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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
1995-7-5
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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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-1310621,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-1311770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-1420334,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-14731757,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-1482379,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-1487073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-1531131,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-1533622,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-1623112,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-1639799,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-1832677,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-2136859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-2137157,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-2148529,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-218557,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-2333094,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-2365086,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-2396974,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-2522394,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-2526299,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-2550240,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-2556810,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-2936963,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-2946940,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-2956093,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-2957692,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-2960376,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-2962537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-2963226,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-2963810,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-2971390,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-2971450,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-3010133,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-3020049,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-3032981,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-3081518,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-3569513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-388439,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-4110573,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-5765779,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-6257680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-6528977,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-6698984,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-7918671,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-8031848,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-8073497,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-8155692,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-8174710,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-8209779,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-8245122,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-8318006,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-8365543,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-8440377,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-8471604,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7772046-8484740
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0264-6021
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
308 ( Pt 2)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
591-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:7772046-Humans,
pubmed-meshheading:7772046-Blood Platelets,
pubmed-meshheading:7772046-Calcium,
pubmed-meshheading:7772046-Thrombin,
pubmed-meshheading:7772046-Phospholipids,
pubmed-meshheading:7772046-Cell Membrane,
pubmed-meshheading:7772046-Protein Binding,
pubmed-meshheading:7772046-Cytosol,
pubmed-meshheading:7772046-Cell Compartmentation,
pubmed-meshheading:7772046-Cross-Linking Reagents,
pubmed-meshheading:7772046-Liposomes
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