α2-antiplasmin is a substrate of tissue transglutaminase

Hevessy Zs, J. Hársfalvi, L. Musbek

Research output: Contribution to journalArticle

Abstract

α2-Antiplasmin (α2AP) is a highly potent inhibitor of plasmin. The main physiological protective mechanism against the prompt fibrinolytic elimination of fibrin clot involves the covalent attachment of α22AP to the ex-chain of fibrin by a transglutaminase, activated blood coagulation factor XIII (FXIII). As endothelial cells contain another transglutaminase, tissue tranglutaminase (transglutaminase C; TGC) which, in certain pathological conditions, has also been implicated in fibrin stabilization. The aim of this study was to explore if TGC stabilized fibrin(ogen) clots could also be protected by this mechanism. As detected by SDS PAGE and fluorography, tissue TG catalyzed the incorporation of TGC substrate primary amines (14C glycin ethylester, 3H putrescine and dansylcadaverine) into α2AP indicating that the protein can provide acyl donor glutamine residue to the crosslinking reaction. The maximal extent of incorporation always remained below 1 mol amine per 1 mol α2AP. The crosslinking of α2AP to fibrin(osen) was investigated by SDS PAGE and immunoblotting. TGC crosslinked α2AP to fibrin and fibrinogen, but not to another α2AP molecule, in a time and concentration dependent manner. After the fast formation of a heterodimer of 140 kDa consisting of α2AP and fibrin a-chain the appearance of higher Mr (>300 kDa) products could be observed and, eventually, the heterodimers were incorporated into the highly crosslinked α-chain polymerincapable of penetrating the concentrating gel. It is proposed that TGC released from injured endothelial cell is involved in the production of fibrinolysis-resistant fibrin(ogen) network by incorporating aoAP into the fibrin(ogen) matrix.

Original languageEnglish
Pages (from-to)120
Number of pages1
JournalFibrinolysis
Volume10
Issue numberSUPPL. 3
Publication statusPublished - 1996

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Antifibrinolytic Agents
Fibrin
Transglutaminases
Amines
Photofluorography
Polyacrylamide Gel Electrophoresis
Endothelial Cells
Factor XIIIa
transglutaminase 2
Putrescine
Fibrinolysis
Glutamine
Immunoblotting
Fibrinogen
Gels

ASJC Scopus subject areas

  • Hematology

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α2-antiplasmin is a substrate of tissue transglutaminase. / Zs, Hevessy; Hársfalvi, J.; Musbek, L.

In: Fibrinolysis, Vol. 10, No. SUPPL. 3, 1996, p. 120.

Research output: Contribution to journalArticle

Zs, H, Hársfalvi, J & Musbek, L 1996, 'α2-antiplasmin is a substrate of tissue transglutaminase', Fibrinolysis, vol. 10, no. SUPPL. 3, pp. 120.
Zs, Hevessy ; Hársfalvi, J. ; Musbek, L. / α2-antiplasmin is a substrate of tissue transglutaminase. In: Fibrinolysis. 1996 ; Vol. 10, No. SUPPL. 3. pp. 120.
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