Source:http://linkedlifedata.com/resource/pubmed/id/17763154
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2007-8-31
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pubmed:abstractText |
Platelet membrane glycoproteins IIb and IIIa form a calcium-dependent heterodimer that plays a key role in platelet adhesion and aggregation. The present objective was to measure the dissociation and reassociation of GPIIb-IIIa by flow cytometric analysis of platelets labelled with mAbs specific for the glycoprotein complex or each monomer. In agreement with previous studies, EDTA chelation of extracellular calcium, [Ca2+]o, dissociated the heterodimer in a time and temperature dependent manner. Agonist stimulation of EDTA-treated platelets induced subunits to reassociate with the following order of potency: thrombin > collagen > ADP. Two-fold increases in GPIIb-IIIa and GPIIb indicate that thrombin caused reassociation of surface subunits and concurrent translocation of complexes from intracellular pools. The latter was partially inhibited by cytochalasin B thus indicating that a subpopulation of GPIIb-IIIa required cytoskeletal remodelling for translocation. Surface GPIIIa as reported by anti-CD61 declined more and upregulated less compared with GPIIb-IIIa or GPIIb. Results suggest that EDTA incubation might have altered the conformation of this epitope and decreased mAb binding. Collagen induced GPIIb-IIIa reassociation but not translocation of cryptic complexes. BAPTA suppression of rises in cytosolic calcium concentration or low [Ca2+]o inhibited GPIIb-IIIa reassociation, thus indicating that this reaction was driven by signal transduction. Thrombin and collagen induced a comparable level of aggregation of EDTA-treated platelets despite a 3-fold difference in cell surface GPIIb-IIIa. It is concluded that the effects of EDTA on GPIIb-IIIa dissociation and loss of adhesive functions are largely but not completely reversible.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/Edetic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Glycoprotein GPIIb-IIIa...,
http://linkedlifedata.com/resource/pubmed/chemical/Thrombin
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0953-7104
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
451-9
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pubmed:meshHeading |
pubmed-meshheading:17763154-Blood Platelets,
pubmed-meshheading:17763154-Calcium,
pubmed-meshheading:17763154-Cells, Cultured,
pubmed-meshheading:17763154-Collagen,
pubmed-meshheading:17763154-Edetic Acid,
pubmed-meshheading:17763154-Humans,
pubmed-meshheading:17763154-Platelet Adhesiveness,
pubmed-meshheading:17763154-Platelet Glycoprotein GPIIb-IIIa Complex,
pubmed-meshheading:17763154-Protein Binding,
pubmed-meshheading:17763154-Protein Transport,
pubmed-meshheading:17763154-Thrombin
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pubmed:year |
2007
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pubmed:articleTitle |
Reassociation and translocation of glycoprotein IIB-IIIA in EDTA-treated human platelets.
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pubmed:affiliation |
The Canadian Blood Services, Edmonton Centre, Edmonton, Alberta, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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