Featured Publications
Unfolded Protein Response Differentially Modulates the Platelet Phenotype
Jain K, Tyagi T, Du J, Hu X, Patell K, Martin KA, Hwa J. Unfolded Protein Response Differentially Modulates the Platelet Phenotype. Circulation Research 2022, 131: 290-307. PMID: 35862006, PMCID: PMC9357223, DOI: 10.1161/circresaha.121.320530.Peer-Reviewed Original ResearchConceptsUPR pathwayProtein responseMouse plateletsUnfolded protein responseActivation of UPRPlatelet phenotypeTranscriptional regulationGenomic regulationProtein misfoldingAnucleate plateletsProtein aggregationUPR activationPhosphorylation of PLCγ2Chemical chaperonesXBP1 pathwayP38 MAPKPERK pathwayUPRPKCδ activationPlatelet physiologyActivation pathwayPathwayPhenotypeIRE1α inhibitionSelective induction
2016
Amelioration of ER stress by 4-phenylbutyric acid reduces chronic hypoxia induced cardiac damage and improves hypoxic tolerance through upregulation of HIF-1α
Jain K, Suryakumar G, Ganju L, Singh SB. Amelioration of ER stress by 4-phenylbutyric acid reduces chronic hypoxia induced cardiac damage and improves hypoxic tolerance through upregulation of HIF-1α. Vascular Pharmacology 2016, 83: 36-46. PMID: 27058435, DOI: 10.1016/j.vph.2016.03.004.Peer-Reviewed Original ResearchMeSH KeywordsAltitudeAnimalsApoptosisApoptosis Regulatory ProteinsChronic DiseaseCytoprotectionDisease Models, AnimalEndoplasmic Reticulum StressHypertrophy, Right VentricularHypoxiaHypoxia-Inducible Factor 1, alpha SubunitMaleMolecular ChaperonesMyocardiumOxidative StressPhenylbutyratesProtein CarbonylationProteolysisRats, Sprague-DawleySignal TransductionTime FactorsUnfolded Protein ResponseUp-RegulationConceptsChronic hypoxiaHIF-1αCardiac damageUnfolded protein responseER stressHypoxic toleranceRight ventricular enlargementExposure of ratsHypoxia-inducible factor-1ER stress modulationEndoplasmic reticulum stressInducible factor-1Ventricular enlargementCardiac injuryCardioprotective actionCardiovascular diseaseCardiac hypertrophyMarked upregulationActivation of UPRUnderlying causeUPR markersHypoxiaReticulum stressConcomitant suppressionFactor 1
2013
Myocardial ER chaperone activation and protein degradation occurs due to synergistic, not individual, cold and hypoxic stress
Jain K, Suryakumar G, Prasad R, Singh SN, Ganju L. Myocardial ER chaperone activation and protein degradation occurs due to synergistic, not individual, cold and hypoxic stress. Biochimie 2013, 95: 1897-1908. PMID: 23816873, DOI: 10.1016/j.biochi.2013.06.018.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisCold TemperatureEndoplasmic Reticulum StressGene Expression RegulationHeat-Shock ProteinsHypoxiaHypoxia-Inducible Factor 1, alpha SubunitLipid PeroxidationMaleMyocardiumOxidation-ReductionProteasome Endopeptidase ComplexProtein CarbonylationProtein Disulfide-IsomerasesProtein FoldingProteolysisRatsRats, Sprague-DawleyTranscription Factor CHOPTunicamycinConceptsStress responseHypoxic stressCellular stress responseCell survival kinasesProtein oxidationEndoplasmic reticulum stress responseER stress responseER stress inducersReticulum stress responseMyocardial protein oxidationER chaperone GRP78Chaperone activationMisfolded proteinsEnvironmental stressProtein degradationChaperone GRP78Cold stressSurvival kinasesProtein oxidative modificationStress inducersHigh altitude stressMolecular levelCHOP expressionMatrix remodelingProtein