Linked Life Data

8391798

Source:http://linkedlifedata.com/resource/pubmed/id/8391798

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-8-5
pubmed:abstractText
The appearance of Ins1P as an index of direct PtdIns breakdown by phospholipase C was examined in rat brain cortical membranes using either exogenous [3H]PtdIns substrate or [3H]inositol-prelabeled endogenous phosphoinositide substrates. Production of [3H]Ins1P was observed using exogenous [3H]PtdIns but not with endogenous substrate over the physiological range of calcium concentrations. [3H]Ins1,4P2 and [3H]Ins4P, derived from phospholipase C breakdown of polyphosphoinositides, were formed by membranes from both exogenous [3H]PtdIns and endogenous 3H-phosphoinositides, in the presence of ATP. The contribution of endogenous PtdInsP2 and PtdInsP to the generation of inositol phosphates was examined in membranes from [3H]inositol-prelabeled brain slices by adding unlabeled Ins1,4,5P3 to trap [3H]Ins1,4,5P3 generated upon breakdown of [3H]PtdInsP2. The maximal rate of [3H]Ins1,4,5P3 appearance was attained in the presence of 150-200 microM added Ins1,4,5P3 and represented 12.5% of the combined rates of formation of [3H]Ins1,4,5P3 and [3H]Ins1,4P2, similar to the content of [3H]PtdInsP2 relative to total 3H-polyphosphoinositides. The results show that, while endogenous PtdIns is not degraded by phospholipase C, the enzyme appears to be equally effective to cleave endogenous PtdInsP2 and PtdInsP.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
193
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1061-7
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Endogenous phosphoinositide precursors of inositol phosphates in rat brain cortical membranes.
pubmed:affiliation
Departamento de Bioquímica y Biología Molecular, Facultad de Medicina, Universidad Autónoma de Barcelona, Bellaterra, Spain.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't