2023
TNFα increases the degradation of pyruvate dehydrogenase kinase 4 by the Lon protease to support proinflammatory genes
Boutagy N, Fowler J, Grabinska K, Cardone R, Sun Q, Vazquez K, Whalen M, Zhu X, Chakraborty R, Martin K, Simons M, Romanoski C, Kibbey R, Sessa W. TNFα increases the degradation of pyruvate dehydrogenase kinase 4 by the Lon protease to support proinflammatory genes. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2218150120. PMID: 37695914, PMCID: PMC10515159, DOI: 10.1073/pnas.2218150120.Peer-Reviewed Original ResearchMeSH KeywordsAcetyl Coenzyme ACytokinesEndothelial CellsHistonesHumansProtease LaTumor Necrosis Factor-alphaConceptsPyruvate dehydrogenase kinase 4Dehydrogenase kinase 4Lon proteasePyruvate dehydrogenase activityHistone acetylationMitochondrial metabolismKinase 4Specific gene lociPDH fluxEndothelial cellsSiRNA-mediated knockdownAcetyl-CoA generationLysine 27Gene transcriptionTCA fluxRNA sequencingHuman umbilical vein endothelial cellsProtein degradationHistone 3Gene locusUmbilical vein endothelial cellsNF-κB-dependent mechanismTricarboxylic acid cycle fluxVein endothelial cellsActive subunit
2010
Activation of Hedgehog Signaling by the Environmental Toxicant Arsenic May Contribute to the Etiology of Arsenic-Induced Tumors
Fei D, Li H, Kozul C, Black K, Singh S, Gosse J, DiRenzo J, Martin K, Wang B, Hamilton J, Karagas M, Robbins D. Activation of Hedgehog Signaling by the Environmental Toxicant Arsenic May Contribute to the Etiology of Arsenic-Induced Tumors. Cancer Research 2010, 70: 1981-1988. PMID: 20179202, PMCID: PMC2831120, DOI: 10.1158/0008-5472.can-09-2898.Peer-Reviewed Original ResearchConceptsArsenic exposureBladder cancerEnvironmental toxicant arsenicBladder cancer patientsSignificant health problemVariety of tumorsHedgehog signalingCancer patientsHealth problemsHigh levelsTumor samplesCancerHedgehog activitySame cancerHuman carcinogenesisMillions of peopleEtiologyTumorsExposureProgressionHedgehogTissue culture cellsActivationSignalingPatients
2007
Regulation of vascular smooth muscle cell differentiation
Rzucidlo E, Martin K, Powell R. Regulation of vascular smooth muscle cell differentiation. Journal Of Vascular Surgery 2007, 45: a25-a32. PMID: 17544021, DOI: 10.1016/j.jvs.2007.03.001.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsVascular smooth muscle cell differentiationSmooth muscle cell differentiationMuscle cell differentiationCell differentiationPathogenesis of atherosclerosisMajor human diseasesLocal environmental cuesEnvironmental cuesContractile roleIntimal hyperplasiaDifferentiated stateVascular aneurysmsMolecular mechanismsVascular developmentPhenotypic switchingHuman diseasesVessel wallVSMCCritical roleDifferentiationEssential componentHypertensionAsthmaAtherosclerosisHyperplasia
2005
Endothelial cell activation of the smooth muscle cell phosphoinositide 3-kinase/Akt pathway promotes differentiation
Brown D, Rzucidlo E, Merenick B, Wagner R, Martin K, Powell R. Endothelial cell activation of the smooth muscle cell phosphoinositide 3-kinase/Akt pathway promotes differentiation. Journal Of Vascular Surgery 2005, 41: 509-516. PMID: 15838487, DOI: 10.1016/j.jvs.2004.12.024.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAorta, ThoracicCattleCell DifferentiationCells, CulturedCoculture TechniquesEndothelial CellsMuscle, Smooth, VascularMyocytes, Smooth MusclePhenotypePhosphatidylinositol 3-KinasesProtein Serine-Threonine KinasesProtein-Tyrosine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-aktSignal TransductionConceptsEC/SMCDifferentiated SMC phenotypeSMC phenotypeSMC differentiationSmooth muscle cellsAkt pathwayProtein markersProtein kinase AktAdenoviral overexpressionContractile protein markersDominant-negative AktEndothelial cellsOpposite endothelial cellsBlood vessel developmentRapid Akt phosphorylationPI3K/Akt pathwayMuscle cellsWestern blottingKinase AktAbility of ECsActive AktPhosphoinositide 3Kinase activityMolecular signalsSynthetic phenotype