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Article: Essential role of GTP in the expression of adenylate cyclase activity after cholera toxin treatment

TitleEssential role of GTP in the expression of adenylate cyclase activity after cholera toxin treatment
Authors
Issue Date1978
Citation
Journal Of Cyclic Nucleotide Research, 1978, v. 4 n. 3, p. 159-168 How to Cite?
AbstractExpression of activation of rat liver adenylate cyclase by the A 1 peptide of cholera toxin and NAD is dependent on GTP. The nucleotide is effective either when added to the assay medium or during toxin (and NAD) treatment. Toxin treatment increases the V(max) for activation by GTP and the effect of GTP persists in toxin-treated membranes, a property seen in control membranes only with non-hydrolyzable analogs of GTP such as Gpp(NH)p. These observations could be explained by a recent report that cholera toxin acts to inhibit a GTPase associated with denylate cyclase. However, the authors have observed that one of the major effects of the toxin is to decrease the affinity of guanine nucleotides for the processes involved in the activation of adenylate cyclase and in the regulation of the binding of glucagon to its receptor. Moreover, the absence of lag time in the activation of adenylate cyclase by GTP, in contrast to by Gpp(NH)p, and the markedly reduced fluoride action after toxin treatment suggest that GTPase inhibition may not be the only action of cholera toxin on the adenylate cyclase system. The authors believe that the multiple effects of toxin action is a reflection of the recently revealed complexity of the regulation of adenylate cyclase by guanine nucleotides.
Persistent Identifierhttp://hdl.handle.net/10722/167444
ISSN
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLin, MCen_US
dc.contributor.authorWelton, AFen_US
dc.contributor.authorBerman, MFen_US
dc.date.accessioned2012-10-08T03:07:05Z-
dc.date.available2012-10-08T03:07:05Z-
dc.date.issued1978en_US
dc.identifier.citationJournal Of Cyclic Nucleotide Research, 1978, v. 4 n. 3, p. 159-168en_US
dc.identifier.issn0095-1544en_US
dc.identifier.urihttp://hdl.handle.net/10722/167444-
dc.description.abstractExpression of activation of rat liver adenylate cyclase by the A 1 peptide of cholera toxin and NAD is dependent on GTP. The nucleotide is effective either when added to the assay medium or during toxin (and NAD) treatment. Toxin treatment increases the V(max) for activation by GTP and the effect of GTP persists in toxin-treated membranes, a property seen in control membranes only with non-hydrolyzable analogs of GTP such as Gpp(NH)p. These observations could be explained by a recent report that cholera toxin acts to inhibit a GTPase associated with denylate cyclase. However, the authors have observed that one of the major effects of the toxin is to decrease the affinity of guanine nucleotides for the processes involved in the activation of adenylate cyclase and in the regulation of the binding of glucagon to its receptor. Moreover, the absence of lag time in the activation of adenylate cyclase by GTP, in contrast to by Gpp(NH)p, and the markedly reduced fluoride action after toxin treatment suggest that GTPase inhibition may not be the only action of cholera toxin on the adenylate cyclase system. The authors believe that the multiple effects of toxin action is a reflection of the recently revealed complexity of the regulation of adenylate cyclase by guanine nucleotides.en_US
dc.languageengen_US
dc.relation.ispartofJournal of Cyclic Nucleotide Researchen_US
dc.subject.meshAdenylate Cyclase - Metabolismen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCell Membrane - Enzymologyen_US
dc.subject.meshCholera Toxin - Pharmacologyen_US
dc.subject.meshEnzyme Activation - Drug Effectsen_US
dc.subject.meshFluorides - Pharmacologyen_US
dc.subject.meshGlucagon - Pharmacologyen_US
dc.subject.meshGuanosine Triphosphate - Pharmacologyen_US
dc.subject.meshGuanylyl Imidodiphosphate - Pharmacologyen_US
dc.subject.meshKineticsen_US
dc.subject.meshLiver - Enzymologyen_US
dc.subject.meshNad - Metabolismen_US
dc.subject.meshPeptide Fragments - Pharmacologyen_US
dc.subject.meshRatsen_US
dc.titleEssential role of GTP in the expression of adenylate cyclase activity after cholera toxin treatmenten_US
dc.typeArticleen_US
dc.identifier.emailLin, MC:mcllin@hkucc.hku.hken_US
dc.identifier.authorityLin, MC=rp00746en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid214459-
dc.identifier.scopuseid_2-s2.0-0018102790en_US
dc.identifier.volume4en_US
dc.identifier.issue3en_US
dc.identifier.spage159en_US
dc.identifier.epage168en_US
dc.identifier.isiWOS:A1978FE06800001-
dc.identifier.scopusauthoridLin, MC=7404816359en_US
dc.identifier.scopusauthoridWelton, AF=7003728787en_US
dc.identifier.scopusauthoridBerman, MF=7202661046en_US

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