Linked Life Data

6421578

Source:http://linkedlifedata.com/resource/pubmed/id/6421578

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1984-4-25
pubmed:abstractText
In a previous paper it was shown that in prelabeled murine thymocytes a direct CoA-mediated transfer of arachidonic acid from phosphatidylcholine to lysophosphatidylethanolamine occurs which does not involve the intermediate formation of free fatty acid. The transfer is ATP-independent and is catalyzed by the acyl-CoA: lysophosphatide acyltransferase operating in reverse. In prelabeled thymocytes phosphatidylcholine was the only arachidonoyl donor and lysophosphatidylethanolamine the only lysoacceptor. In murine bone-marrow-derived macrophages a series of CoA-mediated transfer reactions were detected leading to a redistribution of arachidonic acid between phospholipids. Using exogenous substrates a bidirectional transfer from 1-acyl-2-arachidonoylglycerophosphocholine to lysophosphatidylethanolamine occurs. An unidirectional transfer from 1-acyl-2-arachidonoylglycerophosphoinositol to lysophosphatidylcholine and from 1-acyl-2-arachidonoylglycerophosphoinositol to lysophosphatidylethanolamine was observed. Plasmalogenic lysoacceptors generally have a weaker acceptor capacity than the correspondent acyllysophospholipid. In macrophages the CoA-mediated transfer of arachidonoyl moieties is independent of ATP and Mg2+ and is totally inhibited by sodium cholate, indicating that it is catalyzed by the acyl-CoA: lysophosphatide acyltransferase.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
139
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
431-7
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1984
pubmed:articleTitle
Acyltransferase-catalyzed cleavage of arachidonic acid from phospholipids and transfer to lysophosphatides in macrophages derived from bone marrow. Comparison of different donor- and acceptor substrate combinations.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't