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Vitronectin is a substrate for transglutaminases.

作者信息

Sane D C, Moser T L, Pippen A M, Parker C J, Achyuthan K E, Greenberg C S

机构信息

Department of Medicine, Duke University Medical Center, Durham, NC 27710.

出版信息

Biochem Biophys Res Commun. 1988 Nov 30;157(1):115-20. doi: 10.1016/s0006-291x(88)80020-2.

Abstract

Vitronectin (VN) was found to be a substrate for both plasma transglutaminase (Factor XIIIa) and guinea pig liver transglutaminase (TG). Incorporation of [3H]-putrescine indicated the presence of reactive glutaminyl residues in VN. When VN was incubated with TG or Factor XIIIa, in the absence of putrescine, multimeric covalent complexes were identified, indicating that VN can also contribute lysyl residues to the bond catalyzed by transglutaminases. Cross-linking of VN by TG and Factor XIIIa may modulate the effects of VN on the complement and coagulation systems in hemostatic plugs and extracellular matrix.

摘要

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