Vitronectin is a substrate for transglutaminases

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 put...

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Bibliographic Details
Published in:Biochemical and biophysical research communications Vol. 157; no. 1; p. 115
Main Authors: Sane, D C, Moser, T L, Pippen, A M, Parker, C J, Achyuthan, K E, Greenberg, C S
Format: Journal Article
Language:English
Published: United States 30-11-1988
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Summary: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.
ISSN:0006-291X
DOI:10.1016/S0006-291X(88)80020-2