rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2000-11-27
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pubmed:abstractText |
Shear-induced binding of von Willebrand factor (vWf) to the platelet glycoprotein (GP) Ib/V/IX complex plays a key role in initiating platelet adhesion and aggregation at sites of vascular injury. This study demonstrated that pretreating human platelets with inhibitors of actin polymerization, cytochalasin D or latrunculin B, dramatically enhances platelet aggregation induced by vWf. The effects of these inhibitors were specific to the vWf-GPIbalpha interaction because they enhanced vWf-induced aggregation of Glanzmann thrombasthenic platelets and Chinese hamster ovary (CHO) cells transfected with GPIb/V/IX. Moreover, cytochalasin D enhanced the extent of platelet aggregation induced by high shear stress (5000 s(-1)) and also lowered the shear threshold required to induce aggregation from 3000 s(-1) to as low as 500 s(-1). Studies of CHO cells expressing GPIbalpha cytoplasmic tail truncation mutants that failed to bind actin-binding protein-280 (deletion of residues 569-610 or 535-568) demonstrated that the linkage between GPIb and actin-binding protein-280 was not required for vWf-induced actin polymerization, but was critical for the enhancing effects of cytochalasin D on vWf-induced cell aggregation. Taken together, these studies suggest a fundamentally important role for the cytoskeleton in regulating the adhesive function of GPIb/V/IX.
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pubmed:language |
eng
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pubmed:journal |
|
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Alprostadil,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Bicyclo Compounds, Heterocyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochalasin D,
http://linkedlifedata.com/resource/pubmed/chemical/Depsipeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides, Cyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Aggregation Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Glycoprotein GPIIb-IIIa...,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Glycoprotein GPIb-IX...,
http://linkedlifedata.com/resource/pubmed/chemical/Thiazoles,
http://linkedlifedata.com/resource/pubmed/chemical/Thiazolidines,
http://linkedlifedata.com/resource/pubmed/chemical/jasplakinolide,
http://linkedlifedata.com/resource/pubmed/chemical/latrunculin B,
http://linkedlifedata.com/resource/pubmed/chemical/von Willebrand Factor
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0006-4971
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pubmed:author |
pubmed-author:CranmerS LSL,
pubmed-author:DopheideS MSM,
pubmed-author:DunstanD EDE,
pubmed-author:GiulianiMM,
pubmed-author:HarperII,
pubmed-author:JacksonS PSP,
pubmed-author:LanzaFF,
pubmed-author:ManginPP,
pubmed-author:MistryNN,
pubmed-author:SalemH HHH,
pubmed-author:YubaKK
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
96
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3480-9
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:11071645-Actin Cytoskeleton,
pubmed-meshheading:11071645-Actins,
pubmed-meshheading:11071645-Adenosine Diphosphate,
pubmed-meshheading:11071645-Alprostadil,
pubmed-meshheading:11071645-Animals,
pubmed-meshheading:11071645-Antibodies, Monoclonal,
pubmed-meshheading:11071645-Bicyclo Compounds, Heterocyclic,
pubmed-meshheading:11071645-Blood Platelets,
pubmed-meshheading:11071645-CHO Cells,
pubmed-meshheading:11071645-Cricetinae,
pubmed-meshheading:11071645-Cytochalasin D,
pubmed-meshheading:11071645-Cytoskeleton,
pubmed-meshheading:11071645-Depsipeptides,
pubmed-meshheading:11071645-Humans,
pubmed-meshheading:11071645-Mutagenesis, Site-Directed,
pubmed-meshheading:11071645-Peptides, Cyclic,
pubmed-meshheading:11071645-Platelet Aggregation,
pubmed-meshheading:11071645-Platelet Aggregation Inhibitors,
pubmed-meshheading:11071645-Platelet Glycoprotein GPIIb-IIIa Complex,
pubmed-meshheading:11071645-Platelet Glycoprotein GPIb-IX Complex,
pubmed-meshheading:11071645-Stress, Mechanical,
pubmed-meshheading:11071645-Thiazoles,
pubmed-meshheading:11071645-Thiazolidines,
pubmed-meshheading:11071645-Thrombasthenia,
pubmed-meshheading:11071645-Transfection,
pubmed-meshheading:11071645-von Willebrand Factor
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pubmed:year |
2000
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pubmed:articleTitle |
Cytoskeletal regulation of the platelet glycoprotein Ib/V/IX-von willebrand factor interaction.
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pubmed:affiliation |
Department of Medicine, Australian Centre for Blood Diseases, Monash Medical School, Victoria, Australia.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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