2011
Vacuolar-type H+-ATPase-mediated proton transport in the rat parietal cell
Kopic S, Wagner ME, Griessenauer C, Socrates T, Ritter M, Geibel JP. Vacuolar-type H+-ATPase-mediated proton transport in the rat parietal cell. Pflügers Archiv - European Journal Of Physiology 2011, 463: 419-427. PMID: 22146938, DOI: 10.1007/s00424-011-1060-0.Peer-Reviewed Original ResearchConceptsV-ATPase activityV-ATPaseAcid secretionParietal cellsRat parietal cellsProton pump inhibitor therapyCertain specialized cellsK-ATPaseProton transportVacuolar-type H-ATPaseK-ATPase inhibitionSecretion pathwayTrafficking mechanismsSpecialized cellsMicrotubule networkActive acidificationInhibitor therapyIntracellular organellesK-ATPase activityRat gastric glandsConcanamycin APharmacological inhibitionAcid loadIntracellular alkalinizationAcid breakthrough
2004
Vacuolar ATPase Regulates Zymogen Activation in Pancreatic Acini*
Waterford SD, Kolodecik TR, Thrower EC, Gorelick FS. Vacuolar ATPase Regulates Zymogen Activation in Pancreatic Acini*. Journal Of Biological Chemistry 2004, 280: 5430-5434. PMID: 15582989, PMCID: PMC2846595, DOI: 10.1074/jbc.m413513200.Peer-Reviewed Original ResearchMeSH KeywordsAmylasesAnimalsCalciumCarbacholCell MembraneCells, CulturedCeruletideChloroquineChymotrypsinEnzyme ActivationEnzyme PrecursorsHydrogen-Ion ConcentrationMacrolidesMaleMonensinPancreasProtein SubunitsProtein TransportRatsRats, Sprague-DawleySolubilityThapsigarginTrypsinVacuolar Proton-Translocating ATPasesConceptsPancreatic acinar cellsSupramaximal concentrationsPancreatic aciniAcinar cellsVacuolar ATPase inhibitor bafilomycinConcentration-dependent mannerAcute pancreatitisEffects of agentsATPase inhibitor bafilomycinConcentration-dependent translocationWeak base chloroquineCaerulein stimulationIntracellular pHConcanamycin AChymotrypsin activationActivationBase chloroquineV-ATPase activationInhibitor bafilomycin
1997
Perforin is activated by a proteolytic cleavage during biosynthesis which reveals a phospholipid‐binding C2 domain
Uellner R, Zvelebil M, Hopkins J, Jones J, MacDougall L, Morgan B, Podack E, Waterfield M, Griffiths G. Perforin is activated by a proteolytic cleavage during biosynthesis which reveals a phospholipid‐binding C2 domain. The EMBO Journal 1997, 16: 7287-7296. PMID: 9405358, PMCID: PMC1170329, DOI: 10.1093/emboj/16.24.7287.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCell LineCytotoxicity, ImmunologicGlycosylationHexosaminidasesHumansIsoenzymesKiller Cells, NaturalLiposomesLymphocyte ActivationMembrane GlycoproteinsModels, MolecularMolecular Sequence DataPerforinPhospholipase C deltaPhospholipidsPore Forming Cytotoxic ProteinsProtein ConformationProtein Processing, Post-TranslationalRatsRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidT-Lymphocytes, CytotoxicTransfectionType C PhospholipasesConceptsC2 domainPro-pieceProteolytic cleavagePlasma membrane of target cellsBind phospholipid membranesMembrane of target cellsCalcium-dependent mannerSecreted proteinsIntracellular transportC-terminusPhospholipid membranesNK cell line YTPlasma membraneCleaved formInactive precursorAcidic compartmentsIncreased lytic activityConcanamycin AActive formLytic activityKilling assayE-64CleavageEpitope mappingPore formation
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