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dc.contributor.authorHeyworth, Clare M
dc.contributor.authorWhetton, Anthony D
dc.contributor.authorKinsella, Anne R
dc.contributor.authorHouslay, M D
dc.date.accessioned2011-03-06T22:41:18Z
dc.date.available2011-03-06T22:41:18Z
dc.date.issued1984-05-07
dc.identifier.citationThe phorbol ester, TPA inhibits glucagon-stimulated adenylate cyclase activity. 1984, 170 (1):38-42 FEBS Lett.en
dc.identifier.issn0014-5793
dc.identifier.pmid6327375
dc.identifier.doi10.1016/0014-5793(84)81364-2
dc.identifier.urihttp://hdl.handle.net/10541/123697
dc.description.abstractThe ability of glucagon (10 nM) to increase hepatocyte intracellular cyclic AMP concentrations was reduced markedly by the tumour-promoting phorbol ester TPA (12-O-tetradecanoyl phorbol-13-acetate). The half-maximal inhibitory effect occurred at 0.14 ng/ml TPA. This action occurred in the presence of the cyclic AMP phosphodiesterase inhibitor isobutylmethylxanthine (1 mM) indicating that TPA inhibited glucagon-stimulated adenylate cyclase activity. TPA did not affect either the binding of glucagon to its receptor or ATP concentrations within the cell. TPA did inhibit the increase in intracellular cyclic AMP initiated by the action of cholera toxin (1 microgram/ml) under conditions where phosphodiesterase activity was blocked. TPA did not inhibit glucagon-stimulated adenylate cyclase activity in a broken plasma membrane preparation unless Ca2+, phosphatidylserine and ATP were also present. It is suggested that TPA exerts its inhibitory effect on adenylate cyclase through the action of protein kinase C. This action is presumed to be exerted at the point of regulation of adenylate cyclase by guanine nucleotides.
dc.language.isoenen
dc.subject.meshAdenylate Cyclase
dc.subject.meshAnimals
dc.subject.meshCholera Toxin
dc.subject.meshCyclic AMP
dc.subject.meshDiglycerides
dc.subject.meshGlucagon
dc.subject.meshGuanylyl Imidodiphosphate
dc.subject.meshLiver
dc.subject.meshMale
dc.subject.meshPhorbols
dc.subject.meshProtein Kinase C
dc.subject.meshProtein Kinases
dc.subject.meshRats
dc.subject.meshRats, Inbred Strains
dc.subject.meshTetradecanoylphorbol Acetate
dc.titleThe phorbol ester, TPA inhibits glucagon-stimulated adenylate cyclase activity.en
dc.typeArticleen
dc.contributor.departmentDepartment of Biochemistry and Applied Molecular Biology, University of Manchester Institute of Science and Technology, PO Box 88, Manchester M60 1QDen
dc.identifier.journalFEBS Lettersen
html.description.abstractThe ability of glucagon (10 nM) to increase hepatocyte intracellular cyclic AMP concentrations was reduced markedly by the tumour-promoting phorbol ester TPA (12-O-tetradecanoyl phorbol-13-acetate). The half-maximal inhibitory effect occurred at 0.14 ng/ml TPA. This action occurred in the presence of the cyclic AMP phosphodiesterase inhibitor isobutylmethylxanthine (1 mM) indicating that TPA inhibited glucagon-stimulated adenylate cyclase activity. TPA did not affect either the binding of glucagon to its receptor or ATP concentrations within the cell. TPA did inhibit the increase in intracellular cyclic AMP initiated by the action of cholera toxin (1 microgram/ml) under conditions where phosphodiesterase activity was blocked. TPA did not inhibit glucagon-stimulated adenylate cyclase activity in a broken plasma membrane preparation unless Ca2+, phosphatidylserine and ATP were also present. It is suggested that TPA exerts its inhibitory effect on adenylate cyclase through the action of protein kinase C. This action is presumed to be exerted at the point of regulation of adenylate cyclase by guanine nucleotides.


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