Transglutaminase catalyzes differential crosslinking of small heat shock proteins and amyloid-β
Transglutaminase catalyzes differential crosslinking of small heat shock proteins and amyloid-β
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DOI：
10.1016/j.febslet.2004.08.062
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发表时间：
2004-10-08
期刊：
影响因子：
3.5
通讯作者：
Boelens, WC
中科院分区：
文献类型：
--
作者：
Boros, S;Kamps, B;Boelens, WC
在阿尔茨海默病和散发性包涵体肌炎的特征性淀粉样蛋白（Abeta）沉积物中，组织转氨酶（tTG）引起的蛋白质交联增强。小的热休克蛋白（sHsps）也出现在淀粉样沉积物中。我们在这里报告的底物特性tTG的六sHsps。Hsp 27、Hsp 20和HspB 8都是赖氨酸和谷氨酰胺供体，α B-晶状体蛋白仅是赖氨酸供体，HspB 2是谷氨酰胺供体，而HspB 3根本没有底物。蛋白质的紧密相互作用刺激交联效率，因为不同sHsps之间的交联仅发生在相同的异聚复合物内。我们还观察到α B-晶状体蛋白、Hsp 27和Hsp 20在体外与Abeta缔合，并且可以容易地通过tTG交联。(C)2004年欧洲生物化学学会联合会。由Elsevier B出版。V.保留所有权利。
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.