Question

conclusion for research about advanced glycation end products and diabetes

Answer 1

Reducing sugars such as glucose react nonenzymatically and reversibly with free amino groups in proteins to produce small amounts of stable Amadori products. As a person ages, the further spontaneous irreversible modification of proteins by glucose can produce glycation end products (AGE), the end products of amino-sugar reactions that cross-link in protein backbones such as collagen. In diabetes, this continuous process of protein modification can be amplified as a consequence of chronic hyperglycemia. In diabetes, the AGE accumulates at an increased rate. The development of novel compound dimethyl-3-phenacylthiazolium chloride is responsible to break AGE cross-link that led to several diseases in heart and kidney. In diabetes, AGE not only stiffen collagen backbone but also act as agonists to AGE receptors on various cell types which is responsible to stimulate the release of profibrotic growth factors, promote collagen deposition, increase inflammation, and tissue fibrosis.