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Article: 5' Guanylylimidodiphosphate, a potent activator of adenylate cyclase systems in eukaryotic cells

Title5' Guanylylimidodiphosphate, a potent activator of adenylate cyclase systems in eukaryotic cells
Authors
Issue Date1974
PublisherNational Academy of Sciences. The Journal's web site is located at http://www.pnas.org
Citation
Proceedings Of The National Academy Of Sciences Of The United States Of America, 1974, v. 71 n. 8, p. 3087-3090 How to Cite?
Abstract5' Guanylylimidodiphosphate (Gpp(NH)p) stimulates adenylate cyclase [ATP pyrophosphate lyase (cyclizing), EC 4.6.1.1] activity in plasma membranes isolated from frog and salmon erythrocytes, from rat adrenal, hepatic, and fat cells, and from bovine thyroid cells. The nucleotide acts cooperatively with the various hormones (glucagon, secretin, ACTH, thyrotropin, and catecholamines) that stimulate these adenylate cyclase systems with resultant activities that equal or exceed those obtained with hormone plus GTP or with fluoride ion. In the absence of hormones, Gpp(NH)p is a considerably more effective activator than GTP, and, under certain conditions of incubation, stimulates rat fat cell adenylate cyclase to levels of activity (about 20 nmoles of 3',5' adenosine monophosphate mg protein per min) far higher than reported hitherto for any adenylate cyclase system examined. The nucleotide activates frog erythrocyte adenylate cyclase when the catecholamine receptor is blocked by the competitive antagonist, propranolol, and activates the enzyme from an adrenal tumor cell line which lacks functional ACTH receptors. In contrast, Gpp(NH)p does not stimulate adenylate cyclase in extracts from Escherichia coli B. Gpp(NH)p appears to be a useful probe for investigating the mechanism of hormone and nucleotide action on adenylate cyclase systems in eukaryotic cells.
Persistent Identifierhttp://hdl.handle.net/10722/167431
ISSN
2015 Impact Factor: 9.423
2015 SCImago Journal Rankings: 6.883
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorLondos, Cen_US
dc.contributor.authorSalomon, Yen_US
dc.contributor.authorLin, MCen_US
dc.date.accessioned2012-10-08T03:06:54Z-
dc.date.available2012-10-08T03:06:54Z-
dc.date.issued1974en_US
dc.identifier.citationProceedings Of The National Academy Of Sciences Of The United States Of America, 1974, v. 71 n. 8, p. 3087-3090en_US
dc.identifier.issn0027-8424en_US
dc.identifier.urihttp://hdl.handle.net/10722/167431-
dc.description.abstract5' Guanylylimidodiphosphate (Gpp(NH)p) stimulates adenylate cyclase [ATP pyrophosphate lyase (cyclizing), EC 4.6.1.1] activity in plasma membranes isolated from frog and salmon erythrocytes, from rat adrenal, hepatic, and fat cells, and from bovine thyroid cells. The nucleotide acts cooperatively with the various hormones (glucagon, secretin, ACTH, thyrotropin, and catecholamines) that stimulate these adenylate cyclase systems with resultant activities that equal or exceed those obtained with hormone plus GTP or with fluoride ion. In the absence of hormones, Gpp(NH)p is a considerably more effective activator than GTP, and, under certain conditions of incubation, stimulates rat fat cell adenylate cyclase to levels of activity (about 20 nmoles of 3',5' adenosine monophosphate mg protein per min) far higher than reported hitherto for any adenylate cyclase system examined. The nucleotide activates frog erythrocyte adenylate cyclase when the catecholamine receptor is blocked by the competitive antagonist, propranolol, and activates the enzyme from an adrenal tumor cell line which lacks functional ACTH receptors. In contrast, Gpp(NH)p does not stimulate adenylate cyclase in extracts from Escherichia coli B. Gpp(NH)p appears to be a useful probe for investigating the mechanism of hormone and nucleotide action on adenylate cyclase systems in eukaryotic cells.en_US
dc.languageengen_US
dc.publisherNational Academy of Sciences. The Journal's web site is located at http://www.pnas.orgen_US
dc.relation.ispartofProceedings of the National Academy of Sciences of the United States of Americaen_US
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subject.meshAdenylate Cyclase - Metabolismen_US
dc.subject.meshAdipose Tissue - Enzymologyen_US
dc.subject.meshAdrenal Gland Neoplasms - Enzymologyen_US
dc.subject.meshAdrenal Glands - Enzymologyen_US
dc.subject.meshAllosteric Regulation - Drug Effectsen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAnuraen_US
dc.subject.meshCattleen_US
dc.subject.meshCell Lineen_US
dc.subject.meshCell Membrane - Enzymologyen_US
dc.subject.meshEnzyme Activation - Drug Effectsen_US
dc.subject.meshEpinephrine - Pharmacologyen_US
dc.subject.meshErythrocytes - Enzymologyen_US
dc.subject.meshEscherichia Coli - Enzymologyen_US
dc.subject.meshFluorides - Pharmacologyen_US
dc.subject.meshGlucagon - Pharmacologyen_US
dc.subject.meshGuanine Nucleotides - Pharmacologyen_US
dc.subject.meshGuanosine Triphosphate - Pharmacologyen_US
dc.subject.meshLiver - Enzymologyen_US
dc.subject.meshPropranolol - Pharmacologyen_US
dc.subject.meshRatsen_US
dc.subject.meshSalmonen_US
dc.subject.meshStimulation, Chemicalen_US
dc.subject.meshThyroid Gland - Enzymologyen_US
dc.title5' Guanylylimidodiphosphate, a potent activator of adenylate cyclase systems in eukaryotic cellsen_US
dc.typeArticleen_US
dc.identifier.emailLin, MC:mcllin@hkucc.hku.hken_US
dc.identifier.authorityLin, MC=rp00746en_US
dc.description.naturepublished_or_final_versionen_US
dc.identifier.doi10.1073/pnas.71.8.3087-
dc.identifier.pmid4607368-
dc.identifier.pmcidPMC388626-
dc.identifier.scopuseid_2-s2.0-0016264821en_US
dc.identifier.volume71en_US
dc.identifier.issue8en_US
dc.identifier.spage3087en_US
dc.identifier.epage3090en_US
dc.identifier.isiWOS:A1974U269600037-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridLondos, C=7005200523en_US
dc.identifier.scopusauthoridSalomon, Y=7006956498en_US
dc.identifier.scopusauthoridLin, MC=7404816359en_US

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