| pubmed-article:9225256 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9225256 | lifeskim:mentions | umls-concept:C0023823 | lld:lifeskim |
| pubmed-article:9225256 | lifeskim:mentions | umls-concept:C0024360 | lld:lifeskim |
| pubmed-article:9225256 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:9225256 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
| pubmed-article:9225256 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:9225256 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:9225256 | pubmed:dateCreated | 1997-9-8 | lld:pubmed |
| pubmed-article:9225256 | pubmed:abstractText | The treatment of LDL with bee-venom phospholipase A2 resulted in the formation of lipid-protein particles (phl-LDL) with an increased content of lysophosphatidylcholine (LPC). At the same time, the composition of other lipids and the protein structure remained unaffected. phl-LDL, as well as LPC, abolished the hormone-induced [Ca2+] increase in platelets and platelet aggregation induced by PAF, AMP and thrombin, whereas LDL produced no effect on the hormone-stimulated increase in the intracellular [Ca2+]. The effect persisted in a Ca(2+)-free medium, indicating that phl-LDL and LPC did not abolish the mobilization of intracellular stores with the above-mentioned inducers. Neither LPC no phl-LDL affected the [Ca2+]i level in platelets and suppressed the platelet aggregation evoked by tapsigargine, a specific inhibitor of endoplasmic reticulum Ca(2+)-ATPase, or by phorbol myristate acetate. The inhibitory effect depended on the LPC concentration and the time of platelet incubation with phl-LDL or LPC. The half-maximum efficient LPC concentrations were identical for LPC and phl-LDL (2-4 microM). The inhibitory effect was dependent on the LPC structure: lysophosphatidylethanolamine and phosphatidylcholine displayed no inhibitory effect. The results suggest that when added to washed platelets, free LPC and phl-LDL inhibit only the receptor-dependent increase of [Ca2+]i. | lld:pubmed |
| pubmed-article:9225256 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9225256 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9225256 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9225256 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9225256 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9225256 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9225256 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9225256 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9225256 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9225256 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9225256 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9225256 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9225256 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9225256 | pubmed:issn | 1023-6597 | lld:pubmed |
| pubmed-article:9225256 | pubmed:author | pubmed-author:MorozkinA DAD | lld:pubmed |
| pubmed-article:9225256 | pubmed:author | pubmed-author:ProkazovaN... | lld:pubmed |
| pubmed-article:9225256 | pubmed:author | pubmed-author:CheglakovI... | lld:pubmed |
| pubmed-article:9225256 | pubmed:author | pubmed-author:SuslovaI VIV | lld:pubmed |
| pubmed-article:9225256 | pubmed:author | pubmed-author:KorotaevaA... | lld:pubmed |
| pubmed-article:9225256 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9225256 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:9225256 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9225256 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9225256 | pubmed:pagination | 521-34 | lld:pubmed |
| pubmed-article:9225256 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:9225256 | pubmed:meshHeading | pubmed-meshheading:9225256-... | lld:pubmed |
| pubmed-article:9225256 | pubmed:meshHeading | pubmed-meshheading:9225256-... | lld:pubmed |
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| pubmed-article:9225256 | pubmed:meshHeading | pubmed-meshheading:9225256-... | lld:pubmed |
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| pubmed-article:9225256 | pubmed:meshHeading | pubmed-meshheading:9225256-... | lld:pubmed |
| pubmed-article:9225256 | pubmed:meshHeading | pubmed-meshheading:9225256-... | lld:pubmed |
| pubmed-article:9225256 | pubmed:meshHeading | pubmed-meshheading:9225256-... | lld:pubmed |
| pubmed-article:9225256 | pubmed:meshHeading | pubmed-meshheading:9225256-... | lld:pubmed |
| pubmed-article:9225256 | pubmed:meshHeading | pubmed-meshheading:9225256-... | lld:pubmed |
| pubmed-article:9225256 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9225256 | pubmed:articleTitle | Effect of lysophosphatidylcholine on the structure and function of low density lipoproteins. | lld:pubmed |
| pubmed-article:9225256 | pubmed:affiliation | Institute of Experimental Cardiology, Russian Academy of Medical Sciences, Moscow. | lld:pubmed |
| pubmed-article:9225256 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9225256 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9225256 | lld:pubmed |
