title: Vitronectin is a substrate for transglutaminases.
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.
authors: Department of Medicine, Duke University Medical Center, Durham, NC 27710.
authors: D C
authors: DC
authors: Sane
authors: T L
authors: TL
authors: Moser
authors: A M
authors: AM
authors: Pippen
authors: C J
authors: CJ
authors: Parker
authors: K E
authors: KE
authors: Achyuthan
authors: C S
authors: CS
authors: Greenberg
mesh_terms: D003432:Cross-Linking Reagents; D005176:Factor XIII / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism*; D015151:Immunoblotting; D007700:Kinetics; D008970:Molecular Weight; D011700:Putrescine / Q000378:metabolism; D013379:Substrate Specificity; D011503:Transglutaminases / Q000378:metabolism*; D019096:Vitronectin
chemical_list: D003432:Cross-Linking Reagents; D006023:Glycoproteins; D019096:Vitronectin; D005176:Factor XIII; D011503:Transglutaminases; D011700:Putrescine