| pubmed-article:7772046 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7772046 | lifeskim:mentions | umls-concept:C0025255 | lld:lifeskim |
| pubmed-article:7772046 | lifeskim:mentions | umls-concept:C0086045 | lld:lifeskim |
| pubmed-article:7772046 | lifeskim:mentions | umls-concept:C0059249 | lld:lifeskim |
| pubmed-article:7772046 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:7772046 | lifeskim:mentions | umls-concept:C1145667 | lld:lifeskim |
| pubmed-article:7772046 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:7772046 | pubmed:dateCreated | 1995-7-5 | lld:pubmed |
| pubmed-article:7772046 | pubmed:abstractText | Annexins are a family of calcium-binding proteins that have been implicated in a wide range of intracellular processes. We have previously reported that stimulation of platelets with thrombin can induce the association of intracellular annexin V with membranes in two distinct ways. First, in such a way that it can be eluted from the membrane with EGTA and secondly in a manner such that it is tightly bound to the membrane and requires the non-ionic detergent Triton X-100 for its solubilization. We report that exposure of platelets to the calcium ionophore A23187 mimics the relocation induced by stimulation with thrombin. In separate experiments we demonstrate that a calcium ion concentration [Ca2+] of 0.8 microM is sufficient for maximum binding of the EGTA-resistant form to membranes. In contrast a higher [Ca2+] was required to induce maximal binding of the annexin V which could be extracted with EGTA. We demonstrate that following temperature-induced phase separation in Triton X-114, the membrane-associated annexin V partitions predominantly into the aqueous phase. We also show that the isoelectric point of annexin V does not change following membrane association. These observations suggest that a covalent modification, of annexin V itself, is not responsible for its association with the membrane. Millimolar [Ca2+] is required for maximal binding of purified annexin V to phospholipid vesicles. We show that binding to phospholipids can be reversed entirely by subsequent treatment with EGTA. This suggests that the EGTA-resistant form of annexin V is binding to a membrane component other than phosphatidylserine. Annexin V has previously been shown to bind to protein kinase C. Relocation of annexin V to membranes paralleled that of protein kinase C in thrombin-stimulated cells but not in cells treated with A23187, suggesting that these proteins are not functionally linked in platelet activation. Using bifunctional cross-linking reagents we have identified an 85 kDa complex containing annexin V. This may represent an association between annexin V and an annexin V-binding protein with a molecular mass of approximately 50 kDa. | lld:pubmed |
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| pubmed-article:7772046 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7772046 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7772046 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7772046 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7772046 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:7772046 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:7772046 | pubmed:author | pubmed-author:WalkerJ HJH | lld:pubmed |
| pubmed-article:7772046 | pubmed:author | pubmed-author:OrchardM AMA | lld:pubmed |
| pubmed-article:7772046 | pubmed:author | pubmed-author:TrotterP JPJ | lld:pubmed |
| pubmed-article:7772046 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7772046 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:7772046 | pubmed:volume | 308 ( Pt 2) | lld:pubmed |
| pubmed-article:7772046 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7772046 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7772046 | pubmed:pagination | 591-8 | lld:pubmed |
| pubmed-article:7772046 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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