Linked Life Data

2253702

Source:http://linkedlifedata.com/resource/pubmed/id/2253702

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
1991-1-22
pubmed:abstractText
The equilibrium and kinetic binding characteristics of D-inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) have been studied in membrane preparations of rat cerebellum and bovine adrenal cortex. Saturation analysis of isotopic dilution binding data demonstrated apparent KD values for Ins(1,4,5)P3 binding of 23 +/- 5 nM and 3.0 +/- 1.3 nM for cerebellar and adrenal cortical preparations, respectively, with approximately 20-fold greater receptor density present in the cerebellar preparation (Bmax: 10.2 +/- 2.5 pmol/mg protein). Kinetic analysis confirmed the equilibrium binding-derived KD value for cerebellum (KD: 39.9 nM), but revealed a second, very high affinity site (KD: 0.06 nM) to be present in adrenal cortex. The affinity differences between the investigated preparations was also observed with respect to the IC50 values obtained for inhibition of specific [3H]Ins(1,4,5)P3 binding by a number of inositol polyphosphate analogues including D-inositol 2,4,5-trisphosphate, DL-inositol 1,4,5-trisphosphorothioate and L-Ins(1,4,5)P3. In contrast, the Ins(1,4,5)P3-receptor antagonist heparin displayed greater potency for the cerebellar (IC50: 16.5 +/- 6.2 micrograms . ml-1) compared to the adrenal cortical preparation (IC50: 51.0 +/- 6.1 micrograms . ml-1). The apparent differences between the Ins(1,4,5)P3 receptors characterized in the two tissue preparations are discussed.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0014-2999
pubmed:author
pubmed:issnType
Print
pubmed:day
18
pubmed:volume
189
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
185-93
pubmed:dateRevised
2010-8-25
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Characteristics of inositol 1,4,5-trisphosphate binding to rat cerebellar and bovine adrenal cortical membranes: evidence for the heterogeneity of binding sites.
pubmed:affiliation
Department of Pharmacology and Therapeutics, University of Leicester, U.K.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't