Search results for "MG132"

showing 5 items of 15 documents

Coordinated Sumoylation and Ubiquitination Modulate EGF Induced EGR1 Expression and Stability

2011

Background Human early growth response-1 (EGR1) is a member of the zing-finger family of transcription factors induced by a range of molecular and environmental stimuli including epidermal growth factor (EGF). In a recently published paper we demonstrated that integrin/EGFR cross-talk was required for Egr1 expression through activation of the Erk1/2 and PI3K/Akt/Forkhead pathways. EGR1 activity and stability can be influenced by many different post-translational modifications such as acetylation, phosphorylation, ubiquitination and the recently discovered sumoylation. The aim of this work was to assess the influence of sumoylation on EGF induced Egr1 expression and/or stability. Methods We …

Time FactorsTranscription GeneticSUMO proteinlcsh:MedicineUbiquitin-conjugating enzymeBiochemistrychemistry.chemical_compoundEpidermal growth factorMG132protein 1lcsh:ScienceMitogen-Activated Protein Kinase 1Regulation of gene expressionMitogen-Activated Protein Kinase 3MultidisciplinaryProtein translationProtein Stabilitygene expression regulationCell biologyepidermal growth factorResearch Articlemedicine.drugProteasome Endopeptidase Complexendocrine systemkinase 1SUMO-1 ProteinBiologyDNA-binding proteinsGeneticsmedicineHumansBiologySettore BIO/10 - BIOCHIMICAProtein kinase BPI3K/AKT/mTOR pathwayEarly Growth Response Protein 1lcsh:RMitogen-activated proteinProteinsSumoylationRegulatory proteinsenzyme activationRNA stabilityMolecular biologychemistryProteolysisUbiquitin-Conjugating EnzymesProteasome inhibitorlcsh:QEarly growth responseGene expressionCell linePLoS ONE
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Proteasome comprising a beta1 inducible subunit acts as a negative regulator of NADPH oxidase during elicitation of plant defense reactions.

2005

Elicitation of defense reactions in tobacco by cryptogein, triggered a production of active oxygen species (AOS) via the NADPH oxidase, NtrbohD, and an accumulation of beta1din, a defense induced beta-type subunit of 20S proteasome. The proteasome inhibitor, MG132, stimulated this AOS production. Tobacco cells transformed with sense constructs of beta1din showed an inhibition of the AOS production following elicitin treatment, whereas the antisense transformed cells showed a strongly enhanced AOS production. In cells transformed with sense construct of beta1din, the NtrbohD transcripts failed to be induced by cryptogein as observed in control and antisense transformed cells. Conversely, in …

Tobacco BY-2 cellsHypersensitive responseProteasome Endopeptidase ComplexLeupeptinsBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyCysteine Proteinase InhibitorsBiochemistrychemistry.chemical_compoundStructural BiologyMG132Sense (molecular biology)TobaccoGeneticsmedicineNADPH OXIDASEPROTEASOMEMolecular Biology[SDV.BC] Life Sciences [q-bio]/Cellular BiologyComputingMilieux_MISCELLANEOUSPlant ProteinsCRYPTOGEINNADPH oxidaseTOBACCO BY-2 CELLSNADPH OxidasesElicitinCell BiologyOligonucleotides AntisenseProtein SubunitsProteasomechemistryBiochemistryProteasome inhibitorbiology.proteinPLANT DEFENSEAOS PRODUCTIONReactive Oxygen SpeciesProteasome Inhibitorsmedicine.drugFEBS letters
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Induction of apoptosis by the proteasome inhibitor MG132 in human HCC cells: Possible correlation with specific caspase-dependent cleavage of β-caten…

2004

Proteasome inhibitors, like MG132, can exert cell growth inhibitory and apoptotic effects in different tumor types. The apoptotic mechanism of these compounds involves the activation of the effector caspases. beta-catenin, also an oncogene, represents one of the substrates of these proteases, but the consequences of its cleavage are poorly understood. We investigated its function during apoptosis induced by MG132 in three hepatocellular carcinoma (HCC) cell lines, endowed (HepG2 and HuH-6) or not (HA22T/VGH) with activating mutations of beta-catenin. Induction of apoptosis was associated with cell growth inhibition, accumulation of the cells at the G(2)/M phases of the cell cycle, as well a…

hepatocellular carcinoma ß-catenin apoptosis proteasome MG132 survivinSettore MED/09 - Medicina InternabiologyCell growthGeneral MedicineCell cycleCell biologychemistry.chemical_compoundProteasomechemistryApoptosisMG132SurvivinGeneticsProteasome inhibitormedicineCancer researchbiology.proteinCaspasemedicine.drug
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Synergistic cytotoxic interactions between sodium butyrate, MG132 and camptothecin in human retinoblastoma Y79 cells.

2000

This paper studies the effects caused in human retinoblastoma Y79 cells by treatment with combinations of sodium butyrate, the inhibitor of topoisomerase I camptothecin and the inhibitor of 26S proteasome MG132. The combination of sodium butyrate and camptothecin resulted in a strong synergistic cytotoxicity, as revealed by combination indices of 0.77 and 0.52 calculated at IC(50) and IC(75). Synergistic interactions were also demonstrated for combinations of sodium butyrate and MG132, camptothecin and MG132 and for a combination of all three compounds. The cytotoxic effects observed after the combined treatments can be considered a consequence of apoptosis, as suggested by the appearance o…

medicine.drug_classCell SurvivalLeupeptinsSodiumchemistry.chemical_elementApoptosisButyrateBiologyCysteine Proteinase Inhibitorschemistry.chemical_compoundMG132Antineoplastic Combined Chemotherapy ProtocolsmedicineTumor Cells CulturedHumansheterocyclic compoundsEnzyme InhibitorsRetinoblastomaCaspase 3TopoisomeraseRetinoblastomaSodium butyrateDrug SynergismGeneral Medicinemedicine.diseaseeye diseasesEnzyme ActivationButyrateschemistryBiochemistryProto-Oncogene Proteins c-bcl-2CaspasesCancer researchbiology.proteinCamptothecinTopoisomerase I InhibitorsTumor Suppressor Protein p53CamptothecinTopoisomerase inhibitormedicine.drugTumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine
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Assembly and Translocation of Papillomavirus Capsid Proteins

2002

ABSTRACT The major and minor capsid proteins of polyomavirus are preassembled in the cytoplasm and translocated to the nucleus only as a VP1-VP2/VP3 complex. In this study, we describe independent nuclear translocation of the L1 major protein and the L2 minor capsid protein of human papillomavirus type 33 by several approaches. First, we observed that expression and nuclear translocation of L2 in natural lesions precede expression of L1. Second, using a cell culture system for coexpression, we found that accumulation of L2 in nuclear domain 10 (ND10) subnuclear structures precedes L1 by several hours. In contrast, complexes of L2 and mutants of L1 forced to assemble in the cytoplasm are tra…

virusesImmunologyActive Transport Cell NucleusChromosomal translocationBiologyMicrobiologychemistry.chemical_compoundCapsidVirologyMG132medicineAnimalsHumansPapillomaviridaeCOS cellsStructure and AssemblyVirus AssemblyOncogene Proteins Viralbiochemical phenomena metabolism and nutritionMolecular biologymedicine.anatomical_structureCapsidchemistryCytoplasmCell cultureInsect ScienceCOS CellsProteasome inhibitorCapsid ProteinsFemaleNucleusmedicine.drug
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