Please use this identifier to cite or link to this item:
Title: Effects of advanced glycation end products on ezrin-dependent functions in LLC-PK1 proximal tubule cells.
Austin Authors: Bach, Leon A;Gallicchio, Marisa A;McRobert, E Anne;Tikoo, Anjali;Cooper, Mark E
University of Melbourne, Department of Medicine, Austin Hospital, Heidelberg, Vic 3084 Australia
Issue Date: 1-Jun-2005
Publication information: Annals of the New York Academy of Sciences; 1043(): 609-16
Abstract: 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.
Gov't Doc #: 16037284
DOI: 10.1196/annals.1338.069
Type: Journal Article
Subjects: Animals
Cell Line
Cell Membrane.physiology
Cytoskeletal Proteins
Glycosylation End Products, Advanced.metabolism
Kidney Tubules, Proximal.physiology
Membrane Proteins.physiology
Receptors, Immunologic.physiology
Appears in Collections:Journal articles

Show full item record

Page view(s)

checked on Nov 28, 2022

Google ScholarTM


Items in AHRO are protected by copyright, with all rights reserved, unless otherwise indicated.