Search results for " Cell Cycle"

showing 10 items of 92 documents

Synthesis and induction of G0–G1 phase arrest with apoptosis of 3,5-dimethyl-6-phenyl-8-(trifluoromethyl)-5,6-dihydropyrazolo[3,4-f][1,2,3,5]tetrazep…

2007

The multistep synthesis of 3,5-dimethyl-6-phenyl-8-(trifluoromethyl)-5,6-dihydropyrazolo[3,4-f][1,2,3,5]tetrazepin-4(3H)-one 15 has been carried out. The compound showed antiproliferative and apoptotic effects against K562, K562-R (imatinib mesilate resistant), HL60 and multidrug resistant (MDR) HL60 cell lines. Compound 15 showed a pro-apoptotic activity against HL60 and K562 resistant cell lines markedly higher than etoposide and busulfan, respectively. Flow cytometry studies carried out on K562 cells allowed to establish that 15 induces G0-G1 phase arrest followed by apoptosis.

HL60StereochemistryApoptosisHL-60 CellsAntiproliferative activityResting Phase Cell CycleChemical synthesisPyrazolo[34-f][1234]tetrazepinoneFlow cytometrychemistry.chemical_compoundhemic and lymphatic diseasesDrug DiscoverymedicineHumansCytotoxicityEtoposideG0-G1 arrestPharmacologyTrifluoromethylMolecular Structuremedicine.diagnostic_testOrganic ChemistryG1 PhaseApoptosiAzepinesGeneral MedicineSettore CHIM/08 - Chimica FarmaceuticaMolecular biologyMultiple drug resistancechemistryApoptosisDrug resistancePyrazoles1234-TetrazepinoneK562 Cellsmedicine.drugEuropean Journal of Medicinal Chemistry
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3-[4-(1H-indol-3-yl)-1,3-thiazol-2-yl]-1H-pyrrolo[2,3-b]pyridines, nortopsentin Analogues with antiproliferative activity

2015

A new series of nortopsentin analogues, in which the imidazole ring of the natural product was replaced by thiazole and the indole unit bound to position 2 of the thiazole ring was substituted by a 7-azaindole moiety, was efficiently synthesized. Two of the new nortopsentin analogues showed good antiproliferative effect against the totality of the NCI full panel of human tumor cell lines (~60) having GI50 values ranging from low micromolar to nanomolar level. The mechanism of the antiproliferative effect of these derivatives, investigated on human hepatoma HepG2 cells, was pro-apoptotic, being associated with externalization of plasma membrane phosphatidylserine and mitochondrial dysfunctio…

IndolesHalogenationPyridines3-b]pyridinesPharmaceutical ScienceApoptosisAntiproliferative activity3-[4-(1<i>H</i>-indol-3-yl)-13-thiazol-2-yl]-1<i>H</i>-pyrrolo[23-<i>b</i>]pyridineschemistry.chemical_compoundNeoplasmsDrug DiscoveryImidazoleMoietyindolyl alkaloidsPharmacology Toxicology and Pharmaceutics (miscellaneous)lcsh:QH301-705.5Membrane Potential MitochondrialMolecular Structure3-[4-(1H-indol-3-yl)-1; 3-thiazol-2-yl]-1H-pyrrolo[2; 3-b]pyridines; Antiproliferative activity; Indolyl alkaloids; Marine alkaloids; Nortopsentin analogues; Drug Discovery3003 Pharmaceutical ScienceImidazolesPhosphatidylserineMitochondrianortopsentin analoguesIndolyl alkaloidmarine alkaloidsG2 PhaseStereochemistryNortopsentin analogueAntineoplastic AgentsMethylationResting Phase Cell CycleArticleAlkaloids3-[4-(1H-indol-3-yl)-1Cell Line TumorHumansPyrroles3-[4-(1H-indol-3-yl)-13-thiazol-2-yl]-1H-pyrrolo[23-b]pyridines3-thiazol-2-yl]-1H-pyrrolo[2ThiazoleCell ProliferationIndole testNatural productCell growthDrug Discovery3003 Pharmaceutical ScienceSettore CHIM/08 - Chimica FarmaceuticaThiazoleschemistrylcsh:Biology (General)Cell cultureDrug DesignMarine alkaloid3-[4-(1H-indol-3-yl)-13-thiazol-2-yl]-1H-pyrrolo[23-b]pyridine
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The novel dual PI3K/mTOR inhibitor GDC-0941 synergizes with the MEK inhibitor U0126 in non-small cell lung cancer cells.

2011

Lung cancer is a malignant disease with poor outcome, which has led to a search for new therapeutics. The PI3K/Akt/mTOR and Ras/raf/Erk pathways are key regulators of tumor growth and survival. In the present study, their roles were evaluated by MTT assay, flow cytometry and Western blotting in lung cancer cells. We found that a high efficacy of antitumor activity was shown with GDC-0941 treatment in two gefitinib-resistant non-small cell lung cancer (NSCLC) cell lines, A549 and H460. In addition, H460 cells with activating mutations of PIK3CA were relatively more sensitive to GDC-0941 than A549 cells with wild-type PIK3CA. Furthermore, GDC-0941 was highly efficacious in combination with U0…

MAPK/ERK pathwayCancer ResearchIndazolesLung NeoplasmsApoptosisBiologyBiochemistryPhosphatidylinositol 3-KinasesCarcinoma Non-Small-Cell LungCell Line TumorNitrilesGeneticsmedicineButadienesHumansMolecular BiologyProtein kinase BProtein Kinase InhibitorsPI3K/AKT/mTOR pathwayPhosphoinositide-3 Kinase InhibitorsSulfonamidesOncogeneCell growthMEK inhibitorTOR Serine-Threonine KinasesCancerDrug SynergismCell cyclemedicine.diseaseG1 Phase Cell Cycle Checkpointsrespiratory tract diseasesEnzyme ActivationOncologyCancer researchMolecular MedicineMitogen-Activated Protein KinasesSignal TransductionMolecular medicine reports
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Involvement of the transcription factor FoxM1 in contact inhibition

2012

Contact inhibition is a crucial mechanism regulating proliferation in vitro and in vivo. Although it is generally accepted that contact inhibition plays a pivotal role in maintaining tissue homeostasis, the molecular mechanisms of contact inhibition are still not fully understood. FoxM1 is known as a proliferation-associated transcription factor and is upregulated in many cancer types. Vice versa, anti-proliferative signals, such as TGF-β and differentiation signals decrease FoxM1 expression. Here we investigated the role of FoxM1 in contact inhibition in fibroblasts. We show that protein expression of FoxM1 is severely and rapidly downregulated upon contact inhibition, probably by inhibiti…

MAPK/ERK pathwayCyclin ABiophysicsDown-RegulationCell Cycle ProteinsCyclin AProtein Serine-Threonine KinasesBiochemistryMiceDownregulation and upregulationProto-Oncogene ProteinsAnimalsPhosphorylationRNA Small InterferingExtracellular Signal-Regulated MAP KinasesMolecular BiologyTranscription factorTissue homeostasisbiologyContact InhibitionKinaseForkhead Box Protein M1Contact inhibitionForkhead Transcription FactorsCell BiologyG1 Phase Cell Cycle CheckpointsCell biologyNIH 3T3 Cellsbiology.proteinEctopic expressionBiochemical and Biophysical Research Communications
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A phosphorylation cycle shapes gradients of the DYRK family kinase Pom1 at the plasma membrane.

2011

http://linkinghub.elsevier.com/; International audience; Concentration gradients regulate many cell biological and developmental processes. In rod-shaped fission yeast cells, polar cortical gradients of the DYRK family kinase Pom1 couple cell length with mitotic commitment by inhibiting a mitotic inducer positioned at midcell. However, how Pom1 gradients are established is unknown. Here, we show that Tea4, which is normally deposited at cell tips by microtubules, is both necessary and, upon ectopic cortical localization, sufficient to recruit Pom1 to the cell cortex. Pom1 then moves laterally at the plasma membrane, which it binds through a basic region exhibiting direct lipid interaction. …

MESH : Molecular Sequence Data[SDV]Life Sciences [q-bio]CellMESH: Cell CycleMESH: Amino Acid SequenceAmino Acid Sequence; Cell Cycle; Cell Membrane/metabolism; Microtubule-Associated Proteins/metabolism; Molecular Sequence Data; Phosphorylation; Protein Kinases/chemistry; Protein Kinases/metabolism; Schizosaccharomyces/cytology; Schizosaccharomyces/metabolism; Schizosaccharomyces pombe Proteins/metabolism; Sequence AlignmentMESH : Phosphorylation0302 clinical medicinePhosphorylation0303 health sciencesKinaseMESH : Amino Acid SequenceMESH : Sequence AlignmentCell CycleCortical gradientMESH : Schizosaccharomyces pombe ProteinsFission yeastCell biologymedicine.anatomical_structureMESH: SchizosaccharomycesPom1PhosphorylationMicrotubule-Associated ProteinsMESH : Cell MembraneMolecular Sequence DataMESH: Sequence AlignmentMESH : Protein KinasesBiologyGeneral Biochemistry Genetics and Molecular BiologyPom1Dephosphorylation03 medical and health sciencesMicrotubuleMESH : Cell CycleSchizosaccharomycesCell cortexmedicineAmino Acid SequenceMitosisMESH: Protein Kinases030304 developmental biologyMESH: Molecular Sequence Data[ SDV ] Life Sciences [q-bio]Phosphorylation cycleMESH: PhosphorylationBiochemistry Genetics and Molecular Biology(all)Cell MembraneMESH: Schizosaccharomyces pombe ProteinsMESH: Microtubule-Associated ProteinsMESH : SchizosaccharomycesMESH : Microtubule-Associated ProteinsSchizosaccharomyces pombe ProteinsDYRK family kinaseProtein KinasesSequence Alignment030217 neurology & neurosurgeryMESH: Cell Membrane
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Sodium butyrate with UCN-01 has marked antitumour activity against cervical cancer cells.

2010

The effect of combining sodium butyrate (NaB), a histone deacetylase inhibitor, and 7-hydroxy-staurosporine (UCN-01) on cytotoxicity in human cervical carcinoma cells was evaluated.HeLa and CaSki cells were treated using NaB alone or in combination with staurosporine (STS) or its analog UCN-01. Cytotoxicity was determined by flow cytometry and morphological assays. Apoptotic pathways were characterized by Western blotting and immunostaining. CaSki cells were also xenografted into nude mice to assess the in vivo effects of NaB/UCN-01 combination.Treatment with NaB and STS or UCN-01 resulted in enhanced apoptosis of cancer cells. Apoptosis involved mitochondrial pathways and overexpression of…

MESH : StaurosporineMESH : Hela CellsMESH : Antineoplastic Combined Chemotherapy Protocolshealth care facilities manpower and servicesUterine Cervical NeoplasmsMESH: ButyratesMESH: Cell CycleApoptosisMESH: Papillomavirus Infections[ SDV.CAN ] Life Sciences [q-bio]/CancerMiceAntineoplastic Combined Chemotherapy ProtocolsMESH: AnimalsMESH: Human papillomavirus 18MESH : Human papillomavirus 18MESH : Femalehealth care economics and organizationsMESH: Human papillomavirus 16MESH : Papillomavirus InfectionsHuman papillomavirus 16Human papillomavirus 18Cell CycleMESH : Mice NudeMESH: Uterine Cervical NeoplasmsMESH: Antineoplastic Combined Chemotherapy ProtocolsButyratesMESH: Cell Growth ProcessesFemaleMESH: Xenograft Model Antitumor Assaysendocrine systemMESH: Cell Line TumoreducationMESH : Uterine Cervical NeoplasmsMice Nude[SDV.CAN]Life Sciences [q-bio]/CancerCell Growth ProcessesMESH : Xenograft Model Antitumor Assays[SDV.CAN] Life Sciences [q-bio]/CancerCell Line TumorMESH : ButyratesMESH : MiceMESH : Cell CycleMESH: Mice Nudeotorhinolaryngologic diseasesAnimalsHumansMESH: MiceMESH: HumansMESH : Cell Line TumorMESH: ApoptosisPapillomavirus InfectionsMESH : HumansMESH : Human papillomavirus 16StaurosporineXenograft Model Antitumor AssaysMESH: Hela CellsMESH : Cell Growth ProcessesMESH: StaurosporineMESH : AnimalsMESH: FemaleMESH : ApoptosisHeLa Cells
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Use of CDC2 from etoposide-treated cells as substrate to assay CDC25 phosphatase activity

1999

International audience; Cyclin-dependent kinases (CDKs) regulate the key transition of the cell cycle in all organisms. In response to Etoposide (VP-16) induced DNA damage, cells undergo a G2-phase arrest resulting in the accumulation of inactive CDK1 (CDC2) kinase complexes. Here we report that upon Etoposide treatment CDC2 is phosphorylated on tyrosine 15 and is dephosphorylated and activated in vitro by recombinant CDC25 phosphatase. We also show that inactive CDC2 kinase from Etoposide-treated cells can be used as a substrate in a sensitive two-step assay of CDC25 phosphatase. This assay, which is very simple to set-up, is based on the monitoring of CDC2 kinase activity after CDC25-depe…

MESH: HumansMESH: Phosphorylation[SDV]Life Sciences [q-bio]Cell Cycle Proteins[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]MESH: CDC2 Protein KinaseMESH: Tyrosine[SDV] Life Sciences [q-bio]AGENT ANTITUMORALenzymes and coenzymes (carbohydrates)MESH: Cell Cycle ProteinsMESH: cdc25 PhosphatasesCDC2 Protein KinaseMESH: HeLa CellsMESH: Phosphoprotein PhosphatasesPhosphoprotein PhosphatasesHumansTyrosinecdc25 PhosphatasesPhosphorylationbiological phenomena cell phenomena and immunityEtoposideHeLa CellsMESH: Etoposide
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p14(ARF) Prevents Proliferation of Aneuploid Cells by Inducing p53-Dependent Apoptosis.

2014

Weakening the Spindle Assembly Checkpoint by reduced expression of its components induces chromosome instability and aneuploidy that are hallmarks of cancer cells. The tumor suppressor p14(ARF) is overexpressed in response to oncogenic stimuli to stabilize p53 halting cell progression. Previously, we found that lack or reduced expression of p14(ARF) is involved in the maintenance of aneuploid cells in primary human cells, suggesting that it could be part of a pathway controlling their proliferation. To investigate this aspect further, p14(ARF) was ectopically expressed in HCT116 cells after depletion of the Spindle Assembly Checkpoint MAD2 protein that was used as a trigger for aneuploidy. …

Mad2 ProteinApoptosis; M Phase Cell Cycle Checkpoints; Mad2 Proteins; RNA Interference; Tumor Suppressor Protein p14ARF; AneuploidyApoptosiMitosisApoptosisM Phase Cell Cycle CheckpointAneuploidyHCT116 CellsSettore BIO/18 - GeneticaGene Knockout TechniquesMad2 ProteinsTumor Suppressor Protein p14ARFHumansM Phase Cell Cycle CheckpointsRNA InterferenceTumor Suppressor Protein p53Cell ProliferationJournal of cellular physiology
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Expression of spindle assembly checkpoint proteins BubR1 and Mad2 expression as potential biomarkers of malignant transformation of oral leukoplakia:…

2021

Background The Spindle Assembly Checkpoint (SAC) is a surveillance mechanism essential to ensure the accuracy of chromosome segregation during mitosis. Our aim was to evaluate the expression of SAC proteins in oral carcinogenesis, and to assess their potential in predicting malignant transformation of oral leukoplakia. Material and Methods We analysed the immunoexpression of BubR1, Mad2, Bub3, and Spindly proteins in 64 oral biopsies from 52 oral leukoplakias and 12 normal tissues. Univariate and multivariate analysis were performed to evaluate predictive factors for malignant transformation (MT). Results We observed that BubR1 and Mad2 were more highly expressed in high dysplasia grade les…

Mad2BUB3medicine.disease_causeMalignant transformationOral Cancer and Potentially malignant disordersmedicineoral dysplasiawnt ligandsHumansGeneral DentistryMitosisUNESCO:CIENCIAS MÉDICASLeukoplakiadestruction complexbusiness.industryResearchoral cancermedicine.disease?-cateninSpindle checkpointstomatognathic diseasesCell Transformation NeoplasticOtorhinolaryngologyDysplasiaMad2 ProteinsCancer researchM Phase Cell Cycle CheckpointsSurgeryLeukoplakia OralbusinessCarcinogenesisBiomarkersMedicina Oral, Patología Oral y Cirugía Bucal
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Rac1 GTPase, a multifunctional player in the regulation of genotoxic stress response

2013

The Ras-related C3 botulinum toxin substrate 1 (Rac1) belongs to the Ras-homologous (Rho) family of small GTPases, which transduce signals from the outside to the inside of a cell. Rac1 becomes activated upon ligand binding of a variety of receptors, including receptor tyrosine kinases and heterotrimeric G-protein-coupled receptors. After GTP loading by guanine exchange factors (GEFs), GTP-bound Rac1 engages numerous effector proteins, thereby eventually regulating cell motility and adhesion, cell cycle progression through G1, mitosis and meiosis, as well as cell death and metastasis.1 Besides, Rac1 adjusts cellular responses to genotoxic agents, such as UV light and alkylating agents, by r…

Malerac1 GTP-Binding Proteintopoisomerase IIAgingRHOADNA repairDNA damagep38 mitogen-activated protein kinasesApoptosisRAC1Editorials: Cell Cycle FeaturesDNA damage responseReceptor tyrosine kinasechemical carcinogenesisHistonesMiceTransforming Growth Factor betaRho GTPasesAnimalsMolecular BiologyTranscription factoranthracyclinesMice KnockoutbiologyKinaseNeuropeptidesConnective Tissue Growth FactorHMG-CoA reductase inhibitors (statins)Cell BiologyFibrosisgenotoxic stressActinsrac GTP-Binding ProteinsCell biologyOxidative Stressnormal tissue damageGene Expression RegulationLiverBiochemistryDoxorubicinGamma Raysbiology.proteinFemaleDNA DamageMutagensSignal TransductionDevelopmental BiologyCell Cycle
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