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dc.contributor.authorKosgodage, Uchini S
dc.contributor.authorUysal-Onganer, Pinar
dc.contributor.authorMacLatchy, Amy
dc.contributor.authorKraev, Igor
dc.contributor.authorChatterton, Nicholas
dc.contributor.authorNicholas, Anthony P.
dc.contributor.authorInal, Jameel
dc.contributor.authorLange, Sigrun
dc.date.accessioned2019-01-16T13:00:01Z
dc.date.available2019-01-16T13:00:01Z
dc.date.issued2018-12-28
dc.identifier.citationKosgodage , U S , Uysal-Onganer , P , MacLatchy , A , Kraev , I , Chatterton , N , Nicholas , A P , Inal , J & Lange , S 2018 , ' Peptidylarginine Deiminases Post-Translationally Deiminate Prohibitin and Modulate Extracellular Vesicle Release and MicroRNAs in Glioblastoma Multiforme ' , International Journal of Molecular Sciences , vol. 20 , no. 1 , 103 . https://doi.org/10.3390/ijms20010103
dc.identifier.issn1422-0067
dc.identifier.otherPURE: 16013790
dc.identifier.otherPURE UUID: 91fbe834-f9f1-407a-a599-7355c2f43c98
dc.identifier.otherScopus: 85059253805
dc.identifier.urihttp://hdl.handle.net/2299/20968
dc.description.abstractGlioblastoma multiforme (GBM) is the most aggressive form of adult primary malignant brain tumour with poor prognosis. Extracellular vesicles (EVs) are a key-mediator through which GBM cells promote a pro-oncogenic microenvironment. Peptidylarginine deiminases (PADs), which catalyze the post-translational protein deimination of target proteins, are implicated in cancer, including via EV modulation. Pan-PAD inhibitor Cl-amidine affected EV release from GBM cells, and EV related microRNA cargo, with reduced pro-oncogenic microRNA21 and increased anti-oncogenic microRNA126, also in combinatory treatment with the chemotherapeutic agent temozolomide (TMZ). The GBM cell lines under study, LN18 and LN229, differed in PAD2, PAD3 and PAD4 isozyme expression. Various cytoskeletal, nuclear and mitochondrial proteins were identified to be deiminated in GBM, including prohibitin (PHB), a key protein in mitochondrial integrity and also involved in chemo-resistance. Post-translational deimination of PHB, and PHB protein levels, were reduced after 1 h treatment with pan-PAD inhibitor Cl-amidine in GBM cells. Histone H3 deimination was also reduced following Cl-amidine treatment. Multifaceted roles for PADs on EV-mediated pathways, as well as deimination of mitochondrial, nuclear and invadopodia related proteins, highlight PADs as novel targets for modulating GBM tumour communication.en
dc.language.isoeng
dc.relation.ispartofInternational Journal of Molecular Sciences
dc.rightsOpen
dc.subjectDeiminated histone H3
dc.subjectExtracellular vesicles (EVs)
dc.subjectGlioblastoma multiforme (GBM)
dc.subjectPeptidylarginine deiminase (PAD)
dc.subjectProhibitin (PHB)
dc.subjectCatalysis
dc.subjectMolecular Biology
dc.subjectSpectroscopy
dc.subjectComputer Science Applications
dc.subjectPhysical and Theoretical Chemistry
dc.subjectOrganic Chemistry
dc.subjectInorganic Chemistry
dc.titlePeptidylarginine Deiminases Post-Translationally Deiminate Prohibitin and Modulate Extracellular Vesicle Release and MicroRNAs in Glioblastoma Multiformeen
dc.contributor.institutionSchool of Life and Medical Sciences
dc.contributor.institutionBiosciences Research Group
dc.contributor.institutionExtracellular Vesicle Research Unit
dc.description.statusPeer reviewed
dc.identifier.urlhttp://www.scopus.com/inward/record.url?scp=85059253805&partnerID=8YFLogxK
dc.relation.schoolSchool of Life and Medical Sciences
dc.description.versiontypeFinal Published version
dcterms.dateAccepted2018-12-28
rioxxterms.versionVoR
rioxxterms.versionofrecordhttps://doi.org/10.3390/ijms20010103
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/
rioxxterms.typeJournal Article/Review
herts.preservation.rarelyaccessedtrue
herts.rights.accesstypeOpen


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