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 pu...

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Veröffentlicht in:	Biochemical and biophysical research communications 1988-11, Vol.157 (1), p.115-120
Hauptverfasser:	Sane, David C., Moser, Tammy L., Pippen, Anne M.M., Parker, Charles J., Achyuthan, Komandoor E., Greenberg, Charles S.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Biological and medical sciences coagulation factor XIIIa Cross-Linking Reagents Factor XIII - metabolism Fundamental and applied biological sciences. Psychology Glycoproteins Glycoproteins - metabolism Immunoblotting Kinetics Molecular Weight protein-glutamine gamma -glutamyltransferase Proteins Putrescine - metabolism Substrate Specificity Transglutaminases - metabolism Vitronectin
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Beschreibung
Zusammenfassung:	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 1090-2104
DOI:	10.1016/S0006-291X(88)80020-2