Abstract
Abstract: :
Purpose: To survey the expression of receptors for advanced glycosylation end products on bovine retinal pericytes. Methods: Proteins that have been modified by long-term expose to glucose accumulate advanced glycosylation end products (AGEs), which are found in the plasma and accumulate in the tissues during aging and at an accelerated rate in diabetes. A novel integral membrane protein, termed receptor for AGE (RAGE), forms a central part of the cell surface binding site for AGEs. In these studies, we have examined the interaction of AGE-BSA with bovine retinal capillary pericytes (BRP). Using polyconal antibody raised to synthetic peptide that corresponds to amino acids 42-59 of the human receptor for advanced glycated end products and reverse transcriptase-polymerase chain reaction of RAGE mRNA to detect the expressiong of RAGE. Results: Immunostaining showed RAGE in the retinal pericytes. Consistent with these data, RAGE mRNA were identified through reverse transcriptase-polymerase chain reaction. Conclusions: These results indicate that RAGE is present in retinal pericytes and suggest that AGEs taken up through RAGE on retinal pericytes might play a role in influencing the growth of retinal pericytes.
Keywords: diabetic retinopathy • immunohistochemistry • vascular cells