Interaction between tissue transglutaminase and amyloid-beta: Protein-protein binding versus enzymatic crosslinking

被引:9
作者
Wilhelmus, Micha M. M. [1 ]
Jongenelen, Cornelis A. [1 ]
Bol, John G. J. M. [1 ]
Drukarch, Benjamin [1 ]
机构
[1] Vrije Univ Amsterdam, Dept Anat & Neurosci, Amsterdam UMC, Amsterdam Neurosci, De Boelelaan 1117, Amsterdam, Netherlands
关键词
Amyloid-beta; Transglutaminase; Protein-complexes; Protein aggregation; HEAT-SHOCK PROTEINS; ALZHEIMERS-DISEASE; APOLIPOPROTEIN-E; ALPHA-SYNUCLEIN; PEPTIDE; PATHOGENESIS; AGGREGATION; COLOCALIZES; ASSOCIATION; ENZYMES;
D O I
10.1016/j.ab.2020.113578
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Self-interaction, chaperone binding and posttranslational modification of amyloid-beta (A beta) is essential in the initiation and propagation of A beta aggregation. Aggregation results in insoluble A beta deposits characteristic of Alzheimer's disease (AD) brain lesions, i.e. senile plaques and cerebral amyloid angiopathy. Tissue transglutaminase (tTG) is a calcium-dependent enzyme that catalyzes posttranslational modifications including the formation of covalent epsilon-(gamma-glutamyl)ysine isopeptide bonds (molecular crosslinks), and colocalizes with A beta deposits in AD. Two independent groups recently found that apart from the induction of A beta oligomerization, the blood-derived transglutaminase member FXIIIa forms stable protein-protein complexes with A beta independent of the transamidation reaction. Here, we investigated whether also tTG forms rigid protein complexes with A beta in the absence of catalytic activation. We found that both A beta(1.40) and A beta(1-42) are substrates for tTG-catalyzed crosslinking. In addition, in the absence of calcium or the presence of a peptidergic inhibitor of tTG, stable tTG-A beta(1.40) complexes were found. Interestingly, the stable complexes between tTG and A beta(1-)(40), were only found at 'physiological' concentrations of A beta(1.40). Together, our data suggest that depending on the A beta species at hand, and on the concentration of A beta, rigid protein-complexes are formed between tTG and A beta(1-40) without the involvement of the crosslinking reaction.
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页数:6
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