Abnormal dermal proteoglycan in aspartylglycosaminuria: a possible mechanism for ultrastructural changes of collagen fibrils in a glycoprotein storage disorder.

摘要: Changes in the structure and organization of collagen fibrils were recently described skin aspartylglycosaminuria patients1. The patients contained a normal amount distribution glycosaminoglycans. but dermatan sulfate was more sensitive to chondroitinase AC digestion, resulting unsaturated 4-sulfated disaccharides which not detected controls. Isolated chains as well present intact core protein synthesized by fibroblasts from an patient also digestible with AC. while those control fibroblast culture could be digested ABC only. This is indirect evidence for abnormal epimerization patients, may associated changes fibril formation.