pubmed-article:3101672 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3101672 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:3101672 | lifeskim:mentions | umls-concept:C0005821 | lld:lifeskim |
pubmed-article:3101672 | lifeskim:mentions | umls-concept:C0016006 | lld:lifeskim |
pubmed-article:3101672 | lifeskim:mentions | umls-concept:C0085862 | lld:lifeskim |
pubmed-article:3101672 | lifeskim:mentions | umls-concept:C1299583 | lld:lifeskim |
pubmed-article:3101672 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
pubmed-article:3101672 | lifeskim:mentions | umls-concept:C0032172 | lld:lifeskim |
pubmed-article:3101672 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
pubmed-article:3101672 | lifeskim:mentions | umls-concept:C1608386 | lld:lifeskim |
pubmed-article:3101672 | lifeskim:mentions | umls-concept:C1549571 | lld:lifeskim |
pubmed-article:3101672 | lifeskim:mentions | umls-concept:C0441712 | lld:lifeskim |
pubmed-article:3101672 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:3101672 | pubmed:dateCreated | 1987-3-26 | lld:pubmed |
pubmed-article:3101672 | pubmed:abstractText | When human platelets are incubated with 500 nM-PAF-acether (platelet-activating factor. 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine) under equilibrium conditions (60 min, 22 degrees C, non-stirred suspensions), two classes of fibrinogen binding sites are exposed: one class with a high affinity [Kd (7.2 +/- 2.1) X 10(-8) M, 2367 +/- 485 sites/platelet, n = 9] and one class with a low affinity [Kd (5.9 +/- 2.4) X 10(-7) M, 26972 +/- 8267 sites/platelet]. Preincubation with inhibitors of cyclo-oxygenase (acetylsalicylic acid, indomethacin) or thromboxane synthetase (UK 38.485) completely abolishes high-affinity binding, leaving low-affinity binding unchanged. In contrast, ADP scavengers (phosphocreatine/creatine kinase or phosphoenol pyruvate/pyruvate kinase) completely prevent low-affinity binding, leaving high-affinity binding unaltered. Initial binding studies (2-10 min incubation) confirm these findings with a major part of the binding being sensitive to ADP scavengers, a minor part sensitive to indomethacin and complete blockade with both inhibitors. Increasing the temperature to 37 degrees C decreases the number of low affinity-binding sites 6-fold without changing high-affinity binding. Aggregation, measured as the rate of single platelet disappearance, then depends on high-affinity binding at 10 nM-fibrinogen or less, whereas at 100 nM-fibrinogen or more low-affinity binding becomes predominant. These findings point at considerable platelet activation during binding experiments. However, arachidonate metabolism [( 3H]arachidonate mobilization and thromboxane synthesis) and secretion [( 14C]serotonin and beta-thromboglobulin) are about 10% or less of the amounts found under optimal conditions (5 units of thrombin/ml 37 degrees C, stirring). We conclude that PAF-acether induces little platelet activation under binding conditions. The amounts of thromboxane A2 and secreted ADP, however, are sufficient for initiating high- and low-affinity fibrinogen binding via mutually independent mechanisms. | lld:pubmed |
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pubmed-article:3101672 | pubmed:language | eng | lld:pubmed |
pubmed-article:3101672 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3101672 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:3101672 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3101672 | pubmed:month | Dec | lld:pubmed |
pubmed-article:3101672 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:3101672 | pubmed:author | pubmed-author:AkkermanJ WJW | lld:pubmed |
pubmed-article:3101672 | pubmed:author | pubmed-author:KloproggeEE | lld:pubmed |
pubmed-article:3101672 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3101672 | pubmed:day | 1 | lld:pubmed |
pubmed-article:3101672 | pubmed:volume | 240 | lld:pubmed |
pubmed-article:3101672 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3101672 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3101672 | pubmed:pagination | 403-12 | lld:pubmed |
pubmed-article:3101672 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:3101672 | pubmed:year | 1986 | lld:pubmed |
pubmed-article:3101672 | pubmed:articleTitle | Platelet-activating factor (PAF-acether) induces high- and low-affinity binding of fibrinogen to human platelets via independent mechanisms. | lld:pubmed |
pubmed-article:3101672 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3101672 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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