Mechanical stretching changes crosslinking and glycation levels in the collagen of mouse tail tendon.

ABSTRACT: Collagen I is a major tendon protein whose polypeptide chains are linked by covalent crosslinks. It is unknown how the crosslinking contributes to the mechanical properties of tendon or whether crosslinking changes in response to stretching or relaxation. Since their discovery, imine bonds within collagen have been recognized as being important in both crosslink formation and collagen structure. They are often described as acidic or thermally labile, but no evidence is available from direct measurements of crosslink levels whether these bonds contribute to the mechanical properties of collagen. Here, we used MS to analyze these imine bonds after reduction with sodium borohydride while under tension and found that their levels are altered in stretched tendon. We studied the changes in cross

SUBMITTER: Stammers M 

PROVIDER: S-EPMC7397108 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature