Linked Life Data

3265177

Source:http://linkedlifedata.com/resource/pubmed/id/3265177

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1989-3-3
pubmed:abstractText
In a wide variety of cells, inositol 1,4,5-triphosphate (IP3) is a second messenger which interacts with specific intracellular receptors and triggers the release of sequestered Ca2+ from an intracellular store. When bovine adrenal cortex microsomes were incubated in the presence of dithiothreitol [(DTT) IC50 = 50 mM] or n-ethylmaleimide [(NEM) IC50 = 0.5 mM], they lost their IP3 binding capacity. Scatchard analysis of the binding data revealed that DTT decreased the affinity while NEM decreased the number of binding sites for IP3. The effect of DTT was reversible whereas the effect of NEM was permanent. pH variations between 6.5 and 9 increased the IP3 binding capacity of the microsomes. The effects of DTT, NEM, and pH on IP3-induced Ca2+ release from the microsomes were consistent with their effects on IP3 binding. Our data show that the binding sites for IP3 in the bovine adrenal cortex are proteins containing disulfide bridges and free sulfhydryl group(s) which are essential features for the recognition of IP3. These results also suggest that the binding sites for IP3 are the physiological receptors through which IP3 triggers the mobilization of Ca2+ in adrenal cortex in response to angiotensin II and other Ca2+ mobilizing ligands.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0888-8809
pubmed:author
pubmed:issnType
Print
pubmed:volume
2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1249-55
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Effects of pH, reducing and alkylating reagents on the binding and Ca2+ release activities of inositol 1,4,5-triphosphate in the bovine adrenal cortex.
pubmed:affiliation
Department of Pharmacology, Faculty of Medicine, University of Sherbrooke, Quebec, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't