| pubmed-article:8103046 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8103046 | lifeskim:mentions | umls-concept:C0205102 | lld:lifeskim |
| pubmed-article:8103046 | lifeskim:mentions | umls-concept:C0016017 | lld:lifeskim |
| pubmed-article:8103046 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:8103046 | lifeskim:mentions | umls-concept:C2349975 | lld:lifeskim |
| pubmed-article:8103046 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
| pubmed-article:8103046 | lifeskim:mentions | umls-concept:C0086987 | lld:lifeskim |
| pubmed-article:8103046 | pubmed:issue | 25 | lld:pubmed |
| pubmed-article:8103046 | pubmed:dateCreated | 1993-9-30 | lld:pubmed |
| pubmed-article:8103046 | pubmed:abstractText | The activation of plasminogen at the surface of fibrin by single-chain urokinase-type plasminogen activator (scu-PA) was investigated using recombinant forms of a plasmin-resistant mutant of scu-PA, rscu-PA-Glu158, and an inactive catalytic site mutant of human plasminogen, rPg-Ala741. Conversion of cleavable 125I-labeled single-chain proteins to their two-chain forms, was quantitated by radioisotope counting of protein bands on reduced SDS-polyacrylamide gels. The efficiency of the activation (moles of plasmin generated per mol of plasminogen activator) of native Glu-plasminogen bound to degraded fibrin was comparable for scu-PA and its two-chain form (tcu-PA) and approximately 4-fold lower for rscu-PA-Glu158. The corresponding values with rPg-Ala741 were 4-fold or 9-fold lower for scu-PA or rscu-PA-Glu158, as compared to tcu-PA. In contrast, in solution in the absence of fibrin, the efficiency of scu-PA for activation of rPg-Ala741 was 100-fold lower than that of tcu-PA. Initial activation rates of rPg-Ala741 (32.7 fmol/well containing 50 microliters of solution) with 4 nM tcu-PA were comparable in solution and bound to degraded fibrin (v(o) = 1.01 and 1.16 fmol/min, respectively). In contrast, with 4 nM scu-PA the corresponding values when rPg-Ala741 was bound to degraded fibrin were 20-fold higher as compared to the soluble phase (v(o) = 0.23 and 0.012 fmol/min, respectively). Comparable results were obtained when using Glu- or Lys-forms of rPg-Ala741. Furthermore, in the presence of normal human plasma, activation of Glu-plasminogen bound to degraded fibrin was found to be about 2.5-fold more efficient with scu-PA than with tcu-PA. These findings indicate that the fibrin specificity of scu-PA does not require its conversion to tcu-PA, nor conversion of Glu- to Lys-plasminogen, but appears to be due to the additional binding of plasminogen to partially digested fibrin; scu-PA may thus represent a physiological functional form of u-PA in plasma. | lld:pubmed |
| pubmed-article:8103046 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8103046 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8103046 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8103046 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8103046 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8103046 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8103046 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8103046 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8103046 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8103046 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8103046 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8103046 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8103046 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8103046 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8103046 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8103046 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:8103046 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8103046 | pubmed:author | pubmed-author:LijnenH RHR | lld:pubmed |
| pubmed-article:8103046 | pubmed:author | pubmed-author:Anglés-CanoEE | lld:pubmed |
| pubmed-article:8103046 | pubmed:author | pubmed-author:FleuryVV | lld:pubmed |
| pubmed-article:8103046 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8103046 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:8103046 | pubmed:volume | 268 | lld:pubmed |
| pubmed-article:8103046 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8103046 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8103046 | pubmed:pagination | 18554-9 | lld:pubmed |
| pubmed-article:8103046 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:8103046 | pubmed:meshHeading | pubmed-meshheading:8103046-... | lld:pubmed |
| pubmed-article:8103046 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8103046 | pubmed:articleTitle | Mechanism of the enhanced intrinsic activity of single-chain urokinase-type plasminogen activator during ongoing fibrinolysis. | lld:pubmed |
| pubmed-article:8103046 | pubmed:affiliation | Institut National de la Santé et de la Recherche Médicale U.143, Hôpital de Bicêtre, France. | lld:pubmed |
| pubmed-article:8103046 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8103046 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8103046 | lld:pubmed |
