Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2-3
pubmed:dateCreated
1989-5-30
pubmed:abstractText
We have examined the effects of sodium (Na+) salts on rat liver adenylate cyclase. Increasing concentrations of Na+ salts produced biphasic stimulation and inhibition of adenylate cyclase and potentiated enzyme activation by GTP and its hydrolysis resistant analog 5'-guanylyl imidodiphosphate. Salt effects were temperature dependent, of rapid onset, and specific for the Na+ cation though also partly dependent on the accompanying anion. Sodium salt stimulation of adenylate cyclase and enhancement of GTP activation were attenuated by agents (pertussis toxin and N-ethylmaleimide) which inactivate the inhibitory guanine nucleotide-binding regulatory component (Gi) of adenylate cyclase. Cholera toxin, which activates the stimulatory guanine nucleotide-binding regulatory component (Gs) of adenylate cyclase and thereby increases enzyme activity, augmented the inhibitory phase of Na+ salt action. These results suggest that the stimulatory and inhibitory effects of Na+ salts may be due, respectively, to inhibition of Gi and Gs modulation of adenylate cyclase.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Cyclase, http://linkedlifedata.com/resource/pubmed/chemical/Adenylate Cyclase Toxin, http://linkedlifedata.com/resource/pubmed/chemical/Azides, http://linkedlifedata.com/resource/pubmed/chemical/Cations, Monovalent, http://linkedlifedata.com/resource/pubmed/chemical/Cholera Toxin, http://linkedlifedata.com/resource/pubmed/chemical/Ethylmaleimide, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Manganese, http://linkedlifedata.com/resource/pubmed/chemical/Pertussis Toxin, http://linkedlifedata.com/resource/pubmed/chemical/Sodium Azide, http://linkedlifedata.com/resource/pubmed/chemical/Sodium Chloride, http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors, Bordetella
pubmed:status
MEDLINE
pubmed:issn
0895-7479
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
105-21
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:3149674-Adenylate Cyclase, pubmed-meshheading:3149674-Adenylate Cyclase Toxin, pubmed-meshheading:3149674-Animals, pubmed-meshheading:3149674-Azides, pubmed-meshheading:3149674-Cations, Monovalent, pubmed-meshheading:3149674-Cholera Toxin, pubmed-meshheading:3149674-Dose-Response Relationship, Drug, pubmed-meshheading:3149674-Ethylmaleimide, pubmed-meshheading:3149674-GTP-Binding Proteins, pubmed-meshheading:3149674-Liver, pubmed-meshheading:3149674-Male, pubmed-meshheading:3149674-Manganese, pubmed-meshheading:3149674-Pertussis Toxin, pubmed-meshheading:3149674-Rats, pubmed-meshheading:3149674-Rats, Inbred Strains, pubmed-meshheading:3149674-Sodium Azide, pubmed-meshheading:3149674-Sodium Chloride, pubmed-meshheading:3149674-Time Factors, pubmed-meshheading:3149674-Virulence Factors, Bordetella
pubmed:year
1988
pubmed:articleTitle
Stimulatory and inhibitory effects of sodium salts on adenylate cyclase of rat liver. Implications for salt modulation of guanine nucleotide-binding regulatory component function.
pubmed:affiliation
Department of Medicine, University of Texas Health Science Center, San Antonio 78284.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.