Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.73 (urokinase-type plasminogen activator)
 10,685 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Neutrophils (polymorphonuclear neutrophils [PMNs]) have been implicated as mediators of reperfusion injury. Heparin, urokinase, and ancrod are agents used routinely to prevent and treat thrombosis, yet their effects on PMN function are unknown. Therefore human PMNs were obtained and incubated for 30 minutes with either saline solution or one of the following pharmacologic agents, each tested at three different concentrations: group 1, saline solution (control, n = 14); groups 2 through 4, heparin (5000 units/ml, n = 8; 2500 units/ml, n = 6; and 1250 units/ml, n = 6, respectively); groups 5 through 7, urokinase (50,000 units/ml, n = 8; 25,000 units/ml, n = 6; and 12,500 units/ml, n = 6, respectively), and groups 8 through 10, ancrod (70 units/ml, n = 8; 35 units/ml, n = 6; and 17.5 units/ml, n = 6). Superoxide anion production was measured by the reduction of cytochrome c in a spectrophotometric assay. Chemotaxis was evaluated by the number of PMNs migrating across a filter with a Neuro Probe chamber (Neuro Probe, Cabin John, Md.). Phagocytosis was determined by the ingestion of opsonized zymosan particles by PMNs. Serum obtained from each PMN donor was used both to opsonize the zymosan and as a chemoattractant in the chemotaxis assay. Statistical comparison was evaluated by analysis of variance, and post hoc comparisons for each agent with control were performed with the unpaired Student t test. No agent, at any dose, significantly changed superoxide anion production compared with control cells. All three agents significantly inhibited PMN chemotaxis (p < 0.01). In the control group the number of PMNs counted was 27.6 +/- 4.9.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Heparin, urokinase, and ancrod alter neutrophil function. 132 94

Scavengers of different active oxygen species affect fibrin plate lysis, catalysed by various proteinases, only at relatively high concentrations (> 10(-2) M). Singlet oxygen scavengers change proteinase activity insignificantly except for strong inhibition of pepsin and papain by sodium azide, but pepsin-by histidine, and fibrinolytic urokinase activity-by all used O2 delta 1 scavengers. Of all used scavengers of OH-radical only ethanol caused significant changes in the proteinases under study, except for alpha-chymotrypsin. The most strong inhibitory effect on proteinase activity was demonstrated by scavengers of superoxide radical. Thus, nitrotetrazolium blue strongly inhibited the activity of plasmin, urokinase (fibrinolytic activity), papain and pepsin. Catalase changed proteinase activity insignificantly, though it leads to total inhibition of pepsin activity at final 4.5 x 10(-4) M concentration. These facts and our previous findings on generating of active oxygen species by proteinases give us grounds to suppose that minor active oxygen species, endogenous for the "proteinase-substrate" system, can participate in the catalytic function of some proteinases.
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PMID:Effect of active oxygen species scavengers on fibrinolytic activity of some proteinases. 874 26

Urokinase stimulates the production of superoxide radical in cultured aortal smooth muscle cells simultaneously with activation of the expression of NAD(F)H-oxidases nox1, nox4, and phox22. Antioxidant ebselen abolishes the stimulating effect of urokinase on smooth muscle cell proliferation. The data showed that urokinase can potentiate oxidative stress in the arterial wall and can play an important role in the development of adverse arterial remodeling.
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PMID:Urokinase induces ROS production in vascular smooth muscle cells. 1742 35