Effects of Advanced Glycation End Products on Ezrin-Dependent Functions in LLC-PK1 Proximal Tubule Cells

: 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 cri...

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Bibliographic Details
Published in:Annals of the New York Academy of Sciences 2005-06, Vol.1043 (1), p.609-616
Main Authors: BACH, LEON A., GALLICCHIO, MARISA A., McROBERT, E ANNE, TIKOO, ANJALI, COOPER, MARK E.
Format: Article
Language:English
Subjects:
Adhesion
advanced glycation end products
Age
Animals
Cell Line
Cell Membrane - physiology
Cytoskeletal Proteins
diabetes
diabetic complications
Disrupting
ERM proteins
ezrin
Glycation End Products, Advanced - metabolism
Growth factors
Humans
kidney
Kidney Tubules, Proximal - physiology
Membrane Proteins - physiology
Modulation
nephropathy
Phosphoproteins - physiology
Phosphorylation
Proteins
proximal tubule
Receptor for Advanced Glycation End Products
Receptors
Receptors, Immunologic - physiology
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Summary:: 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.
ISSN:0077-8923
1749-6632
DOI:10.1196/annals.1338.069