Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1987-5-29
pubmed:abstractText
We have previously shown that treatment of T lymphocytes with mitogenic ligands induces a rapid activation of ornithine decarboxylase (ODC) through a mechanism that is independent of protein synthesis but requires energy and an intact cytoskeleton. Here we show by immunoprecipitation experiments and by chemical analyses that ODC is covalently linked to the cell membrane by inositol. Treatment of sonicated cells with a phosphatidylinositol-specific phospholipase C from B. thuringiensis caused a rapid 3-fold increase in ODC activity. Similar treatment of intact cells had no effect, suggesting that the ODC is attached to the cytoplasmic surface of the membrane. We conclude that ODC release and activation occur by a novel mechanism involving phosphatidylinositol breakdown following ligand-receptor interaction.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
49
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
171-6
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Growth signal transduction: rapid activation of covalently bound ornithine decarboxylase during phosphatidylinositol breakdown.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't