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

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Boros S,Kamps B,Wunderink L,de Bruijn W,de Jong WW,Boelens WC

doi

10.1016/j.febslet.2004.08.062

keywords:

subject

Has Abstract

pub_date

2004-10-08 00:00:00

pages

57-62

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

S0014579304010816

journal_volume

576

pub_type

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