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dc.contributor.authorStephens, Andrew-
dc.contributor.otherZhang, Hui-
dc.contributor.otherMaqsudi, Sadiqa-
dc.contributor.otherRainczuk, Adam-
dc.contributor.otherDuffield, Nadine-
dc.contributor.otherLawrence, Josie-
dc.contributor.otherKeane, Fiona-
dc.contributor.otherJusta-Schuch, Daniela-
dc.contributor.otherGeiss-Friedlander, Ruth-
dc.contributor.otherGorrell, Mark-
dc.identifier.citationThe FEBS Journal 2015 Jul 14en_US
dc.description.abstractDipeptidyl peptidase 9 (DPP9) is a member of the S9B/DPPIV (DPP4) serine protease family, which cleaves N-terminal dipeptides at an Xaa-Pro consensus motif. Cytoplasmic DPP9 has roles in epidermal growth factor signalling and in antigen processing, whilst the role of the recently discovered nuclear form of DPP9 is unknown. Mice lacking DPP9 proteolytic activity die as neonates. We applied a modified 2D differential in-gel electrophoresis approach to identify novel DPP9 substrates, using mouse embryonic fibroblasts lacking endogenous DPP9 activity. A total of 111 potential new DPP9 substrates were identified, with nine proteins/peptides confirmed as DPP9 substrates by MALDI-TOF or immunoblotting. Moreover, we also identified the dipeptide Val-Ala as a consensus site for DPP9 cleavage that was not recognized by DPP8, suggesting different in vivo roles for these closely related enzymes. The relative kinetics for the cleavage of these nine candidate substrates by DPP9, DPP8 and DPP4 were determined. This is the first identification of DPP9 substrates from cells lacking endogenous DPP9 activity. These data greatly expand the potential roles of DPP9 and suggest different in vivo roles for DPP9 and DPP8.en_US
dc.subjectEpworth Research Institute, Epworth HealthCare, Richmond, Victoria, Australiaen_US
dc.subjectDipeptidyl Peptidase 9, Mouseen_US
dc.subjectDipeptidyl Peptidase 9, Humanen_US
dc.subjectMass Spectrometryen_US
dc.subjectSpectrometry, Massen_US
dc.subjectSpectrum Analysis, Massen_US
dc.subjectAnalysis, Mass Spectrumen_US
dc.subjectChromogenic Substratesen_US
dc.subjectSerine Proteasesen_US
dc.subjectEpidermal Growth Factoren_US
dc.subjectProtein Digestionen_US
dc.subjectProtein Degradationen_US
dc.titleIdentification of novel dipeptidyl peptidase 9 substrates by two-dimensional differential in-gel electrophoresis.en_US
dc.typeJournal Articleen_US
dc.identifier.journaltitleThe FEBS Journal © Federation of European Biochemical Societiesen_US
dc.description.affiliatesMolecular Hepatology, Liver Injury and Cancer Group, Centenary Institute, Sydney Medical School, University of Sydney, Australiaen_US
dc.description.affiliatesCentre for Cancer Research, Hudson Institute of Medical Research, Clayton, Victoria, Australiaen_US
dc.description.affiliatesDepartment of Molecular and Translational Sciences, Monash University, Clayton, Victoria, Australiaen_US
dc.description.affiliatesDepartment of Molecular Biology, Faculty of Medicine, Georg-August-University of Goettingen, Germanyen_US
dc.type.studyortrialDescriptive Studyen_US
Appears in Collections:Pre-Clinical

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