Premium
Effects of Advanced Glycation End Products on Ezrin‐Dependent Functions in LLC‐PK1 Proximal Tubule Cells
Author(s) -
BACH LEON A.,
GALLICCHIO MARISA A.,
McROBERT E ANNE,
TIKOO ANJALI,
COOPER MARK E.
Publication year - 2005
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1196/annals.1338.069
Subject(s) - ezrin , moesin , radixin , microbiology and biotechnology , glycation , phosphorylation , chemistry , signal transduction , actin cytoskeleton , cytoskeleton , receptor , cell , biology , biochemistry
A bstract : We have recently shown that advanced glycation products (AGEs) bind to the ERM (ezrin, radixin, moesin) family of proteins. ERM proteins act as cross‐linkers between cell membrane proteins and the actin cytoskeleton. They are also involved in signal transduction pathways. They therefore have a critical role in normal cell processes, including modulation of cell shape, adhesion, and motility. We postulate that AGEs may contribute to diabetic complications by disrupting ERM function. In support of this hypothesis, AGEs inhibit ezrin‐dependent tubulogenesis of proximal tubule cells. Phosphorylation is an important activating mechanism for ERM proteins, and AGEs inhibit ezrin phosphorylation mediated by the epidermal growth factor receptor.