2023
Cellular protection from H2O2 toxicity by Fv-Hsp70: protection via catalase and gamma-glutamyl-cysteine synthase
Hino C, Chan G, Jordaan G, Chang S, Saunders J, Bashir M, Hansen J, Gera J, Weisbart R, Nishimura R. Cellular protection from H2O2 toxicity by Fv-Hsp70: protection via catalase and gamma-glutamyl-cysteine synthase. Cell Stress And Chaperones 2023, 28: 429-439. PMID: 37171750, PMCID: PMC10352194, DOI: 10.1007/s12192-023-01349-6.Peer-Reviewed Original ResearchConceptsHeat shock proteinsGamma-glutamylcysteine synthaseCellular protectionAcute oxidative stressLid domainProtein-binding domainsATPase domainCysteine synthaseOxidative stressCellular stressRecombinant proteinsSH-SY5Y cellsEndogenous heat shock proteinsShock proteinsCell deathProteinProtein catalaseHSP70H2O2 toxicityCellsSynthaseΜM concentrationsDomainCatalaseDirect response
2015
Endothelial CD74 mediates macrophage migration inhibitory factor protection in hyperoxic lung injury
Sauler M, Zhang Y, Min J, Leng L, Shan P, Roberts S, Jorgensen WL, Bucala R, Lee PJ. Endothelial CD74 mediates macrophage migration inhibitory factor protection in hyperoxic lung injury. The FASEB Journal 2015, 29: 1940-1949. PMID: 25609432, PMCID: PMC4415022, DOI: 10.1096/fj.14-260299.Peer-Reviewed Original ResearchConceptsMacrophage migration inhibitory factorLung endothelial cellsMurine lung endothelial cellsLung injuryEndothelial cellsProtective effectExogenous MIFCD74 deficient miceCD74-dependent mannerHours of hyperoxiaMIF receptor CD74Acute lung injuryHyperoxic lung injuryBronchoalveolar lavage proteinMigration inhibitory factorBronchoalveolar proteinMIF deficiencyMedian survivalEndothelial injuryWT miceAcute oxidative stressReceptor CD74Lavage proteinReceptor antagonistReceptor inhibitors
2007
Nitrosative Stress and Myocardial Sarcoplasmic Endoreticular Calcium Adenosine Triphosphatase Subtype 2a Activity after Lung Resection in Swine
Heerdt PM, Lane P, Pan BY, Schaefer U, Crabtree M, Hong R, Singer AA, Levi R, Park BJ. Nitrosative Stress and Myocardial Sarcoplasmic Endoreticular Calcium Adenosine Triphosphatase Subtype 2a Activity after Lung Resection in Swine. Anesthesiology 2007, 107: 954-962. PMID: 18043064, DOI: 10.1097/01.anes.0000291446.70921.61.Peer-Reviewed Original ResearchConceptsNitrosative stressForce-frequency relationLung resectionSERCA2a activityAcute oxidative stressOxidative stressPhosphorylation stateSubcellular processesBiochemical basisProtein phospholambanDisease-associated oxidative stressRegulatory protein phospholambanPhospholamban phosphorylationReticular membranesProtein expressionImpaired calcium cyclingPhosphorylationWestern blottingExpressionPerioperative changesUpper lobectomyPhospholamban expressionSham groupAcute eventChronic illness
2005
Werner Protein Protects Nonproliferating Cells from Oxidative DNA Damage
Szekely AM, Bleichert F, Nümann A, Van Komen S, Manasanch E, Nasr A, Canaan A, Weissman SM. Werner Protein Protects Nonproliferating Cells from Oxidative DNA Damage. Molecular And Cellular Biology 2005, 25: 10492-10506. PMID: 16287861, PMCID: PMC1291253, DOI: 10.1128/mcb.25.23.10492-10506.2005.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesCell ProliferationCells, CulturedCellular SenescenceDNADNA DamageDNA HelicasesDNA ReplicationExodeoxyribonucleasesFibroblastsGene Expression RegulationHumansOxidation-ReductionOxidative StressOxygenRecQ HelicasesRNA InterferenceTelomeric Repeat Binding Protein 2Werner Syndrome HelicaseConceptsDNA damage responseWerner syndromeDamage responseDNA damageRNA interferenceOxidative DNA damageWRN-depleted cellsInduction of gammaH2AXDNA damage fociCellular senescence phenotypePrimary human fibroblastsWRN depletionWerner proteinWRN proteinNuclear fociWRN deficiencyProtein TRF2Telomere maintenanceAcute oxidative stressBLM expressionDNA homeostasisDNA replicationDamage fociSenescence phenotypePhysiological oxygen
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply