Search results for "kinases"

showing 10 items of 929 documents

Heme oxygenase-1 inhibits apoptosis in Caco-2 cells via activation of Akt pathway

2005

Heme oxygenase-1 can play a protective role against cellular stress. In colon cancer cells, these effects would be relevant to oncogenesis and resistance to chemotherapy. The aim of the study was to examine the effects of heme oxygenase-1 induction on cell survival in a human colon cancer cell line, Caco-2. Serum deprivation induced apoptosis, reduced Akt and p38 phosphorylation, and increased p21(Cip/WAF1) levels. Heme oxygenase-1 induction by treatment with cobalt protoporphyrin IX resulted in resistance to apoptosis, activation of Akt, reduction in p21(Cip/WAF1) levels and modification of bcl2/bax ratio towards survival. Indomethacin reduced apoptosis but in contrast to heme oxygenase-1,…

Cyclin-Dependent Kinase Inhibitor p21BiliverdinCell SurvivalChemistryBilirubinp38 mitogen-activated protein kinasesProtoporphyrinsApoptosisCell BiologyBiochemistryCulture Media Serum-FreeCell biologyHeme oxygenasechemistry.chemical_compoundApoptosisEnzyme InductionHumansCaco-2 CellsProto-Oncogene Proteins c-aktHemeProtein kinase BHeme Oxygenase-1PI3K/AKT/mTOR pathwayThe International Journal of Biochemistry & Cell Biology
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Calmodulin binds to p21(Cip1) and is involved in the regulation of its nuclear localization.

1999

p21(Cip1), first described as an inhibitor of cyclin-dependent kinases, has recently been shown to have a function in the formation of cyclin D-Cdk4 complexes and in their nuclear translocation. The dual behavior of p21(Cip1) may be due to its association with other proteins. Different evidence presented here indicate an in vitro and in vivo interaction of p21(Cip1) with calmodulin: 1) purified p21(Cip1) is able to bind to calmodulin-Sepharose in a Ca(2+)-dependent manner, and this binding is inhibited by the calmodulin-binding domain of calmodulin-dependent kinase II; 2) both molecules coimmunoprecipitate when extracted from cellular lysates; and 3) colocalization of calmodulin and p21(Cip…

Cyclin-Dependent Kinase Inhibitor p21CalmodulinMolecular Sequence DataBiologyBiochemistryCell LineCalmodulinIn vivoCyclinsProto-Oncogene ProteinsmedicineAnimalsCyclin D1Amino Acid SequencePhosphorylationMolecular BiologyCyclinCell NucleusSulfonamidesKinaseColocalizationCyclin-Dependent Kinase 4Cell BiologyImmunogold labellingPrecipitin TestsCyclin-Dependent KinasesCell biologyRatsEnzyme ActivationCell nucleusMicroscopy Electronmedicine.anatomical_structurebiology.proteinNuclear localization sequenceProtein BindingThe Journal of biological chemistry
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Lovastatin causes sensitization of HeLa cells to ionizing radiation‐induced apoptosis by the abrogation of G2 blockage

2003

To investigate the effect of inhibition of Ras/Rho-regulated signalling by 3-hydroxy-3-methylglutaryl coenzyme A (HMG-CoA) reductase inhibitors (statins) on radiation-induced cell killing and apoptosis.Different human cell lines were pretreated or not with lovastatin before exposure to gamma-rays. Afterwards, radiation-induced cell killing, formation and repair of double-strand breaks, activation of radiation-inducible signal mechanisms (i.e. p53, p21, extracellular-signal-related kinase (ERK), NF-kappaB), changes in cell cycle progression and apoptosis were analysed.As shown by a colony formation assay, lovastatin sensitized HeLa cells to gamma-radiation-induced cell killing. The lovastati…

Cyclin-Dependent Kinase Inhibitor p21G2 PhaseMAPK/ERK pathwayApoptosisBiologyHeLaCyclinspolycyclic compoundsmedicineHumansRadiology Nuclear Medicine and imagingLovastatinSensitizationRadiological and Ultrasound TechnologyKinaseNF-kappa Bnutritional and metabolic diseasesCell cyclebiology.organism_classificationCell biologyCell killingmedicine.anatomical_structureGamma RaysApoptosislipids (amino acids peptides and proteins)LovastatinHydroxymethylglutaryl-CoA Reductase InhibitorsMitogen-Activated Protein KinasesTumor Suppressor Protein p53DNA DamageHeLa Cellsmedicine.drugInternational Journal of Radiation Biology
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The role of reactive oxygen species and subsequent DNA-damage response in the emergence of resistance towards resveratrol in colon cancer models

2014

AbstractIn spite of the novel strategies to treat colon cancer, mortality rates associated with this disease remain consistently high. Tumour recurrence has been linked to the induction of resistance towards chemotherapy that involves cellular events that enable cancer cells to escape cell death. Treatment of colon cancer mainly implicates direct or indirect DNA-damaging agents and increased repair or tolerances towards subsequent lesions contribute to generate resistant populations. Resveratrol (RSV), a potent chemosensitising polyphenol, might share common properties with chemotherapeutic drugs through its indirect DNA-damaging effects reported in vitro. In this study, we investigated how…

Cyclin-Dependent Kinase Inhibitor p21SenescenceCancer ResearchProgrammed cell deathColonDNA damageColorectal cancerImmunologyApoptosisBiologyResveratrolS PhaseHistonesPolyploidyCellular and Molecular Neurosciencechemistry.chemical_compoundCell Line TumorStilbenesmedicineAnimalsHumansCHEK1Cyclin-Dependent Kinase Inhibitor p16Cell Biologymedicine.diseaseAntineoplastic Agents PhytogenicRatsGene Expression Regulation NeoplasticCheckpoint Kinase 2chemistryDrug Resistance NeoplasmResveratrolApoptosisCheckpoint Kinase 1Cancer cellImmunologyCancer researchOriginal ArticleTumor Suppressor Protein p53Reactive Oxygen SpeciesProtein KinasesDNA DamageSignal TransductionCell Death & Disease
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A p16INK4a-insensitive CDK4 mutant targeted by cytolytic T lymphocytes in a human melanoma.

1995

A mutated cyclin-dependent kinase 4 (CDK4) was identified as a tumor-specific antigen recognized by HLA-A2. 1-restricted autologous cytolytic T lymphocytes (CTLs) in a human melanoma. The mutated CDK4 allele was present in autologous cultured melanoma cells and metastasis tissue, but not in the patient's lymphocytes. The mutation, an arginine-to-cysteine exchange at residue 24, was part of the CDK4 peptide recognized by CTLs and prevented binding of the CDK4 inhibitor p16INK4a, but not of p21 or of p27KIP1. The same mutation was found in one additional melanoma among 28 melanomas analyzed. These results suggest that mutation of CDK4 can create a tumor-specific antigen and can disrupt the ce…

Cyclin-Dependent Kinase Inhibitor p21Tumor suppressor geneMutantMolecular Sequence DataCell Cycle ProteinsBiologyProtein Serine-Threonine Kinasesmedicine.disease_causeTransfectionPolymerase Chain ReactionMetastasisCell LineAntigenCyclinsProto-Oncogene ProteinsHLA-A2 AntigenmedicineTumor Cells CulturedAnimalsHumansPoint MutationAmino Acid SequenceCloning MolecularneoplasmsMelanomaCyclin-Dependent Kinase Inhibitor p16Cyclin-Dependent Kinase Inhibitor p15MutationMultidisciplinaryintegumentary systemBase SequenceMelanomaTumor Suppressor ProteinsCyclin-Dependent Kinase 4Cell cyclemedicine.diseaseCyclin-Dependent KinasesCytolysisCancer researchCarrier ProteinsMicrotubule-Associated ProteinsCyclin-Dependent Kinase Inhibitor p27T-Lymphocytes CytotoxicScience (New York, N.Y.)
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Roflumilast N-oxide reverses corticosteroid resistance in neutrophils from patients with chronic obstructive pulmonary disease

2013

Background Glucocorticoid functions are markedly impaired in patients with chronic obstructive pulmonary disease (COPD). The phosphodiesterase 4 inhibitor roflumilast N-oxide (RNO) is the active metabolite of roflumilast approved as a treatment to reduce the risk of exacerbations in patients with severe COPD. Objective We sought to characterize the differential effects of RNO versus corticosteroids and their potential additive/synergistic effect in neutrophils from patients with COPD, thus providing scientific rationale for the combination of roflumilast with corticosteroids in the clinic. Methods Peripheral blood neutrophils were isolated from patients with COPD (n = 32), smokers (n = 7), …

CyclopropanesLipopolysaccharidesMaleMAPK/ERK pathwaymedicine.medical_specialtyNeutrophilsPrimary Cell CultureImmunologyDrug ResistanceAminopyridinesGene ExpressionComplex MixturesDexamethasoneHistone DeacetylasesPhosphatidylinositol 3-KinasesPulmonary Disease Chronic ObstructiveGlucocorticoid receptorAdrenal Cortex HormonesInternal medicineTobaccomedicineHumansImmunology and AllergyMacrophage Migration-Inhibitory FactorsDexamethasoneActive metaboliteRoflumilastAgedCOPDbusiness.industryInterleukin-8Drug SynergismMiddle Agedmedicine.diseaseIntramolecular OxidoreductasesEndocrinologyMatrix Metalloproteinase 9BenzamidesMitogen-Activated Protein Kinase PhosphatasesFemaleMacrophage migration inhibitory factorPhosphodiesterase 4 InhibitorsbusinessBiomarkersGlucocorticoidmedicine.drugJournal of Allergy and Clinical Immunology
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“Cysteinyl leukotriene-1 receptor activation in a human bronchial epithelial cell line leads to signal transducer and activator of transcription 1-me…

2008

Abstract We studied the effect of leukotriene D(4) (LTD(4)) on a human bronchial epithelial cell line (16HBE) overexpressing the cysteinyl leukotriene (CysLT) (1) receptor (HBECysLT(1)R), looking at the associated signal transduction mechanisms as well as at effects on inflammatory cell adhesion. The results obtained showed that LTD(4) increases the phosphorylation of extracellular signal-regulated protein kinase (ERK) 1/2 and of the signal transducer and activator of transcription 1 (STAT-1) in serine 727 (STAT-1Ser727), resulting in increased eosinophil adhesion to HBECysLT(1)R, associated with enhanced surface expression of intercellular adhesion molecule (ICAM) 1. Pretreatment with a Cy…

CyclopropanesMAPK/ERK pathwayIndolesBronchiAcetatesSulfidesBiologyCysteinyl leukotriene-1cysteinyl leukotrieneCell LineLeukotriene D4MaleimidesInterferon-gammaCell AdhesionHumansProtein kinase ACells CulturedProtein kinase CReceptors LeukotrienePharmacologyKinaseMEK inhibitorMembrane ProteinsEpithelial CellsIntercellular Adhesion Molecule-1Intercellular adhesion moleculeCell biologyEosinophilsSTAT1 Transcription FactorQuinolinesLeukotriene AntagonistsMolecular MedicinePhosphorylationMitogen-Activated Protein KinasesSignal transduction
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Inhibition of Mitochondrial Function by Efavirenz Increases Lipid Content in Hepatic Cells

2010

Efavirenz (EFV) is a non-nucleoside reverse transcriptase inhibitor (NNRTI) widely used in human immunodeficiency virus (HIV) infection therapy. It has been associated with hepatotoxic effects and alterations in lipid and body fat composition. Given the importance of the liver in lipid regulation, we have evaluated the effects of clinically used concentrations of EFV on the mitochondria and lipid metabolism of human hepatic cells in vitro. Mitochondrial function was rapidly undermined by EFV to an extent that varied with the concentration employed; in particular, respiration and intracellular adenosine triphosphate (ATP) levels were reduced whereas reactive oxygen species (ROS) production i…

CyclopropanesMaleEfavirenzAnti-HIV AgentsRespiratory chainMitochondria LiverPharmacologyBiologyMitochondrionNucleoside Reverse Transcriptase InhibitorRats Sprague-Dawleychemistry.chemical_compoundOxygen ConsumptionAMP-Activated Protein Kinase KinasesmedicineAnimalsHumansHepatologyAMPKLipid metabolismLipid MetabolismAdenosineLipidsBenzoxazinesRatschemistryBiochemistryAlkynesHepatocytesAdenosine triphosphateProtein Kinasesmedicine.drug
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Isoenzyme-specific phosphorylation of cytochromes P-450 and other drug metabolizing enzymes.

1987

Abstract A series of fourteen cytochrome P-450 isoenzymes was treated with three different protein kinases and found to devide into isoenzymes phosphorylated (i) by both the cyclic AMP-dependent kinase and the calcium-phospholipid-dependent kinase (P-450 PB 3a and PB 2e), (ii) by none of these kinases (P-450 PB 1b, MC 1b, UT 1, and thromboxane synthase), and (iii) by either the cyclic AMP-dependent kinase (P-450 LM 2, PB 2d, and PB 3b) or the calcium-phospholipid-dependent kinase (P-450 PB 1a, PB 2a, MC 1a, LM 3c, and LM 4). Other components of the monooxygenase system, cytochrome P-450 reductase, cytochrome b5, cytochrome b5 reductase as well as microsomal epoxide hydrolase, were poor subs…

CytochromeBiophysicsReductaseBiochemistrySubstrate SpecificityCytochrome P-450 Enzyme SystemCytochrome b5Cyclic AMPAnimalsPhosphorylationMolecular BiologyCytochrome b5 reductaseProtein Kinase CGlutathione TransferasebiologyChemistryKinaseCell BiologyMonooxygenaseMolecular biologyRatsIsoenzymesBiochemistryPharmaceutical PreparationsMicrosomal epoxide hydrolasebiology.proteinThromboxane-A synthaseRabbitsCasein KinasesProtein KinasesBiochemical and biophysical research communications
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Phosphorylation of rabbit liver cytochrome P-450 LM2 and its effect on monooxygenase activity

1984

The phosphorylation of rabbit liver microsomal cytochrome P-450 LM2 by catalytic subunit of cyclic AMP-dependent protein kinase (W. Pyerin et al. (1983) Carcinogenesis 4, 573) has now been studied in detail with purified soluble form of cytochrome P-450 as well as with the purified protein incorporated into model membranes. The apparent Km values for P-450 of the phosphorylation reaction in all experimental systems were in a range of 2-8 microM, while the Vmax values were dependent on the state of P-450. Upon phosphorylation, the reconstituted enzyme activities with benzphetamine (N-demethylation) and 7-ethoxycoumarin (O-deethylation) as substrates were reduced to 30-40% of control.

CytochromeProtein subunitBiophysicsBiochemistryMixed Function OxygenasesCytochrome P-450 Enzyme SystemmedicineAnimalsPhosphorylationProtein kinase AMolecular Biologychemistry.chemical_classificationbiologyKinaseCell BiologyMolecular biologyKineticsEnzymechemistryBiochemistryPhenobarbitalMicrosomes Liverbiology.proteinMicrosomePhosphorylationRabbitsBenzphetamineProtein Kinasesmedicine.drugBiochemical and Biophysical Research Communications
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