Source:http://linkedlifedata.com/resource/pubmed/id/11038351
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
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| pubmed:dateCreated |
2001-3-6
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| pubmed:abstractText |
Although glycoprotein Ia/IIa (GPIa/IIa, integrin alpha(2)beta(1)) has established its role as a collagen receptor, it remains unclear whether GPIa/IIa mediates activation signals. In this study, we show that rhodocytin, purified from the Calloselasma rhodostoma venom, induces platelet aggregation, which can be blocked by anti-GPIa monoclonal antibodies. Studies with rhodocytin-coupled beads and liposomes loaded with recombinant GPIa/IIa demonstrated that rhodocytin directly binds to GPIa/IIa independently of divalent cations. In vitro kinase assays and Western blotting of GPIa immunoprecipitates revealed that Src and Lyn constitutively associate with GPIa/IIa and that Src activity increases transiently after rhodocytin stimulation. Src specifically associates with p130 Crk-associated substrate (Cas) in a manner dependent upon Cas phosphorylation, suggesting that Src is responsible for Cas tyrosine phosphorylation. While all these phenomena occur early after rhodocytin stimulation in a cAMP-resistant manner, tyrosine phosphorylation of Syk and phospholipase Cgamma2, intracellular Ca(2+) mobilization, and platelet aggregation occur later in a cAMP-sensitive manner. Cytochalasin D, which interferes with actin polymerization and blocks receptor clustering, inhibits all the rhodocytin-mediated signals we examined in this study. We suggest that rhodocytin, by clustering GPIa/IIa, activates GPIa/IIa-associated Src, which then mediates downstream activation signals.
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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/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Blood Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Dinoprostone,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins, C-Type,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Collagen,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, IgG,
http://linkedlifedata.com/resource/pubmed/chemical/Tyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Viper Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/rhodocytin protein, Calloselasma...
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| pubmed:status |
MEDLINE
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| pubmed:month |
Jan
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| pubmed:issn |
0021-9258
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
12
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| pubmed:volume |
276
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
1643-52
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11038351-Animals,
pubmed-meshheading:11038351-Antibodies, Monoclonal,
pubmed-meshheading:11038351-Blood Platelets,
pubmed-meshheading:11038351-Blood Proteins,
pubmed-meshheading:11038351-Dinoprostone,
pubmed-meshheading:11038351-Humans,
pubmed-meshheading:11038351-Integrins,
pubmed-meshheading:11038351-Kinetics,
pubmed-meshheading:11038351-Lectins,
pubmed-meshheading:11038351-Lectins, C-Type,
pubmed-meshheading:11038351-Mice,
pubmed-meshheading:11038351-Mice, Inbred C57BL,
pubmed-meshheading:11038351-Phosphorylation,
pubmed-meshheading:11038351-Phosphotyrosine,
pubmed-meshheading:11038351-Platelet Adhesiveness,
pubmed-meshheading:11038351-Platelet Aggregation,
pubmed-meshheading:11038351-Receptors, Collagen,
pubmed-meshheading:11038351-Receptors, IgG,
pubmed-meshheading:11038351-Tyrosine,
pubmed-meshheading:11038351-Viper Venoms,
pubmed-meshheading:11038351-Viperidae
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| pubmed:year |
2001
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| pubmed:articleTitle |
Rhodocytin induces platelet aggregation by interacting with glycoprotein Ia/IIa (GPIa/IIa, Integrin alpha 2beta 1). Involvement of GPIa/IIa-associated src and protein tyrosine phosphorylation.
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| pubmed:affiliation |
Department of Clinical and Laboratory Medicine, Yamanashi Medical University, Yamanashi 409-3898, Japan.
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| pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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