Isolation and characterization of two binding proteins for advanced glycosylation end products from bovine lung which are present on the endothelial cell surface.
AM Schmidt, M Vianna, M Gerlach, J Brett… - Journal of Biological …, 1992 - ASBMB
Nonenzymatic glycosylation of proteins, as occurs at an accelerated rate in diabetes, can
lead to the formation of advanced glycosylation end products of proteins (AGEs), which can
bind to endothelial cells, thereby altering cellular function in a manner which could
contribute to the pathogenesis of diabetic angiopathy. In this report, we describe the
isolation of two endothelial cell surface-associated proteins which mediate, at least in part,
the interaction of AGEs with endothelium. Based on pilot studies demonstrating AGE binding …
lead to the formation of advanced glycosylation end products of proteins (AGEs), which can
bind to endothelial cells, thereby altering cellular function in a manner which could
contribute to the pathogenesis of diabetic angiopathy. In this report, we describe the
isolation of two endothelial cell surface-associated proteins which mediate, at least in part,
the interaction of AGEs with endothelium. Based on pilot studies demonstrating AGE binding …