| pubmed-article:10610687 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10610687 | lifeskim:mentions | umls-concept:C0030940 | lld:lifeskim |
| pubmed-article:10610687 | lifeskim:mentions | umls-concept:C1257901 | lld:lifeskim |
| pubmed-article:10610687 | lifeskim:mentions | umls-concept:C0680730 | lld:lifeskim |
| pubmed-article:10610687 | lifeskim:mentions | umls-concept:C1511790 | lld:lifeskim |
| pubmed-article:10610687 | lifeskim:mentions | umls-concept:C1149593 | lld:lifeskim |
| pubmed-article:10610687 | lifeskim:mentions | umls-concept:C1510438 | lld:lifeskim |
| pubmed-article:10610687 | lifeskim:mentions | umls-concept:C1148554 | lld:lifeskim |
| pubmed-article:10610687 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:10610687 | pubmed:dateCreated | 2000-4-18 | lld:pubmed |
| pubmed-article:10610687 | pubmed:abstractText | This paper describes the development of galactosidase protease-activated receptor (GPAR) as a recombinant protein obtained by fusion of beta-galactosidase, the extracellular domains of protease-activated receptors (PARs), and a biotin acceptor domain. Used as an immobilized substrate, this protein allows the detection of thrombin in the sub-picomolar range. A comparative analysis for proteolytic cleavage of murine PAR1, PAR2, and PAR3 and human PAR4 was performed, involving mutated and nonmutated GPAR fusion proteins. Thrombin cleaved GPAR1 (2.6 mol(beta-galactosidase)/(mol(thrombin) * min)), GPAR3 (410 mmol(beta-galactosidase)/(mol(thrombin) * min)), and GPAR4 (4.3 mmol(beta-galactosidase)/(mol(thrombin) * min)) specifically at the proteolytic activation site. A second possible cleavage site for thrombin is present in murine PAR1 and PAR3. Trypsin and plasmin cleaved all receptor fusion proteins with little specificity for the activation site, except for a marked preference of trypsin for cleavage at the activation site of GPAR2. Chymotrypsin cleaves GPAR1 at a rate (58 mmol(beta-galactosidase)/(mol(thrombin) * min)) that suggests the possibility of chymotryptic inactivation of PAR1. Elastase may inactivate PAR1 and PAR3, but probably not PAR2 and PAR4. Neither activated protein C nor the plasminogen activators cleave any GPAR fusion protein at considerable rates. | lld:pubmed |
| pubmed-article:10610687 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10610687 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10610687 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10610687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10610687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10610687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10610687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10610687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10610687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10610687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10610687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10610687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10610687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10610687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10610687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10610687 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10610687 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10610687 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:10610687 | pubmed:issn | 0003-2697 | lld:pubmed |
| pubmed-article:10610687 | pubmed:author | pubmed-author:MonardDD | lld:pubmed |
| pubmed-article:10610687 | pubmed:author | pubmed-author:AltroggeL MLM | lld:pubmed |
| pubmed-article:10610687 | pubmed:copyrightInfo | Copyright 2000 Academic Press. | lld:pubmed |
| pubmed-article:10610687 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10610687 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:10610687 | pubmed:volume | 277 | lld:pubmed |
| pubmed-article:10610687 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10610687 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10610687 | pubmed:pagination | 33-45 | lld:pubmed |
| pubmed-article:10610687 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:10610687 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10610687 | pubmed:articleTitle | An assay for high-sensitivity detection of thrombin activity and determination of proteases activating or inactivating protease-activated receptors. | lld:pubmed |
| pubmed-article:10610687 | pubmed:affiliation | Friedrich Miescher-Institut, Postfach 2543, Basel, CH-4002, Switzerland. | lld:pubmed |
| pubmed-article:10610687 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10610687 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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