|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:dateCreated |
1994-4-14
|
|
pubmed:abstractText |
1-O-Alkyl-2-acyl-sn-glycero-3-phosphocholine (alkylacyl-GPC) is the precursor of platelet-activating factor. It is formed via the CoA-independent transacylase reaction, which transfers the polyenoyl acyl group from the sn-2 position of a diacyl phospholipid to the sn-2 position of 1-O-alkyl-sn-glycero-3-phosphocholine (alkyl-GPC). We have reported previously that vitamin E alters phospholipid turnover in the endothelial cells by increasing arachidonic acid release and prostacyclin synthesis. In the present study, the role of vitamin E in the formation of alkylacyl-GPC was investigated. Incubation of endothelial cells with vitamin E resulted in an increase in the formation of [3H]alkylacyl-GPC from [3H]alkyl-GPC. The effect of vitamin E was dose-dependent at concentrations below 23 microM. However, vitamin E did not have a direct effect on the transacylase activity. When endothelial cells were incubated with vitamin E, the CoA-independent transacylase activity in the cell homogenate was found to be enhanced. Kinetic analysis of the transacylase activity in the pre-incubated cells showed that the enhancement of enzyme activity was at the enzyme-substrate level. When endothelial cells were incubated with vitamin E analogues (Trolox, tocol and tocopherol acetate), only limited enhancement of the transacylation process was detected. It is clear that vitamin E enhanced the synthesis of alkylacyl-GPC from alkyl-GPC in a very specific manner by an indirect stimulation of the CoA-independent transacylase activity. The regulation by vitamin E of the formation of alkylacyl-GPC may mediate the transfer of arachidonate from the diacyl phospholipid pool into the ether-linked phospholipid pool.
|
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-13671378,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-14907713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-1546171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-1900206,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-1903305,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-2107879,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-2115518,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-2325505,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-2351875,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-2539804,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-2673414,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-2775221,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-3086318,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-3128538,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-3143417,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-3707974,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-3918041,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-4008481,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-4024051,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-476122,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-6372154,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-6401298,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-6408071,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-6417134,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-6434535,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-6436245,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8129709-7118885
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Feb
|
|
pubmed:issn |
0264-6021
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
15
|
|
pubmed:volume |
298 ( Pt 1)
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
115-9
|
|
pubmed:dateRevised |
2009-11-18
|
|
pubmed:meshHeading |
pubmed-meshheading:8129709-Acetyl-CoA C-Acyltransferase,
pubmed-meshheading:8129709-Acylation,
pubmed-meshheading:8129709-Acyltransferases,
pubmed-meshheading:8129709-Binding Sites,
pubmed-meshheading:8129709-Cells, Cultured,
pubmed-meshheading:8129709-Endothelium, Vascular,
pubmed-meshheading:8129709-Humans,
pubmed-meshheading:8129709-Platelet Activating Factor,
pubmed-meshheading:8129709-Vitamin E
|
|
pubmed:year |
1994
|
|
pubmed:articleTitle |
Vitamin E enhances the acylation of 1-O-alkyl-sn-glycero-3-phosphocholine in human endothelial cells.
|
|
pubmed:affiliation |
Department of Biochemistry, School of Medicine, University of Ottawa, Ontario, Canada.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
