Cloning and expression of a cell surface receptor for advanced glycosylation end products of proteins.
M Neeper, AM Schmidt, J Brett, SD Yan, F Wang… - Journal of biological …, 1992 - ASBMB
Advanced glycosylation end products of proteins (AGEs) are nonenzymatically glycosylated
proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes.
A approximately 35-kDa polypeptide with a unique NH2-terminal sequence has been
isolated from bovine lung and found to be present on the surface of endothelial cells where it
mediates the binding of AGEs (receptor for advanced glycosylation end product or RAGE).
Using an oligonucleotide probe based on the amino-terminal sequence of RAGE, an …
proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes.
A approximately 35-kDa polypeptide with a unique NH2-terminal sequence has been
isolated from bovine lung and found to be present on the surface of endothelial cells where it
mediates the binding of AGEs (receptor for advanced glycosylation end product or RAGE).
Using an oligonucleotide probe based on the amino-terminal sequence of RAGE, an …