Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1986-5-15
pubmed:abstractText
Incubation of purified cardiac sarcolemmal vesicles (SL) in the presence of S-adenosyl-L-methionine, a methyl donor for the enzymatic N-methylation of phosphatidylethanolamine (PE), increased the Ca2+-stimulated ATPase and ATP-dependent Ca2+ accumulation activities. Quantitative analysis of the methylated phospholipids revealed that maximal increase of Ca2+-pump activities was associated with predominant synthesis and intramembranal accumulation of phosphatidyl-N,N-dimethylethanolamine. The stimulation of SL Ca2+-pump activities was prevented by inhibitors of PE N-methylation such as S-adenosyl-L-homocysteine and methyl acetimidate hydrochloride. The results suggest a possible role of PE N-methylation in the regulation of Ca2+-transport across the heart SL membrane.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
856
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
383-7
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Stimulation of Ca2+-pump in rat heart sarcolemma by phosphatidylethanolamine N-methylation.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't