2010
Apical Surface Expression of Aspartic Protease Plasmepsin 4, a Potential Transmission-blocking Target of the Plasmodium Ookinete*
Li F, Patra KP, Yowell CA, Dame JB, Chin K, Vinetz JM. Apical Surface Expression of Aspartic Protease Plasmepsin 4, a Potential Transmission-blocking Target of the Plasmodium Ookinete*. Journal Of Biological Chemistry 2010, 285: 8076-8083. PMID: 20056606, PMCID: PMC2832958, DOI: 10.1074/jbc.m109.063388.Peer-Reviewed Original ResearchConceptsPlasmepsin 4Midgut invasionAspartic proteasesDigestive vacuoleMidgut peritrophic matrixApical surface expressionChitin-binding proteinsMass spectrometry sequencingMalaria parasitesPeritrophic matrixPlasmodium invasionAspartic protease inhibitorsPlasmodium ookinetesParasite infectivityApical surfaceDefinitive hostsMechanistic roleAffinity columnBlood-stage PlasmodiumSurface expressionCalpain inhibitorsMidgut basal laminaProteinVaccine targetsVacuoles
2007
Characterization of the Intracellular Proteolytic Cleavage of Myocilin and Identification of Calpain II as a Myocilin-processing Protease*
Sánchez-Sánchez F, Martínez-Redondo F, Aroca-Aguilar JD, Coca-Prados M, Escribano J. Characterization of the Intracellular Proteolytic Cleavage of Myocilin and Identification of Calpain II as a Myocilin-processing Protease*. Journal Of Biological Chemistry 2007, 282: 27810-27824. PMID: 17650508, DOI: 10.1074/jbc.m609608200.Peer-Reviewed Original ResearchConceptsExtracellular calciumCalpain IICalcium-activated proteaseIntraocular pressureT cellsIntracellular proteolytic cleavageCalpain inhibitorsCalcium uptakeProteolytic cleavageCalpain inhibitor IVOlfactomedin-like domainCalpain IInhibitor IVMyocilinEndoplasmic reticulumIntracellular processingLumenRNA interference knockdownCalciumProteolytic processingCellsCulture mediumGlaucomaSubcellular fractionationEndoproteolytic processingCalpain regulation of AMPA receptor channels in cortical pyramidal neurons
Yuen EY, Gu Z, Yan Z. Calpain regulation of AMPA receptor channels in cortical pyramidal neurons. The Journal Of Physiology 2007, 580: 241-254. PMID: 17234699, PMCID: PMC2075435, DOI: 10.1113/jphysiol.2006.122754.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBlotting, WesternCalpainCells, CulturedCerebral CortexElectrophysiologyEndocytosisGerbillinaeImmunohistochemistryMaleMAP Kinase Kinase 2NeuronsNeuroprotective AgentsPatch-Clamp TechniquesPyramidal CellsRatsRats, Sprague-DawleyReceptors, AMPAReceptors, Cell SurfaceReceptors, N-Methyl-D-AspartateStimulation, ChemicalSynapsesSynaptic TransmissionConceptsCortical pyramidal neuronsNMDA receptorsPyramidal neuronsAMPA receptorsNMDA treatmentCalpain inhibitorsIschaemia-induced depressionFast excitatory synaptic transmissionTransient ischemic insultAMPAR-mediated currentsExcitatory synaptic transmissionCalpain-dependent mannerAMPA receptor channelsSelective calpain inhibitorsExcitotoxic conditionsIschemic animalsIschemic insultNeuronal excitotoxicityAMPAR currentsAMPA responsesCortical culturesExtracellular glutamateGlutamate receptorsGlutamate triggersNeuronal excitability
2005
μ-Calpain Regulates Receptor Activator of NF-κB Ligand (RANKL)-supported Osteoclastogenesis via NF-κB Activation in RAW 264.7 Cells*
Lee FY, Kim DW, Karmin JA, Hong D, Chang SS, Fujisawa M, Takayanagi H, Bigliani LU, Blaine TA, Lee HJ. μ-Calpain Regulates Receptor Activator of NF-κB Ligand (RANKL)-supported Osteoclastogenesis via NF-κB Activation in RAW 264.7 Cells*. Journal Of Biological Chemistry 2005, 280: 29929-29936. PMID: 15955824, DOI: 10.1074/jbc.m414600200.Peer-Reviewed Original ResearchConceptsRAW 264.7 cellsNF-kappaB activationReceptor activatorCalpain inhibitorsCell-permeable calpain inhibitorMatrix metalloproteinase-9Regulation of RANKLNF-κB activationNF-κB ligandNF-kappaB ligandMonocyte/macrophage progenitorsRole of calpainMurine RAW 264.7 cellsCell typesMetalloproteinase-9Osteoclastogenic markersCalpain activationResistant acidDecreased expressionOsteoclastogenesisRANKLCalpain activityMu-calpainInhibitorsActivationRegulation of N-Methyl-D-aspartate Receptors by Calpain in Cortical Neurons*
Wu HY, Yuen EY, Lu YF, Matsushita M, Matsui H, Yan Z, Tomizawa K. Regulation of N-Methyl-D-aspartate Receptors by Calpain in Cortical Neurons*. Journal Of Biological Chemistry 2005, 280: 21588-21593. PMID: 15790561, DOI: 10.1074/jbc.m501603200.Peer-Reviewed Original ResearchConceptsN-methyl-D-aspartate receptorsNMDA receptorsNMDAR currentsCortical neuronsCalpain inhibitorsCultured cortical neuronsCortical pyramidal neuronsDynamin inhibitory peptideFunction of NMDARsInhibitory peptidesInvolvement of calpainNMDAR-mediated currentsNMDAR channel functionSelective calpain inhibitorsNMDAR internalizationNMDAR overstimulationNeuroprotective mechanismsPyramidal neuronsNMDA treatmentBath applicationIntracellular injectionNR2B subunitCalcium entryPathologic functionsProlonged treatment
1999
Calcium‐Dependent Cleavage of Striatal Enriched Tyrosine Phosphatase (STEP)
Nguyen T, Paul S, Xu Y, Gurd J, Lombroso P. Calcium‐Dependent Cleavage of Striatal Enriched Tyrosine Phosphatase (STEP). Journal Of Neurochemistry 1999, 73: 1995-2001. PMID: 10537058, DOI: 10.1046/j.1471-4159.1999.01995.x.Peer-Reviewed Original ResearchConceptsPostsynaptic densityTransient hypoxia-ischemiaPrimary neuronal culturesNeuronal precursor cellsCalcium-dependent cleavageHypoxia-ischemiaStriatal neuronsNeuronal insultsRat striatumNeuronal culturesCalcium ionophoreCalpain inhibitorsSTEP61Precursor cellsLow molecular weight formMolecular weight formsPhosphorylation levelsSmaller isoformSignificant increaseTyrosine phosphorylation levelsRapid appearanceCalpain treatmentRapid influxWeight formsCells
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