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 proteolytic activity of plasmin on soluble caprine beta-casein (CN) was studied in 50 mM Tris.HCI buffer, pH 8.0, at 37 degrees C. Electrophoretic studies showed that hydrolysis of this protein results in an electrophoretic pattern that is similar to the pattern obtained from plasmin hydrolysis of bovine beta-CN (gamma-CN and complementary N-terminal fragments), suggesting that plasmin probably attacks the same regions that are susceptible to cleavage in bovine beta-CN. As determined by SDS-PAGE, the gamma-like components of caprine milk consisted of two fragments with relative molecular mass of 9200 and two with relative molecular mass of 21,400 that could differ in the level of phosphorylation. Apparently, the high molecular mass components are homologous to bovine beta-CN (f 29-209) (gamma 1-CN), and the low molecular mass components are homologous to bovine beta-CN (f 106-209) and beta-CN (f 108-209) (gamma 2- and gamma 3-CN). Complementary N-terminal fragments had values for molecular masses in the range 13,600 to 8500 and urea-PAGE patterns that were more complex than those obtained in bovine casein because of the different phosphorylation levels in caprine beta-CN. These fragments were also present in the hydrolysate of whole caprine casein that had been treated with plasmin.
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PMID:Hydrolysis of caprine beta-casein by plasmin. 936 Nov 97

Membrane binding of urokinase type plasminogen activator (u-PA) is thought to play a pivotal role in connective tissue remodeling and invasive processes. We compare the ability of different matrix-metalloproteinases involved in connective tissue turnover to cleave pro-urokinase type plasminogen activator between the catalytic domain and the receptor binding part to investigate a potential role for matrix-metalloproteinases in the regulation of membrane-associated proteolytic activity. We employed several forms of human stromelysin-1 (full length, C-truncated, and recombinant catalytic domain), rabbit C-truncated stromelysin-1, the human gelatinases A and B and the human catalytic domain of neutrophil collagenase. The gelatinases and the collagenase did not separate the receptor binding domain of pro-urokinase type plasminogen activator from the catalytic domain, whereas all stromelysin-1 forms cleaved the glutamic acid 143-leucine 144 bond of pro-urokinase type plasminogen activator. This reaction could be inhibited by specific inhibitors of matrix metalloproteinases and was not affected by inhibitors of serine proteinases. The M(r) 31000 cleavage product with leucine 144 as N-terminus displayed no proteolytic activity towards the pro-urokinase type plasminogen activator substrate pyroGlu-Gly-Arg-pNA-HCI (S2444), but it could be activated by an additional treatment with plasmin. Comparison between full length stromelysin-1 and its C-truncated forms, showed that both exhibited the same cleavage properties towards pro-urokinase type plasminogen activator. Thus, the cleavage of pro-urokinase type plasminogen activator by stromelysin-1 is not influenced by the presence or absence of the C-terminal domain. The recombinant catalytic domain of MMP-3 generated pro-urokinase type plasminogen activator, whereas incubation of pro-urokinase type plasminogen activator with the native forms of human or rabbit stromelysin-1 led to a moderate activation of pro-uPA due to an additional cleavage that is catalyzed by a serine proteinase.
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PMID:The cleavage of pro-urokinase type plasminogen activator by stromelysin-1. 980 93