Expression of Receptors for Advanced Glycosylation End Products on Renal Cell Carcinoma Cells in Vitro

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 albumi...

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Published inBiochemical and biophysical research communications Vol. 196; no. 2; pp. 984 - 989
Main Authors Miki, S., Kasayama, S., Miki, Y., Nakamura, Y., Yamamoto, M., Sato, B., Kishimoto, T.
Format Journal Article
LanguageEnglish
Published San Diego, CA Elsevier Inc 29.10.1993
Elsevier
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Summary: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.
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content type line 23
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1993.2346