| pubmed-article:10887121 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10887121 | lifeskim:mentions | umls-concept:C0031621 | lld:lifeskim |
| pubmed-article:10887121 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:10887121 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
| pubmed-article:10887121 | lifeskim:mentions | umls-concept:C0032195 | lld:lifeskim |
| pubmed-article:10887121 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:10887121 | pubmed:dateCreated | 2000-8-17 | lld:pubmed |
| pubmed-article:10887121 | pubmed:abstractText | The binding of von Willebrand factor (vWF) to glycoprotein (GP) Ib-IX-V stimulates transmembrane signaling events that lead to platelet adhesion and aggregation. Recent studies have revealed that the signaling protein 14-3-3 zeta binds directly to the cytoplasmic domain of GP Ib alpha. In this study, the dynamic association of 14-3-3 zeta with GP Ib-IX, the phosphoinositide 3-kinase (PI 3-kinase), or both, was investigated in resting, thrombin, or vWF and botrocetin-stimulated platelets by analysis of discrete subcellular fractions. Results of this study demonstrate maximal coimmunoprecipitation of 14-3-3 zeta with GP Ib-IX in the nonstimulated cytosolic fraction and in the actin cytoskeletal fraction of thrombin- or vWF-stimulated human platelets. Immunoprecipitated 14-3-3 zeta or GP Ib from cytosolic fractions contained PI 3-kinase enzyme activity and an 85-kd polypeptide recognized by antibodies to the p85 subunit of PI 3-kinase. After platelet activation, the level of association between these species decreased in the cytosolic fraction. However, increased complex formation between 14-3-3 zeta and GP Ib-IX and between PI 3-kinase and GP Ib-IX was detected in actin cytoskeletal fractions derived from thrombin- or vWF-stimulated platelets. Recombinant glutathione S-transferase-14-3-3 zeta fusion protein (14-3-3 zeta-GST) inhibited affinity-captured PI 3-kinase enzyme activity up to 70% at 2 mcmol/L 14-3-3 zeta-GST. However, increasing concentrations up to 5 mcmol/L 14-3-3 zeta-GST resulted in the 3-fold enhancement of PI 3-kinase enzyme activity. We propose that the association between PI 3-kinase and 14-3-3 zeta with GP Ib-IX serves to promote the rapid translocation of these signaling proteins to the activated cytoskeleton, thereby regulating the formation of 3-position phosphoinositide-signaling molecules in this subcellular compartment. (Blood. 2000;96:577-584) | lld:pubmed |
| pubmed-article:10887121 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10887121 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10887121 | pubmed:citationSubset | AIM | lld:pubmed |
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| pubmed-article:10887121 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10887121 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:10887121 | pubmed:issn | 0006-4971 | lld:pubmed |
| pubmed-article:10887121 | pubmed:author | pubmed-author:MitchellC ACA | lld:pubmed |
| pubmed-article:10887121 | pubmed:author | pubmed-author:BerndtM CMC | lld:pubmed |
| pubmed-article:10887121 | pubmed:author | pubmed-author:MundayA DAD | lld:pubmed |
| pubmed-article:10887121 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10887121 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:10887121 | pubmed:volume | 96 | lld:pubmed |
| pubmed-article:10887121 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10887121 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10887121 | pubmed:pagination | 577-84 | lld:pubmed |
| pubmed-article:10887121 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:10887121 | pubmed:year | 2000 | lld:pubmed |
| pubmed-article:10887121 | pubmed:articleTitle | Phosphoinositide 3-kinase forms a complex with platelet membrane glycoprotein Ib-IX-V complex and 14-3-3zeta. | lld:pubmed |
| pubmed-article:10887121 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, Australia. | lld:pubmed |
| pubmed-article:10887121 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10887121 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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