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Am J Physiol Endocrinol Metab (June 21, 2005). doi:10.1152/ajpendo.00243.2005
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Submitted on June 1, 2005
Accepted on June 15, 2005

Collagen synthesis in human musculoskeletal tissues and skin

J. A Babraj1*, D.J.R. Cuthbertson1, K. Smith2, H. Langberg3, B.F. Miller3, M. R. Krogsgaard3, M. Kjaer3, and M. J. Rennie2

1 Division of Molecular Physiology, University of Dundee, Dundee, United Kingdom
2 Division of Clinical Physiology, University of Nottingham, Derby, United Kingdom
3 Sports Medicine Research Unit, Copenhagen University Hospital at Bispebjerg, Copenhagen, Denmark

* To whom correspondence should be addressed. E-mail: j.a.babraj{at}dundee.ac.uk.

We have developed a direct method for the measurement of human musculoskeletal collagen synthesis based upon the incorporation of stable isotope labelled proline or leucine into protein and have used it to measure the rate of synthesis of collagen in tendon, ligament, muscle and skin. In post-absorptive, healthy young men (28 ± 6 y) synthetic rates for tendon, ligament, muscle and skin collagen were 0.046 ± 0.005, 0.040 ± 0.006, 0.016 ± 0.002 and 0.037 ±0.003 %.h-1 respectively (means ± SD). In post-absorptive, healthy elderly men (70 ± 6 y) the rate of skeletal muscle collagen synthesis is greater than in the young (0.023 ± 0.002 %.h-1, P< 0.05 vs. young). The rates of synthesis of tendon and ligament collagen are similar to those of mixed skeletal muscle protein in the post-absorptive state whereas the rate for muscle collagen synthesis is much lower in both young and elderly men. After nutritient provision, collagen synthesis was unaltered in tendon and skeletal muscle, remaining at post absorptive values (young: tendon, 0.045 ± 0.008 %.h-1; muscle, 0.016 ± 0.003 %.h-1; elderly: muscle, 0.024 ± 0.003 %.h-1). These results demonstrate that the rate of human musculoskeletal tissue collagen synthesis can be directly and robustly measured using stable isotope methodology.




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