Non-enzymatic Glycation of Type I Collagen in Rat Tail Tendons- Diabetic Complications to Structure and Function of Collagen

Diabetes causes changes to the structure of extracellular matrix elements such as collagen. The effects of diabetes on collagen can lead to complications: low tissue repair, glaucoma, faster aging, altered periodontal cell behavior, neuropathy and other issues. Here we try to explore the effect of non-enzymatic glycation of type I collagen from rat tail tendons in a trial to mimic hyperglycemic and hypoglycemic conditions and relate these results and effects to the structural changes in collagen, in relevance to the aforementioned diseases and also see how proteolytic degradation of glycated collagen changes under these conditions. Preliminary experiments suggest that at hyper- and hypoglycemic conditions of glucose, the collagenolysis by MMP1 was higher when compared to collagenolysis at normal, non-pathological physiological concentration of sugar. From this we can predict that crosslinks formed by sugars result in altered accessibility for the MMP1 molecules that helps them to better degrade collagen. We will present evidence of the nature of the structural changes brought about in fibrillar collagen because of glycation, using X-ray diffraction of the glycated fibers.