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Transglutaminase catalyzes differential crosslinking of small heat shock proteins and amyloid‐β
Author(s) -
Boros Sandor,
Kamps Bram,
Wunderink Lisa,
de Bruijn Willem,
de Jong Wilfried W.,
Boelens Wilbert C.
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.08.062
Subject(s) - tissue transglutaminase , hsp27 , heat shock protein , lysine , chemistry , amyloid (mycology) , glutamine , substrate (aquarium) , protein aggregation , biochemistry , in vitro , biophysics , hsp70 , amino acid , enzyme , biology , inorganic chemistry , ecology , gene
Crosslinking of proteins by tissue transglutaminase (tTG) is enhanced in amyloid (Aβ) 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, αB‐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 αB‐crystallin, Hsp27 and Hsp20 associate with Aβ in vitro, and can be readily crosslinked by tTG.