Collagen synthesis in human musculoskeletal tissues and skin

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Collagen synthesis in human musculoskeletal tissues and skin. / Babraj, J A; Cuthbertson, D J R; Smith, K; Langberg, Henning; Miller, B; Krogsgaard, M R; Kjaer, M; Rennie, M J.

In: American Journal of Physiology: Endocrinology and Metabolism, Vol. 289, No. 5, 2005, p. E864-9.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Babraj, JA, Cuthbertson, DJR, Smith, K, Langberg, H, Miller, B, Krogsgaard, MR, Kjaer, M & Rennie, MJ 2005, 'Collagen synthesis in human musculoskeletal tissues and skin', American Journal of Physiology: Endocrinology and Metabolism, vol. 289, no. 5, pp. E864-9. https://doi.org/10.1152/ajpendo.00243.2005

APA

Babraj, J. A., Cuthbertson, D. J. R., Smith, K., Langberg, H., Miller, B., Krogsgaard, M. R., ... Rennie, M. J. (2005). Collagen synthesis in human musculoskeletal tissues and skin. American Journal of Physiology: Endocrinology and Metabolism, 289(5), E864-9. https://doi.org/10.1152/ajpendo.00243.2005

Vancouver

Babraj JA, Cuthbertson DJR, Smith K, Langberg H, Miller B, Krogsgaard MR et al. Collagen synthesis in human musculoskeletal tissues and skin. American Journal of Physiology: Endocrinology and Metabolism. 2005;289(5):E864-9. https://doi.org/10.1152/ajpendo.00243.2005

Author

Babraj, J A ; Cuthbertson, D J R ; Smith, K ; Langberg, Henning ; Miller, B ; Krogsgaard, M R ; Kjaer, M ; Rennie, M J. / Collagen synthesis in human musculoskeletal tissues and skin. In: American Journal of Physiology: Endocrinology and Metabolism. 2005 ; Vol. 289, No. 5. pp. E864-9.

Bibtex

@article{4507bb7220e24d8d8d8ecb1f878c8ffd,
title = "Collagen synthesis in human musculoskeletal tissues and skin",
abstract = "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 nutrient 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.",
keywords = "Adult, Age Factors, Aged, Amino Acids, Essential, Biopsy, Needle, Collagen, Humans, Ligaments, Male, Muscle, Skeletal, Skin, Tendons",
author = "Babraj, {J A} and Cuthbertson, {D J R} and K Smith and Henning Langberg and B Miller and Krogsgaard, {M R} and M Kjaer and Rennie, {M J}",
year = "2005",
doi = "10.1152/ajpendo.00243.2005",
language = "English",
volume = "289",
pages = "E864--9",
journal = "American Journal of Physiology: Endocrinology and Metabolism",
issn = "0193-1849",
publisher = "American Physiological Society",
number = "5",

}

RIS

TY - JOUR

T1 - Collagen synthesis in human musculoskeletal tissues and skin

AU - Babraj, J A

AU - Cuthbertson, D J R

AU - Smith, K

AU - Langberg, Henning

AU - Miller, B

AU - Krogsgaard, M R

AU - Kjaer, M

AU - Rennie, M J

PY - 2005

Y1 - 2005

N2 - 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 nutrient 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.

AB - 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 nutrient 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.

KW - Adult

KW - Age Factors

KW - Aged

KW - Amino Acids, Essential

KW - Biopsy, Needle

KW - Collagen

KW - Humans

KW - Ligaments

KW - Male

KW - Muscle, Skeletal

KW - Skin

KW - Tendons

U2 - 10.1152/ajpendo.00243.2005

DO - 10.1152/ajpendo.00243.2005

M3 - Journal article

VL - 289

SP - E864-9

JO - American Journal of Physiology: Endocrinology and Metabolism

JF - American Journal of Physiology: Endocrinology and Metabolism

SN - 0193-1849

IS - 5

ER -

ID: 38367093