Transglutaminases catalyze cross-linking of plasminogen to fibronectin and human endothelial cells.

摘要: We have previously reported that apolipoprotein (a) is a substrate for transglutaminases. now demonstrate plasminogen which homologous to (a), also modified by these enzymes. Transglutaminases from different sources mediated the incorporation of monodansyl-cadaverine into plasminogen, indicating presence reactive glutamine(s) in plasminogen. Reactive lysines were identified using lysine-decorating peptide dansyl-PGGQQIV. In addition, transglutaminases catalyzed formation homopolymers and plasminogen-fibronectin heteropolymers. Human umbilical vein endothelial cells cross-linked high molecular mass aggregates. Cross-linked was cell associated, no cross-linking seen fluid-phase. Large generated on human (HUVEC) surface could not be eluted with epsilon-aminocapoic acid activatable tissue activator. These results suggest that, following non-covalent association HUVEC surface, surface-associated transglutaminase catalyzes large aggregates can converted functional plasmin. It proposed may function localize surfaces matrices tissues.