| pubmed-article:3383851 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3383851 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:3383851 | lifeskim:mentions | umls-concept:C0005821 | lld:lifeskim |
| pubmed-article:3383851 | lifeskim:mentions | umls-concept:C0005456 | lld:lifeskim |
| pubmed-article:3383851 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:3383851 | lifeskim:mentions | umls-concept:C0017052 | lld:lifeskim |
| pubmed-article:3383851 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:3383851 | pubmed:dateCreated | 1988-8-4 | lld:pubmed |
| pubmed-article:3383851 | pubmed:abstractText | The interaction of thrombin with proteins at the platelet surface was assessed by chemical cross-linking with the membrane-impermeable reagents bis(sulphosuccinimidyl)suberate and dithiobis(sulphosuccinimidyl propionate) under conditions which induced no modification of intracellular proteins and minimal cross-linking of membrane glycoproteins. The proteins covalently linked to 125I-labelled alpha and gamma-thrombin were analyzed by sodium dodecyl sulfate/polyacrylamide gel electrophoresis and crossed immunoelectrophoresis. 125I-alpha-thrombin was detected in high-molecular-mass complexes (a) at the top of a 3% acrylamide stacking gel and (b) with a Mr approximately equal to 400,000. In addition, two complexes of 240 kDa and 78 kDa were characterized. Hirudin prevented the formation of each of these complexes. The 78-kDa complex occurred spontaneously in the absence of bifunctional reagents, was only observed with active alpha-thrombin and was not dissociated by hirudin. Such characteristics are similar to those of a serpin serine-protease complex. The 240-kDa complex was formed with 0.8-100 nM alpha-thrombin, was observed after a short incubation time (30 s) and occurred with TosLysCH2Cl-inactivated alpha-thrombin. After analysis of Triton-X-100-soluble extracts of cross-linked platelets by crossed immunoelectrophoresis against a rabbit antiserum to platelets, two principal precipitates contained 125I-alpha-thrombin. These were a precipitate containing GPIIb-IIIa complexes and a precipitate in the position of GPIb. Indirect immunoprecipitation of GPIb, using a murine monoclonal antibody, confirmed it to be the major platelet component in the 240-kDa complex. Significantly, 125I-gamma-thrombin, which activates platelets with a prolonged lag phase, failed to bind to GPIb and complexes in the 240-kDa and 78-kDa molecular mass range were not observed. We conclude that several binding sites for alpha-thrombin are present at the platelet surface, and that GPIb is one of them. The studies with gamma-thrombin suggest that binding to GPIb is not obligatory for platelet activation although it could be involved in an initial step of the platelet response. | lld:pubmed |
| pubmed-article:3383851 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3383851 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3383851 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3383851 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3383851 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3383851 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3383851 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3383851 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3383851 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:3383851 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:3383851 | pubmed:author | pubmed-author:GuillinM CMC | lld:pubmed |
| pubmed-article:3383851 | pubmed:author | pubmed-author:NurdenA TAT | lld:pubmed |
| pubmed-article:3383851 | pubmed:author | pubmed-author:Jandrot-Perru... | lld:pubmed |
| pubmed-article:3383851 | pubmed:author | pubmed-author:DidryDD | lld:pubmed |
| pubmed-article:3383851 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3383851 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:3383851 | pubmed:volume | 174 | lld:pubmed |
| pubmed-article:3383851 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3383851 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3383851 | pubmed:pagination | 359-67 | lld:pubmed |
| pubmed-article:3383851 | pubmed:dateRevised | 2007-7-23 | lld:pubmed |
| pubmed-article:3383851 | pubmed:meshHeading | pubmed-meshheading:3383851-... | lld:pubmed |
| pubmed-article:3383851 | pubmed:meshHeading | pubmed-meshheading:3383851-... | lld:pubmed |
| pubmed-article:3383851 | pubmed:meshHeading | pubmed-meshheading:3383851-... | lld:pubmed |
| pubmed-article:3383851 | pubmed:meshHeading | pubmed-meshheading:3383851-... | lld:pubmed |
| pubmed-article:3383851 | pubmed:meshHeading | pubmed-meshheading:3383851-... | lld:pubmed |
| pubmed-article:3383851 | pubmed:meshHeading | pubmed-meshheading:3383851-... | lld:pubmed |
| pubmed-article:3383851 | pubmed:meshHeading | pubmed-meshheading:3383851-... | lld:pubmed |
| pubmed-article:3383851 | pubmed:meshHeading | pubmed-meshheading:3383851-... | lld:pubmed |
| pubmed-article:3383851 | pubmed:meshHeading | pubmed-meshheading:3383851-... | lld:pubmed |
| pubmed-article:3383851 | pubmed:meshHeading | pubmed-meshheading:3383851-... | lld:pubmed |
| pubmed-article:3383851 | pubmed:year | 1988 | lld:pubmed |
| pubmed-article:3383851 | pubmed:articleTitle | Cross-linking of alpha and gamma-thrombin to distinct binding sites on human platelets. | lld:pubmed |
| pubmed-article:3383851 | pubmed:affiliation | Laboratoire de Recherche sur l'Hémostase et la Thrombose, Faculté Xavier Bichat, Paris, France. | lld:pubmed |
| pubmed-article:3383851 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3383851 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3383851 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3383851 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3383851 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3383851 | lld:pubmed |
