Transglutaminase catalyzes differential crosslinking of small heat shock proteins and amyloid-β

被引：34

作者：

Boros, S ^{[1
]}

Kamps, B ^{[1
]}

Wunderink, L ^{[1
]}

de Bruijn, W ^{[1
]}

de Jong, WW ^{[1
]}

Boelens, WC ^{[1
]}

机构：

[1] Univ Nijmegen, Nijmegen Ctr Mol Life Sci, Dept Biochem 161, NL-6500 HB Nijmegen, Netherlands

来源：

FEBS LETTERS | 2004年 / 576卷 / 1-2期

关键词：

transglutaminase; small heat shock protein; crossfinking; amyloid-beta; protein aggregate;

D O I：

10.1016/j.febslet.2004.08.062

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

Crosslinking of proteins by tissue transglutaminase (tTG) is enhanced in amyloid (Abeta) deposits characteristic of Alzheimer's disease and sporadic inclusion body myositis. Small heat shock proteins (sHsps) also occur in amyloid deposits. We here report the substrate characteristics for tTG of six sHsps. Hsp27, Hsp20 and HspB8 are both lysine- and glutamine-donors, alphaB-crystallin only is a lysine-donor, HspB2 a glutamine-donor, and HspB3 no substrate at all. Close interaction of proteins stimulates crosslinking efficiency as crosslinking between different sHsps only takes place within the same heteromeric complex. We also observed that alphaB-crystallin, Hsp27 and Hsp20 associate with Abeta in vitro, and can be readily crosslinked by tTG. (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.

引用

页码：57 / 62

页数：6

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