Age-related changes in the physical properties, cross-linking, and glycation of collagen from mouse tail tendon.

ABSTRACT: Collagen is a structural protein whose internal cross-linking critically determines the properties and functions of connective tissue. Knowing how the cross-linking of collagen changes with age is key to understanding why the mechanical properties of tissues change over a lifetime. The current scientific consensus is that collagen cross-linking increases with age and that this increase leads to tendon stiffening. Here, we show that this view should be reconsidered. Using MS-based analyses, we demonstrated that during aging of healthy C57BL/6 mice, the overall levels of collagen cross-linking in tail tendon decreased with age. However, the levels of lysine glycation in collagen, which is not considered a cross-link, increased dramatically with age. We found that in 16-week-old diabetic db/d

SUBMITTER: Stammers M 

PROVIDER: S-EPMC7397091 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature