Please use this identifier to cite or link to this item: http://ahro.austin.org.au/austinjspui/handle/1/9966
Title: Effects of advanced glycation end products on ezrin-dependent functions in LLC-PK1 proximal tubule cells.
Authors: Bach, Leon A;Gallicchio, Marisa A;McRobert, E Anne;Tikoo, Anjali;Cooper, Mark E
Affiliation: University of Melbourne, Department of Medicine, Austin Hospital, Heidelberg, Vic 3084 Australia. leon.bach@med.monash.edu.au
Issue Date: 1-Jun-2005
Citation: 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.
Internal ID Number: 16037284
URI: http://ahro.austin.org.au/austinjspui/handle/1/9966
DOI: 10.1196/annals.1338.069
URL: http://www.ncbi.nlm.nih.gov/pubmed/16037284
Type: Journal Article
Subjects: Animals
Cell Line
Cell Membrane.physiology
Cytoskeletal Proteins
Glycosylation End Products, Advanced.metabolism
Humans
Kidney Tubules, Proximal.physiology
Membrane Proteins.physiology
Phosphoproteins.physiology
Receptors, Immunologic.physiology
Appears in Collections:Journal articles

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