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dc.contributor.authorHouslay, M D
dc.contributor.authorHeyworth, Clare M
dc.contributor.authorWhetton, Anthony D
dc.date.accessioned2015-01-08T10:35:33Z
dc.date.available2015-01-08T10:35:33Z
dc.date.issued1983-05-08
dc.identifier.citationMechanism of glucagon activation of adenylate cyclase in the presence of Mn2+. 1983, 155 (2):311-6 FEBS Letten
dc.identifier.issn0014-5793
dc.identifier.pmid6303847
dc.identifier.urihttp://hdl.handle.net/10541/337887
dc.description.abstractFor a variety of ligand states, adenylate cyclase activity in the presence of Mn2+ was greater than with Mg2+. Trypsin treatment of intact hepatocytes, under conditions which destroy cell surface glucagon receptors, led to a first order loss of glucagon-stimulated adenylate cyclase activity in isolated membranes assayed in the presence of Mn2+ whether or not GTP (100 microM) was present in the assays. Arrhenius plots of basal activity exhibited a break at around 22 degrees C, those with NaF were linear and those with glucagon +/- GTP (100 microM) were biphasic with a break at around 28 degrees C. It is suggested that Mn2+ perturbs the coupling interaction between the glucagon receptor and catalytic unit of adenylate cyclase at the level of the guanine nucleotide regulatory protein. This appears to take the form of Mn2+ preventing GTP from initiating glucagon's activation of adenylate cyclase through a collision coupling mechanism.
dc.language.isoenen
dc.rightsArchived with thanks to FEBS lettersen
dc.subject.meshAdenylate Cyclase
dc.subject.meshAnimals
dc.subject.meshCell Membrane
dc.subject.meshEnzyme Activation
dc.subject.meshGlucagon
dc.subject.meshIn Vitro Techniques
dc.subject.meshLiver
dc.subject.meshMagnesium
dc.subject.meshMale
dc.subject.meshManganese
dc.subject.meshRats
dc.subject.meshRats, Inbred Strains
dc.subject.meshReceptors, Cell Surface
dc.subject.meshReceptors, Glucagon
dc.titleMechanism of glucagon activation of adenylate cyclase in the presence of Mn2+.en
dc.typeArticleen
dc.contributor.departmentDepartment of Biochemistry and Applied Molecular Biology, UIMIST, PO Box 88 Manchester M60 1QDen
dc.identifier.journalFEBS Lettersen
html.description.abstractFor a variety of ligand states, adenylate cyclase activity in the presence of Mn2+ was greater than with Mg2+. Trypsin treatment of intact hepatocytes, under conditions which destroy cell surface glucagon receptors, led to a first order loss of glucagon-stimulated adenylate cyclase activity in isolated membranes assayed in the presence of Mn2+ whether or not GTP (100 microM) was present in the assays. Arrhenius plots of basal activity exhibited a break at around 22 degrees C, those with NaF were linear and those with glucagon +/- GTP (100 microM) were biphasic with a break at around 28 degrees C. It is suggested that Mn2+ perturbs the coupling interaction between the glucagon receptor and catalytic unit of adenylate cyclase at the level of the guanine nucleotide regulatory protein. This appears to take the form of Mn2+ preventing GTP from initiating glucagon's activation of adenylate cyclase through a collision coupling mechanism.


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