Intramuscular collagen cross‐linking in aging men and women

• Published in: The FASEB journal 2007, Vol.21 (6), p.LB118-LB118
• Main Authors: Haus, Jacob M, Carrithers, John A, Miller, Benjamin I, Trappe, Todd A
• Format: Article
• Language: English
• ISSN: 0892-6638; 1530-6860
• DOI: 10.1096/fasebj.21.6.LB118

The connective tissue components of skeletal muscle are primarily comprised of collagen and play a critical role in maintaining muscle structure and transfer of force from contractile elements to the bone. Collagen tensile strength and stability is achieved through both intra‐ and intermolecular cross‐linking. Data from animals have shown that aging skeletal muscle accumulates cross‐links which may play a role in reduced muscle function. We hypothesized the collagen cross‐link concentration of old individuals would be greater than young, thus suggesting a mechanism that contributes to reduced muscle function. Intramuscular (vastus lateralis) collagen cross‐links (pyridinoline) were determined in 18 young (9 M; 9 W; age 25±1) and 22 old individuals (10 M; 12 W; age 77±1) after CF1 extraction from muscle hydrolyzates. Cross‐links were expressed relative to collagen content (APS#7649) as mmol pyridinoline • mole collagen−1. The degree of intramuscular collagen cross‐linking was not affected by age (young: 395±65; old: 351±45) or gender (men: 402±58; women: 343±50). These results suggest that the age related decline in whole muscle function is not related to increases in intramuscular collagen cross‐linking. Supported by NIH grants R01 AG020532, R21 AG15833 and K01 AG00831.