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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
1993-8-3
|
| pubmed:abstractText |
Activation of blood fibrinolysis is initiated by the activation of plasminogen to plasmin by plasminogen activator (PA). The plasmin thus produced can degrade fibrin, the main component of thrombus. Tissue-type PA (t-PA) which is mainly secreted from vascular endothelial cells possesses a high affinity for fibrin in contrast to urokinase-type PA (u-PA). Enzymatic activity of t-PA is expressed in either single-chain form or two-chain form. Further, t-PA activity enhanced markedly in the presence of fibrin; 600-1,000-fold increase. Thus, the thrombolytic therapy is now being performed by using t-PA. The mechanism for thrombolysis by t-PA involves the activation of fibrinolytic system on the fibrin surface. The kringle 2 domain of t-PA molecule plays an important role on the binding to fibrin. But in single-chain t-PA, finger domain plays a role for its binding to fibrin. Recent studies have revealed that the t-PA specific receptor (t-PAR) is expressed on the endothelial cells which localizes t-PA activity by fixing t-PA around the cells.
|
| pubmed:language |
jpn
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jun
|
| pubmed:issn |
0047-1852
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
51
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1620-6
|
| pubmed:dateRevised |
2011-7-27
|
| pubmed:meshHeading | |
| pubmed:year |
1993
|
| pubmed:articleTitle |
[Molecular biology of tissue-type plasminogen activator (t-PA) and clinical application of recombinant t-PA].
|
| pubmed:affiliation |
Department of Physiology, Kinki University School of Medicine.
|
| pubmed:publicationType |
Journal Article,
English Abstract,
Review
|