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

The urinary kallikrein activity (KA) was measured to investigate its significance in the renal diseases by using tosyl-arginine methyl ester (TAME) as a substrate. The examinees were 94 patients with renal diseases and 25 normal persons. The daily urinary kallikrein excretion (KE, KE=KAxdaily urinary volume) is less in chronic glomerulonephritis and outstandingly less in chronic renal failure than in the normal controls. The KE also shows a positive correlation moderately to 15-min PSP excretion and relatively to creatinine clearance. KE is closely related to renal function and decreases with the degree of renal damage. KA has no relation to the concentration of urine protein, but it was parallel, in general, to the urokinase activity. In nephrotic syndrome, KA tends to show a negative correlation to the urinary alpha 1-antitrypsin. alpha 1-antitrypsin may have a function as an inhibitor to the urinary kallikrein.
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PMID:A clinical study on urinary kallikrein in patients with renal diseases. 51 49

Many serine proteases play important regulatory roles in complex biological systems, but only a few have been linked directly with capillary morphogenesis and angiogenesis. Here we provide evidence that serine protease activities, independent of the plasminogen activation cascade, are required for microvascular endothelial cell reorganization and capillary morphogenesis in vitro. A homology cloning approach targeting conserved motifs present in all serine proteases, was used to identify candidate serine proteases involved in these processes, and revealed 5 genes (acrosin, testisin, neurosin, PSP and neurotrypsin), none of which had been associated previously with expression in endothelial cells. A subsequent gene-specific RT-PCR screen for 22 serine proteases confirmed expression of these 5 genes and identified 7 additional serine protease genes expressed by human endothelial cells, urokinase-type plasminogen activator, protein C, TMPRSS2, hepsin, matriptase/MT-SP1, dipeptidylpeptidase IV, and seprase. Differences in serine protease gene expression between microvascular and human umbilical vein endothelial cells (HUVECs) were identified and several serine protease genes were found to be regulated by the nature of the substratum, ie. artificial basement membrane or fibrillar type I collagen. mRNA transcripts of several serine protease genes were associated with blood vessels in vivo by in situ hybridization of human tissue specimens. These data suggest a potential role for serine proteases, not previously associated with endothelium, in vascular function and angiogenesis.
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PMID:Endothelial cell serine proteases expressed during vascular morphogenesis and angiogenesis. 1262 42