How the binding and degrading capabilities of insulin degrading enzyme are-affected by ubiquitin

被引：41

作者：

Grasso, Giuseppe ^{[1
]}

Rizzarelli, Enrico ^{[1
,2
]}

Spoto, Giuseppe ^{[1
,2
]}

机构：

[1] Univ Catania, Dept Chem, I-95125 Catania, Italy

[2] CNR, Ist Biostrutture & Bioimmagini, Catania, Italy

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS | 2008年 / 1784卷 / 7-8期

关键词：

surface plasmon resonance; mass spectrometry; noncovalent interaction; ubiquitin; insulin degrading enzyme;

D O I：

10.1016/j.bbapap.2008.04.011

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：

Insulin degrading enzyme (IDE) is known to play a pivotal role on amyloidogenic peptide degradation but little is known about the changes in the proteolytic activity of the enzyme upon modification of extemal factors. Particularly, although it has been reported that altered ubiquitin concentration and/or hyperinsulinaemia increase the risk of developing Alzheimer's disease (AD), the molecular mechanism involved is unclear. In this work, we study the role that ubiquitin plays on IDE capability of binding and degrading insulin molecules and the obtained results indicate that ubiquitin has an allosteric role for IDE and high ubiquitin levels impair IDE activity. (C) 2008 Elsevier B.V. All rights reserved.

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页码：1122 / 1126

页数：5

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