2011
miR-33a/b contribute to the regulation of fatty acid metabolism and insulin signaling
Dávalos A, Goedeke L, Smibert P, Ramírez CM, Warrier NP, Andreo U, Cirera-Salinas D, Rayner K, Suresh U, Pastor-Pareja JC, Esplugues E, Fisher EA, Penalva LO, Moore KJ, Suárez Y, Lai EC, Fernández-Hernando C. miR-33a/b contribute to the regulation of fatty acid metabolism and insulin signaling. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 9232-9237. PMID: 21576456, PMCID: PMC3107310, DOI: 10.1073/pnas.1102281108.Peer-Reviewed Original ResearchConceptsFatty acid metabolismFatty acid oxidationMiR-33aInsulin receptor substrate 2Sirtuin 6Acid metabolismInsulin-signaling pathwayIntronic microRNAsSterol regulatory element-binding protein 2Acid oxidationHost genesKey enzymeHepatic cell linesMetabolic syndromeCarnitine palmitoyltransferase 1AMetabolic pathwaysSubstrate 2Cellular imbalanceProtein 2Cholesterol homeostasisGenesCell linesLevels of HDLPathwayMetabolism results
2005
Lovastatin-induced PC-12 cell differentiation is associated with RhoA/RhoA kinase pathway inactivation
Fernández-Hernando C, Suárez Y, Lasunción MA. Lovastatin-induced PC-12 cell differentiation is associated with RhoA/RhoA kinase pathway inactivation. Molecular And Cellular Neuroscience 2005, 29: 591-602. PMID: 15951198, DOI: 10.1016/j.mcn.2005.04.012.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell DifferentiationCholesterolDiterpenesEnzyme ActivationEnzyme InhibitorsHydroxymethylglutaryl-CoA Reductase InhibitorsIntracellular Signaling Peptides and ProteinsLovastatinNeuritesPC12 CellsPhosphorylationProtein PrenylationProtein Serine-Threonine KinasesRatsRhoA GTP-Binding ProteinRho-Associated KinasesSterolsTerpenesConceptsNeurite outgrowthNon-sterol mevalonate derivativesPC-12 cell differentiationCellular lipid compositionNon-sterol isoprenoidsEffects of geranylgeraniolBiosynthetic pathwayProtein prenylationRole of cholesterolCofilin phosphorylationRhoA signalingMevalonate derivativesA ReductaseRhoA activationCell differentiationCoenzyme A (HMG-CoA) reductaseLovastatin inhibitsPC-12 cellsCholesterol biosynthesisPathway inactivationRhoA kinaseLipid compositionOutgrowthGeranylgeraniolInhibition
2004
JNK activation is critical for Aplidin™-induced apoptosis
Cuadrado A, González L, Suárez Y, Martínez T, Muñoz A. JNK activation is critical for Aplidin™-induced apoptosis. Oncogene 2004, 23: 4673-4680. PMID: 15122339, DOI: 10.1038/sj.onc.1207636.Peer-Reviewed Original ResearchMeSH KeywordsAntibodies, MonoclonalAntineoplastic AgentsApoptosisBlotting, WesternBreast NeoplasmsCell DivisionCell Line, TumorCell SurvivalDepsipeptidesEnzyme ActivationFemaleFibroblastsHumansMitogen-Activated Protein KinasesNF-kappa BPeptides, CyclicPhosphorylationPrecipitin TestsProto-Oncogene Proteins c-junTranscription Factor AP-1
2002
AplidinTM Induces Apoptosis in Human Cancer Cells via Glutathione Depletion and Sustained Activation of the Epidermal Growth Factor Receptor, Src, JNK, and p38 MAPK*
Cuadrado A, Garcı́a-Fernández L, González L, Suárez Y, Losada A, Alcaide V, Martı́nez T, Fernández-Sousa J, Sánchez-Puelles J, Muñoz A. AplidinTM Induces Apoptosis in Human Cancer Cells via Glutathione Depletion and Sustained Activation of the Epidermal Growth Factor Receptor, Src, JNK, and p38 MAPK*. Journal Of Biological Chemistry 2002, 278: 241-250. PMID: 12414812, DOI: 10.1074/jbc.m201010200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntineoplastic AgentsApoptosisBreast NeoplasmsCell DivisionCell SurvivalCells, CulturedDepsipeptidesEnzyme ActivationEnzyme InhibitorsErbB ReceptorsFemaleFibroblastsFlow CytometryGlutathioneHumansJNK Mitogen-Activated Protein KinasesKidney NeoplasmsMiceMitogen-Activated Protein KinasesP38 Mitogen-Activated Protein KinasesPeptides, CyclicPhosphorylationProto-Oncogene Proteins pp60(c-src)Receptors, Platelet-Derived Growth FactorTumor Cells, CulturedConceptsEpidermal growth factor receptorP38 MAPK activationP38 MAPKNon-receptor protein tyrosine kinase SrcGrowth factor receptorMAPK activationProtein tyrosine kinase SrcStress response programSustained activationFactor receptorCancer cellsMDA-MB-231 breast cancer cellsHuman cancer cellsBenzyloxycarbonyl-VADKinase SrcHuman MDA-MB-231 breast cancer cellsMDA-MB-231 cellsMolecular basisKinase JNKPretreatment of cellsMouse embryosEGFR activationFluoromethyl ketoneGrowth arrestHuman renal cancer
1999
Cholesterol starvation decreases P34cdc2 kinase activity and arrests the cell cycle at G2
Martínez‐Botas J, Suárez Y, Ferruelo A, Gómez‐Coronado D, Lasunció M. Cholesterol starvation decreases P34cdc2 kinase activity and arrests the cell cycle at G2. The FASEB Journal 1999, 13: 1359-1370. PMID: 10428760, DOI: 10.1096/fasebj.13.11.1359.Peer-Reviewed Original Research