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dc.contributor.authorEva, Richard
dc.contributor.authorBouyoucef-Cherchalli, Dalila
dc.contributor.authorPatel, Kalpana
dc.contributor.authorCullen, Peter J
dc.contributor.authorBanting, George
dc.date.accessioned2018-06-29T08:46:35Z
dc.date.available2018-06-29T08:46:35Z
dc.date.issued2012
dc.identifier.issn1932-6203
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/277640
dc.description.abstractThe inositol (1,4,5) trisphosphate 3-kinases comprise a family of enzymes (A, B, and C) that phosphorylate the calcium mobilising molecule inositol (1,4,5) trisphosphate (IP(3)) to generate inositol (1,3,4,5) tetrakisphosphate. This molecule can function as a second messenger, but its roles are not completely understood. The A isoform of inositol (1,4,5) trisphosphate 3-kinase localises to filamentous actin within dendritic spines in the hippocampus and is implicated in the regulation of spine morphology and long term potentiation, however the mechanisms through which it signals in neuronal cells are not completely understood. We have used NGF driven neurite outgrowth from PC12 cells as a platform to examine the impact of signaling via inositol (1,4,5) trisphosphate 3-kinase activity in a neuronal cell. We have found that the catalytic activity of the enzyme opposes neurite outgrowth, whilst pharmacological inhibition of inositol (1,4,5) trisphosphate 3-kinase leads to a significant increase in neurite outgrowth, and we show that the reduction in neurite outgrowth in response to inositol (1,4,5) trisphosphate 3-kinase activity correlates with reduced ERK activity as determined by western blotting using phosphorylation-specific antibodies. Our findings suggest a novel neuronal signaling pathway linking metabolism of IP(3) to signaling via ERK.
dc.format.mediumPrint-Electronic
dc.languageeng
dc.publisherPublic Library of Science (PLoS)
dc.rightsAttribution 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectHippocampus
dc.subjectNeurons
dc.subjectNeurites
dc.subjectPC12 Cells
dc.subjectAnimals
dc.subjectRats
dc.subjectActins
dc.subjectPhosphotransferases (Alcohol Group Acceptor)
dc.subjectExtracellular Signal-Regulated MAP Kinases
dc.subjectNerve Growth Factor
dc.subjectGreen Fluorescent Proteins
dc.subjectFlow Cytometry
dc.subjectCell Separation
dc.subjectSignal Transduction
dc.subjectCell Differentiation
dc.subjectPhenotype
dc.subjectCatalysis
dc.subjectModels, Biological
dc.titleIP3 3-kinase opposes NGF driven neurite outgrowth.
dc.typeArticle
prism.issueIdentifier2
prism.publicationDate2012
prism.publicationNamePLoS One
prism.startingPagee32386
prism.volume7
dc.identifier.doi10.17863/CAM.24972
dcterms.dateAccepted2012-01-28
rioxxterms.versionofrecord10.1371/journal.pone.0032386
rioxxterms.versionVoR
rioxxterms.licenseref.urihttp://www.rioxx.net/licenses/all-rights-reserved
rioxxterms.licenseref.startdate2012-01
dc.contributor.orcidEva, Richard [0000-0003-0305-0452]
dc.identifier.eissn1932-6203
rioxxterms.typeJournal Article/Review
cam.issuedOnline2012-02-22


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Attribution 4.0 International
Except where otherwise noted, this item's licence is described as Attribution 4.0 International