Inhibition of collagen fibril formation in vitro and subsequent cross-linking by glucose.
Glucose inhibits collagen fibril formation in vitro. A linear dose response was observed, with half-maximum inhibition of fibril formation occurring at 50 mM glucose. Nonfibrillar collagen cannot be cross-linked by lysyl oxidase, an enzyme that catalyzes the initial cross-linking reaction. The degree of decreased fibril formation correlated with the loss of ability of the collagen to serve as a substrate for lysyl oxidase. Collagen that is not cross-linked is unstable and more susceptible to collagenolytic attack. Interference with collagen cross-linking and more rapid degradation may explain the decreased amounts of interstitial collagen and the poor healing of wounds associated with diabetes mellitus.
D000818:Animals; D003094:Collagen / Q000378:metabolism*; D003920:Diabetes Mellitus / Q000378:metabolism; D003921:Diabetes Mellitus, Experimental / Q000378:metabolism; D004549:Elastin / Q000378:metabolism; D005947:Glucose / Q000494:pharmacology*; D006801:Humans; D066298:In Vitro Techniques; D046911:Macromolecular Substances; D011487:Protein Conformation; D008249:Protein-Lysine 6-Oxidase / Q000378:metabolism; D051381:Rats
D046911:Macromolecular Substances; D003094:Collagen; D004549:Elastin; D008249:Protein-Lysine 6-Oxidase; D005947:Glucose