Linked Life Data

12562835

Source:http://linkedlifedata.com/resource/pubmed/id/12562835

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2003-3-4
pubmed:abstractText
Ethanolamine phosphotransferase (EPT) is a key enzyme responsible for the synthesis of ethanolamine glycerophospholipids. Plasmenylethanolamine is a predominant molecular subclass of ethanolamine glycerophospholipids in the heart. The present study was designed to identify the selective use of 1-O-alk-1'-enyl-2-acyl-sn-glycerol as a substrate for EPT as a mechanism responsible for the predominance of plasmenylethanolamine in the rabbit heart. EPT activity in rabbit myocardial membranes using 1,2-diacyl-sn-glycerol as substrate is activated by Mn2+, inhibited by dithiobisnitrobenzoic acid (DTNB) and is unaffected by Ca2+. In contrast, ethanolamine phosphotransferase activity using 1-O-alk-1'-enyl-2-acyl-sn-glycerol as substrate is inhibited by Mn2+ and Ca2+, but is activated by DTNB. Additionally, ethanolamine phosphotransferase activity using 1-O-alk-1'-enyl-2-acyl-sn-glycerol substrate was more sensitive to thermal denaturation compared with that of 1,2-diacyl-sn-glycerol. Taken together, these results suggest that separate ethanolamine phosphotransferase activities are present in heart membranes that are responsible for the synthesis of phosphatidylethanolamine and plasmenylethanolamine.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0022-2275
pubmed:author
pubmed:issnType
Print
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
554-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Separate myocardial ethanolamine phosphotransferase activities responsible for plasmenylethanolamine and phosphatidylethanolamine synthesis.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, St. Louis University Health Sciences Center, St. Louis, MO 63104, USA. fordda@slu.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.