Abstract
Proteins that have been modified by long-term expose to glucose accumulate advanced glycosylation end products (AGEs) as a function of protein age. In these studies, we have examined the interaction of AGE-protein with renal cell carcinoma cells (RCC) in vitro, using AGE-modified bovine serum albumin (AGE-BSA) as a probe. AGE-BSA showed tendency to induce in vitro cell growth of RCC cells and promoted the production of interleukin-6 (IL-6), an in vitro autocrine growth factor. Reverse transcriptase-polymerase chain reaction analysis revealed that RCC cells used here express mRNA for a receptor for AGEs (RAGE). These results suggested that AGEs taken up through RAGE on RCC cells might play a role in promoting the growth of RCC cells.
MeSH terms
-
Adenocarcinoma, Clear Cell / metabolism
-
Base Sequence
-
Carcinoma, Renal Cell / metabolism*
-
Cell Division
-
Cells, Cultured
-
DNA Primers
-
Endothelium, Vascular / metabolism
-
Gene Expression
-
Glycation End Products, Advanced / metabolism*
-
Glycation End Products, Advanced / pharmacology*
-
Humans
-
Interleukin-6 / biosynthesis
-
Molecular Sequence Data
-
Polymerase Chain Reaction / methods
-
RNA, Messenger / analysis
-
RNA, Messenger / biosynthesis
-
Receptor for Advanced Glycation End Products
-
Receptors, Immunologic / biosynthesis*
-
Tumor Cells, Cultured
-
Umbilical Veins
-
Urinary Bladder Neoplasms / metabolism*
Substances
-
DNA Primers
-
Glycation End Products, Advanced
-
Interleukin-6
-
RNA, Messenger
-
Receptor for Advanced Glycation End Products
-
Receptors, Immunologic