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rdf:type |
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lifeskim:mentions |
umls-concept:C0003483,
umls-concept:C0003695,
umls-concept:C0025519,
umls-concept:C0030685,
umls-concept:C0031673,
umls-concept:C0031676,
umls-concept:C0225336,
umls-concept:C0391871,
umls-concept:C0680255,
umls-concept:C1135183,
umls-concept:C1283071,
umls-concept:C1512179,
umls-concept:C1963578
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pubmed:issue |
2
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pubmed:dateCreated |
1987-11-5
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pubmed:abstractText |
Confluent cultures of porcine aortic endothelial cells were prelabeled with 1 microM [14C]arachidonic acid complexed to 1 microM bovine serum albumin. After washing, the cells were stimulated with 1 microM A23187 for time intervals between 30 s and 30 min. Cellular lipids were extracted and separated into major lipid classes and phospholipid subclasses. The external medium was analyzed for released radioactive eicosanoids. The time-course of total release of 14C radioactivity demonstrated a biphasic nature of A23187-induced changes in endothelial cell lipids. Early, from 30 s to 5 min, substantial losses of [14C]arachidonic acid from diacylphosphatidylethanolamine and phosphatidylinositol, as well as an abrupt increase in diacylphosphatidylcholine-associated radioactivity were observed. These initial changes coincided with the release of 14C-labeled cyclooxygenase products. Later changes (5-30 min) included a sustained progressive loss of 14C radioactivity from alkenyl (alk-1-enyl) acylphosphatidylethanolamine and diacylphosphatidylcholine. These later changes coincided with the elaboration of 14C-labeled lipoxygenase products. Although unequivocal assignments cannot be made, the data suggest that specific pools of arachidonic acid provide precursors for individual classes of eicosanoids.
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pubmed:grant |
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/15-hydroxy-5,8,11,13-eicosatetraenoi...,
http://linkedlifedata.com/resource/pubmed/chemical/5-hydroxy-6,8,11,14-eicosatetraenoic...,
http://linkedlifedata.com/resource/pubmed/chemical/6-Ketoprostaglandin F1 alpha,
http://linkedlifedata.com/resource/pubmed/chemical/Arachidonic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Arachidonic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Calcimycin,
http://linkedlifedata.com/resource/pubmed/chemical/Ethers,
http://linkedlifedata.com/resource/pubmed/chemical/Fatty Acids, Unsaturated,
http://linkedlifedata.com/resource/pubmed/chemical/Hydroxyeicosatetraenoic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylcholines,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylethanolamines,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Phospholipids
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
921
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
159-66
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:3115300-6-Ketoprostaglandin F1 alpha,
pubmed-meshheading:3115300-Acylation,
pubmed-meshheading:3115300-Animals,
pubmed-meshheading:3115300-Aorta, Thoracic,
pubmed-meshheading:3115300-Arachidonic Acid,
pubmed-meshheading:3115300-Arachidonic Acids,
pubmed-meshheading:3115300-Calcimycin,
pubmed-meshheading:3115300-Cells, Cultured,
pubmed-meshheading:3115300-Endothelium, Vascular,
pubmed-meshheading:3115300-Ethers,
pubmed-meshheading:3115300-Fatty Acids, Unsaturated,
pubmed-meshheading:3115300-Hydroxyeicosatetraenoic Acids,
pubmed-meshheading:3115300-Kinetics,
pubmed-meshheading:3115300-Phosphatidylcholines,
pubmed-meshheading:3115300-Phosphatidylethanolamines,
pubmed-meshheading:3115300-Phosphatidylinositols,
pubmed-meshheading:3115300-Phospholipids,
pubmed-meshheading:3115300-Swine
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pubmed:year |
1987
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pubmed:articleTitle |
Ionophore-induced metabolism of phospholipids and eicosanoid production in porcine aortic endothelial cells: selective release of arachidonic acid from diacyl and ether phospholipids.
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pubmed:affiliation |
Department of Medicine and Biochemistry, Boston University School of Medicine, MA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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