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Collagen synthesis in human musculoskeletal tissues and skin

¹Division of Molecular Physiology, School of Life Sciences, University of Dundee, Dundee, Scotland; ²Division of Clinical Physiology, Graduate Entry Medical School, University of Nottingham School of Biomedical Sciences, City Hospital, Derby, England, United Kingdom; and ³Sports Medicine Research Unit and Department of Orthopaedic Surgery, Copenhagen University Hospital at Bispebjerg, Copenhagen, Denmark

Submitted 1 June 2005 ; accepted in final form 15 June 2005

We have developed a direct method for the measurement of human musculoskeletal collagen synthesis on the basis of the incorporation of stable isotope-labeled proline or leucine into protein and have used it to measure the rate of synthesis of collagen in tendon, ligament, muscle, and skin. In postabsorptive, healthy young men (28 ± 6 yr) 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, respectively (means ± SD). In postabsorptive, healthy elderly men (70 ± 6 yr) the rate of skeletal muscle collagen synthesis is greater than in the young (0.023 ± 0.002%/h, 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 postabsorptive 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 postabsorptive values (young: tendon, 0.045 ± 0.008%/h; muscle, 0.016 ± 0.003%/h; elderly: muscle, 0.024 ± 0.003%/h). These results demonstrate that the rate of human musculoskeletal tissue collagen synthesis can be directly and robustly measured using stable isotope methodology.

stable-isotope tracers; musculoskeletal collagen synthesis; nutrition; aging

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