2024
Malate initiates a proton-sensing pathway essential for pH regulation of inflammation
Chen Y, Shi R, Xiang Y, Fan L, Tang H, He G, Zhou M, Feng X, Tan J, Huang P, Ye X, Zhao K, Fu W, Li L, Bian X, Chen H, Wang F, Wang T, Zhang C, Zhou B, Chen W, Liang T, Lv J, Kang X, Shi Y, Kim E, Qin Y, Hettinghouse A, Wang K, Zhao X, Yang M, Tang Y, Piao H, Guo L, Liu C, Miao H, Tang K. Malate initiates a proton-sensing pathway essential for pH regulation of inflammation. Signal Transduction And Targeted Therapy 2024, 9: 367. PMID: 39737965, PMCID: PMC11683149, DOI: 10.1038/s41392-024-02076-9.Peer-Reviewed Original ResearchConceptsL-malateInflammatory responseCytosolic pHBind BiPTCA intermediatesSensing pathwaysRegulation of inflammatory responsesBiological informationAnti-inflammatory metabolitesAnti-inflammatory proteinPro-inflammatory macrophagesRegulation of inflammationSignaling modalitiesPhysiological adaptationsAnti-inflammatory effectsIRF2BP2BiPPH regulationCarboxylate metaboliteChemical languageIn vivoIn vitroMacrophagesPathwayPH reduction
2004
Activation of a calcium entry pathway by sodium pyrithione in the bag cell neurons of Aplysia
Knox RJ, Magoski NS, Wing D, Barbee SJ, Kaczmarek LK. Activation of a calcium entry pathway by sodium pyrithione in the bag cell neurons of Aplysia. Developmental Neurobiology 2004, 60: 411-423. PMID: 15307146, DOI: 10.1002/neu.20029.Peer-Reviewed Original ResearchConceptsAplysia bag cell neuronsWhole-cell current-clamp recordingsBag cell neuronsPlasma membraneCurrent-clamp recordingsNeuronal physiologyCytosolic pHCytosolic freeMembrane potentialCell neuronsSodium pyrithionePresence of externalRatiometric imagingMV depolarizationClose structural analogueHill coefficientNapStructural analoguesSpecies
2003
Intracellular pH Activates Membrane-Bound Na+/H+ Exchanger and Vacuolar H+-ATPase in Human Embryonic Kidney (HEK) Cells
Lang K, Wagner C, Haddad G, Burnekova O, Geibel J. Intracellular pH Activates Membrane-Bound Na+/H+ Exchanger and Vacuolar H+-ATPase in Human Embryonic Kidney (HEK) Cells. Cellular Physiology And Biochemistry 2003, 13: 257-262. PMID: 14586169, DOI: 10.1159/000074540.Peer-Reviewed Original ResearchConceptsMicroM EIPAIntracellular acidificationFree bath solutionProximal tubule cellsInfluence of intracellularWestern blot analysisTime-dependent mannerTubule cellsHuman embryonic kidney cellsHEK-293 cellsExtruding mechanismHuman embryonic kidney cell line HEK-293NHE3 proteinEmbryonic kidney cellsCell line HEK-293Cytosolic pHKidney cellsBlot analysisAbsence of bicarbonateHEK293 cellsBath solutionEIPAPresent studyActivationCells
1990
Amiloride analogs induce the phosphorylation of elongation factor-2 in vascular endothelial cells.
Demolle D, Lecomte M, Boutherin-Falson O, Cragoe E, Nairn A, Boeynaems J. Amiloride analogs induce the phosphorylation of elongation factor-2 in vascular endothelial cells. Molecular Pharmacology 1990, 37: 827-832. PMID: 2359404, DOI: 10.1016/s0026-895x(25)11052-3.Peer-Reviewed Original ResearchConceptsElongation factor 2Protein synthesisFactor 2Rabbit reticulocyte lysateCell-free systemBovine aortic endothelial cellsDependent phosphorylationReticulocyte lysateEndothelial cellsAmiloride analoguesPhosphorylationSimilar MrCytosolic pHVascular endothelial cellsProteinAnalogues of amilorideAortic endothelial cellsPotent inhibitorInhibitory effectAntiportCellsEIPAAmilorideATPLysates
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