY - 2005/2/7

Y1 - 2005/2/7

N2 - 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 [13C]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 -1 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 approximately 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.

AB - 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 [13C]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 -1 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 approximately 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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DO - 10.1113/jphysiol.2004.077180

M3 - Article

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JO - Journal of Physiology

JF - Journal of Physiology

SN - 0022-3751

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ER -