Effects of advanced glycation end products on ezrin-dependent functions in LLC-PK1 proximal ribule cells

被引：7

作者：

Bach, LA

Gallicchio, MA

McRobert, EA

Tikoo, A

Cooper, ME

机构：

[1] Univ Melbourne, Austin Hosp, Dept Med, Heidelberg, Vic 3084, Australia

[2] Baker Med Res Inst, Prahran, Vic 3181, Australia

来源：

MAILLARD REACTION: CHEMISTRY AT THE INTERFACE OF NUTRITION, AGING, AND DISEASE | 2005年 / 1043卷

关键词：

advanced glycation end products; ERM proteins; ezrin; kidney; proximal tubule; diabetes; nephropathy; diabetic complications;

D O I：

10.1196/annals.1338.069

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：609 / 616

页数：8

共 43 条

[1]

Amieva MR, 1999, J CELL SCI, V112, P111

[2]

Bains R, 1997, J PATHOL, V183, P272

[3] FORMATION OF IMMUNOCHEMICAL ADVANCED GLYCOSYLATION END-PRODUCTS PRECEDES AND CORRELATES WITH EARLY MANIFESTATIONS OF RENAL AND RETINAL DISEASE IN DIABETES [J].