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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1997-9-8
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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.
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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/Adenosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Lipoproteins, LDL,
http://linkedlifedata.com/resource/pubmed/chemical/Lysophosphatidylcholines,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipases A2,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Activating Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Aggregation Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Thrombin
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pubmed:status |
MEDLINE
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pubmed:issn |
1023-6597
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
10
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
521-34
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:9225256-Adenosine Diphosphate,
pubmed-meshheading:9225256-Blood Platelets,
pubmed-meshheading:9225256-Calcium,
pubmed-meshheading:9225256-Hemofiltration,
pubmed-meshheading:9225256-Humans,
pubmed-meshheading:9225256-Lipoproteins, LDL,
pubmed-meshheading:9225256-Lysophosphatidylcholines,
pubmed-meshheading:9225256-Phospholipases A,
pubmed-meshheading:9225256-Phospholipases A2,
pubmed-meshheading:9225256-Platelet Activating Factor,
pubmed-meshheading:9225256-Platelet Activation,
pubmed-meshheading:9225256-Platelet Aggregation,
pubmed-meshheading:9225256-Platelet Aggregation Inhibitors,
pubmed-meshheading:9225256-Structure-Activity Relationship,
pubmed-meshheading:9225256-Thrombin
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pubmed:year |
1997
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pubmed:articleTitle |
Effect of lysophosphatidylcholine on the structure and function of low density lipoproteins.
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pubmed:affiliation |
Institute of Experimental Cardiology, Russian Academy of Medical Sciences, Moscow.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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