2014
Renalase
Guo X, Wang L, Velazquez H, Safirstein R, Desir GV. Renalase. Current Opinion In Nephrology & Hypertension 2014, 23: 513-518. PMID: 24992568, PMCID: PMC4383282, DOI: 10.1097/mnh.0000000000000044.Peer-Reviewed Original ResearchConceptsSingle nucleotide polymorphismsEnzymatic functionType 1 diabetesMitogen-activated protein kinase pathwayNucleotide polymorphismsProtein kinase BProtein kinase pathwayCellular actionsPlasma membraneKinase pathwayKinase BPotential therapeutic utilityCertain single nucleotide polymorphismsEnzymatic propertiesIschemic strokeImmune modulatorsRenalase geneTherapeutic utilityCytoprotective effectsClinical implicationsRenalaseConsistent associationPotential roleDiabetesCytokines
2007
Regulation of insulin secretion and GLUT4 trafficking by the calcium sensor synaptotagmin VII
Li Y, Wang P, Xu J, Gorelick F, Yamazaki H, Andrews N, Desir GV. Regulation of insulin secretion and GLUT4 trafficking by the calcium sensor synaptotagmin VII. Biochemical And Biophysical Research Communications 2007, 362: 658-664. PMID: 17720139, PMCID: PMC2194288, DOI: 10.1016/j.bbrc.2007.08.023.Peer-Reviewed Original ResearchConceptsGLUT4 trafficSyt VIIPlasma membraneGLUT4 translocationConstitutive expressionSecretory granule exocytosisSkeletal muscle cellsGLUT4 traffickingRegulated exocytosisVoltage-gated potassium channel Kv1.3Vesicular trafficSynaptotagmin VIIGLUT4 presentPotassium channel Kv1.3Calcium sensorIntracellular compartmentsDeletion resultsGlucose-stimulated insulin secretionChannel Kv1.3Granule exocytosisPancreatic beta cellsChannel activityInsulin secretionPancreatic islet cellsMuscle cells
2006
Voltage-gated potassium channel Kv1.3 regulates GLUT4 trafficking to the plasma membrane via a Ca2+-dependent mechanism
Li Y, Wang P, Xu J, Desir GV. Voltage-gated potassium channel Kv1.3 regulates GLUT4 trafficking to the plasma membrane via a Ca2+-dependent mechanism. American Journal Of Physiology - Cell Physiology 2006, 290: c345-c351. PMID: 16403947, DOI: 10.1152/ajpcell.00091.2005.Peer-Reviewed Original ResearchConceptsPlasma membraneKv1.3 channel activityAmount of GLUT4GLUT4 protein translocationInsulin sensitivityChannel activityChannel inhibitionAddition of wortmanninGLUT4 traffickingInsulin-dependent pathwayProtein translocationPeripheral insulin sensitivityVoltage-gated potassium channel Kv1.3GLUT4 translocationPotassium channel Kv1.3Gene inactivationInsulin-sensitive tissuesGLUT4 proteinKv1.3 inhibitionGlucose transportPsora-4Channel Kv1.3Adipose tissueBody weightPharmacological inhibition
2004
The voltage-gated potassium channel Kv1.3 regulates peripheral insulin sensitivity
Xu J, Wang P, Li Y, Li G, Kaczmarek LK, Wu Y, Koni PA, Flavell RA, Desir GV. The voltage-gated potassium channel Kv1.3 regulates peripheral insulin sensitivity. Proceedings Of The National Academy Of Sciences Of The United States Of America 2004, 101: 3112-3117. PMID: 14981264, PMCID: PMC365752, DOI: 10.1073/pnas.0308450100.Peer-Reviewed Original ResearchMeSH KeywordsAdipose TissueAnimalsBiological TransportFastingGlucoseInsulinInterleukin-6JNK Mitogen-Activated Protein KinasesKineticsKv1.3 Potassium ChannelMaleMiceMice, Inbred C57BLMice, KnockoutMice, ObeseMitogen-Activated Protein KinasesModels, BiologicalMuscle, SkeletalPotassium ChannelsPotassium Channels, Voltage-GatedTumor Necrosis Factor-alphaConceptsKv1.3-/- micePeripheral glucose homeostasisPeripheral insulin sensitivityPlasma membraneGene inactivationInsulin sensitivityAmount of GLUT4Skeletal muscleTerminal kinase (JNK) activityGlucose homeostasisAdipose tissueLower blood insulin levelsVoltage-gated potassium channelsInsulin-stimulated glucose uptakeVoltage-gated potassium channel Kv1.3Tumor necrosis factor productionExperimental autoimmune encephalitisBlood insulin levelsHigh-fat dietPotassium channel Kv1.3Tumor necrosis factor secretionPeripheral T lymphocytesKinase activityNecrosis factor productionNumber of tissues
1999
The T0 Domain of Rabbit KV1.3 Regulates Steady State Channel Protein Level
Segal A, Yao X, Desir G. The T0 Domain of Rabbit KV1.3 Regulates Steady State Channel Protein Level. Biochemical And Biophysical Research Communications 1999, 254: 54-64. PMID: 9920732, DOI: 10.1006/bbrc.1998.9801.Peer-Reviewed Original ResearchConceptsN-terminal regulatory regionVoltage-gated potassium channelsWild-type channelsRegulatory regionsPlasma membraneAmino terminusChannel assemblyChannel proteinsRecognition domainSingle-channel conductanceKv channelsChannel protein levelsProtein levelsProtein densityPotassium channelsOpen probabilityType channelsChannel conductanceKv1.3Fast inactivationDomainMembraneTerminusProteinInactivation
1991
High affinity binding of amiloride analogs at an internal site in renal microvillus membrane vesicles
Desir GV, Cragoe EJ, Aronson PS. High affinity binding of amiloride analogs at an internal site in renal microvillus membrane vesicles. Journal Of Biological Chemistry 1991, 266: 2267-2271. PMID: 1846621, DOI: 10.1016/s0021-9258(18)52238-9.Peer-Reviewed Original ResearchConceptsMembrane vesiclesMicrovillus membrane vesiclesRenal microvillus membrane vesiclesSimilar rank order potencyBinding sitesInternal sitesHigh-affinity inhibitorsMembrane localizationInternal binding siteAmiloride analoguesPlasma membraneRank order potencyHigh-affinity bindingAffinity inhibitorsHigh affinity-binding siteVesiclesBasolateral membrane vesiclesOrder potency