Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.7 (plasmin)
 9,023 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The role of substances for wound healing in chronic subdural hematoma was investigated. Fibronectin, blood coagulation factor XIII (F X III), alpha 2 -plasmin inhibitor (alpha 2-PI) and alpha 2-PI plasmin complex (PIC) in hematoma fluid were measured, sixty cases of hematoma fluid (15 cases were bilateral chronic subdural hematomas) were used for analysis. The levels of fibronectin in hematoma fluid ranged widely from 40 to 1068 micrograms/ml. The levels of F XIII (except 1 case) in the hematoma fluid were less than 70% (normal plasma level 72-144%). And also the levels of alpha 2-PI in the hematoma fluid were lower than that in normal blood plasma (85-115%). Fibrin, fibronectin, alpha 2-PI and collagen crosslinks to these proteins by the catalytic action of the activated F XIII. These substrate proteins (except fibronectin) and F XIII were extremely low levels for wound healing. Histological analysis of the membrane with dura mater obtained from 13 patients was performed by Abidin-Biotin peroxidase Complex Method. Fibronectin was identified in outer membrane especially in sinusoidal layer. In normal wound healing, fibronectin appears early with the invading fibroblast and disappeares within 5 weeks from injury. But in chronic subdural hematoma it was not disappeares in 8 weeks after the head injury. The fact indicates the neomembrane of the chronic subdural hematoma is not in healing stage. This condition in chronic subdural hematoma is unfavorable for wound healing. Thus, author suspected that in early phase of wound healing after the head injury fibronectin and its related substances may play a role in the formation of chronic subdural hematoma.
 ...
PMID:[Significance of the factors in wound healing for the origin of chronic subdural hematoma--fibronectin and its related substances]. 138 64

Several pathophysiological conditions, including nephrotic syndrome, are characterized by increased renal activity of the epithelial Na(+) channel (ENaC). We recently identified plasmin in nephrotic urine as a stimulator of ENaC activity and undertook this study to investigate the mechanism by which plasmin stimulates ENaC activity. Cy3-labeled plasmin was found to bind to the surface of the mouse cortical collecting duct cell line, M-1. Binding depended on a glycosylphosphatidylinositol (GPI)-anchored protein. Biotin-label transfer showed that plasmin interacted with the GPI-anchored protein prostasin on M-1 cells and that plasmin cleaved prostasin. Prostasin activates ENaC by cleavage of the gamma-subunit, which releases an inhibitory peptide from the extracellular domain. Removal of GPI-anchored proteins from the M-1 cells with phosphatidylinositol-specific phospholipase C (PI-PLC) inhibited plasmin-stimulated ENaC current in monolayers of M-1 cells at low plasmin concentration (1-4 microg/ml). At a high plasmin concentration of 30 microg/ml, there was no difference between cell layers treated with or without PI-PLC. Knockdown of prostasin attenuated binding of plasmin to M1 cells and blocked plasmin-stimulated ENaC current in single M-1 cells, as measured by whole-cell patch clamp. In M-1 cells expressing heterologous FLAG-tagged prostasin, gammaENaC and prostasin were colocalized. A monoclonal antibody directed against the inhibitory peptide of gammaENaC produced specific immunofluorescence labeling of M-1 cells. Pretreatment with plasmin abolished labeling of M-1 cells in a prostasin-dependent way. We conclude that, at low concentrations, plasmin interacts with GPI-anchored prostasin, which leads to cleavage of the gamma-subunit and activation of ENaC, while at higher concentrations, plasmin directly activates ENaC.
 ...
PMID:Prostasin-dependent activation of epithelial Na+ channels by low plasmin concentrations. 1979 56

Plasminogen/plasmin system is involved in such important processes as thrombosis, inflammation and cancer. Plasmin and plasminogen mediate their action through plasminogen-binding proteins on the cell surface. Lys-plasminogen, but not Glu-plasminogen, shows inhibitory effect on platelet aggregation induced by ADP, collagen and thrombin in preparations of both: platelet-rich plasma and washed platelets. We have shown that the kringle domains of Lys-plasminogen mediate interaction of this proenzyme with platelet- surface proteins. The aim of the work is to study the role of certain kringle domains in the inhibitory effect of Lys-plasminogen and to determine possible plasminogen-binding proteins on the platelet surface. All studied plasminogen fragments (K1-3, K4 and K5) abolished the inhibitory effect of Lys-plasminogen on platelet aggregation. We observed that K5 was more effective than K1-3 and K4. Biotin-labeled Lys-plasminogen, Glu-plasminogen and plasminogen fragment K1-3 possessed the highest affinity for actin, whereas the binding of biotin-labeled mini-plasminogen and K4 to actin was negligible. We have suggested that inhibitory effect of Lys-plasminogen is due to the interaction of kringle domains of this proenzyme with membrane-bound proteins which are exposed on the platelet surface during activation and are involved in thrombus formation.
 ...
PMID:Study of the sites of plasminogen molecule which are responsible for inhibitory effect of Lys-plasminogen on platelet aggregation. 2581 91