Search results for "CELLULAR"

showing 10 items of 6449 documents

Highlighting curcumin-induced crosstalk between autophagy and apoptosis: A biochemical approach coupling impedancemetry, imaging, and flow cytometry

2019

Curcumin, a major active component of turmeric (Curcuma longa, L.), is known to have various effects on both healthy and cancerous tissues. In vitro studies suggest that curcumin inhibits cancer cell growth by activating apoptosis, but the mechanism underlying the anticancer effects of curcumin is still unclear. Since there is a consensus about endoplasmic reticulum (ER) stress being involved in the cytotoxicity of many natural compounds, we investigated by Amnis ® Imaging flow cytome-try the mechanistic aspects of curcumin's destabilization of the ER, but also the status of the lysosomal compartment involved in curcumin-associated apoptosis. Curcumin induces ER stress thereby causing an un…

Programmed cell death[SDV]Life Sciences [q-bio][SDV.TOX.TVM]Life Sciences [q-bio]/Toxicology/Vegetal toxicology and mycotoxicology[SDV.CAN]Life Sciences [q-bio]/Cancer[SDV.BC]Life Sciences [q-bio]/Cellular Biology[SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Mitochondrion03 medical and health scienceschemistry.chemical_compound0302 clinical medicine[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology030304 developmental biology0303 health sciencesChemistryAutophagy[SDV.BBM.MN]Life Sciences [q-bio]/Biochemistry Molecular Biology/Molecular Networks [q-bio.MN]Cell cycle3. Good healthCell biology[SDV.BBM.BP]Life Sciences [q-bio]/Biochemistry Molecular Biology/BiophysicsApoptosis030220 oncology & carcinogenesis[SDV.TOX]Life Sciences [q-bio]/ToxicologyCancer cellUnfolded protein responseCurcumin
researchProduct

Highlighting Curcumin-Induced Crosstalk between Autophagy and Apoptosis as Supported by Its Specific Subcellular Localization

2020

Curcumin, a major active component of turmeric (Curcuma longa, L.), is known to have various effects on both healthy and cancerous tissues. In vitro studies suggest that curcumin inhibits cancer cell growth by activating apoptosis, but the mechanism underlying the anticancer effect of curcumin is still unclear. Since there is a recent consensus about endoplasmic reticulum (ER) stress being involved in the cytotoxicity of natural compounds, we have investigated using Image flow cytometry the mechanistic aspects of curcumin&rsquo

Programmed cell deathautophagyCell Membrane PermeabilityCurcumin[SDV]Life Sciences [q-bio][SDV.BC.BC]Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Article03 medical and health scienceschemistry.chemical_compound0302 clinical medicineLysosomeCell Line TumorxCELLigencemedicine[SDV.BC.BC] Life Sciences [q-bio]/Cellular Biology/Subcellular Processes [q-bio.SC]Humanscancerlcsh:QH301-705.5030304 developmental biologyreal-time cellular impedanceCell Nucleus0303 health sciencescalciumEndoplasmic reticulumAutophagyapoptosisROSGeneral Medicine3. Good healthCell biologyMitochondriaendoplasmic reticulummedicine.anatomical_structurecell deathchemistrylcsh:Biology (General)Apoptosis030220 oncology & carcinogenesisCancer cellCurcuminUnfolded protein responseUnfolded Protein ResponselysosomeLysosomes[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologySubcellular Fractions
researchProduct

The Role of Autophagy and Apoptosis During Embryo Development

2015

Programmed cell death (PCD) and cell survival are two sides of the same coin. Autopha‐ gy and apoptosis are crucial processes during embryo development of Invertebrates and Vertebrates organisms, as they are necessary for the formation of a new organism, start‐ ing from a fertilized egg. Fertilization triggers cell remodeling from each gamete to a toti‐ potent zygote. During embryogenesis, the cells undergo various processes, thus allowing the transformation of the embryo into an adult organism. In particular, cells require the appropriate tools to suddenly modify their morphology and protein content in order to respond to intrinsic and external stimuli. Autophagy and apoptosis are involved…

Programmed cell deathbiologyAutophagyCellMorphogenesisEmbryobiology.organism_classificationEmbryonic stem cellCell biologyMulticellular organismmedicine.anatomical_structuremedicineSettore BIO/06 - Anatomia Comparata E CitologiaDrosophila melanogasterCell death apoptosis-autophagy crosstalk stress differentiation embryo model systems
researchProduct

Autophagy-Dependent Anticancer Immune Responses Induced by Chemotherapeutic Agents in Mice

2011

Antineoplastic chemotherapies are particularly efficient when they elicit immunogenic cell death, thus provoking an anticancer immune response. Here we demonstrate that autophagy, which is often disabled in cancer, is dispensable for chemotherapy-induced cell death but required for its immunogenicity. In response to chemotherapy, autophagy-competent, but not autophagy-deficient, cancers attracted dendritic cells and T lymphocytes into the tumor bed. Suppression of autophagy inhibited the release of adenosine triphosphate (ATP) from dying tumor cells. Conversely, inhibition of extracellular ATP-degrading enzymes increased pericellular ATP in autophagy-deficient tumors, reestablished the recr…

Programmed cell deathcells cancer immunogenicity calreticulin exposure hmgb1Antineoplastic AgentsBiologyimmunogenicityNOMicechemistry.chemical_compoundAdenosine TriphosphateImmune systemCell Line TumorNeoplasmsAutophagyExtracellularAnimalsHumanscancerMice Inbred BALB CMultidisciplinaryCell DeathImmunogenicityAutophagyDendritic CellsMice Inbred C57BLhmgb1chemistryCell cultureCancer researchImmunogenic cell deathcellsMitoxantroneCalreticulinAdenosine triphosphatecalreticulin exposure
researchProduct

Role of oxoproline in the regulation of neutral amino acid transport across the blood-brain barrier.

1996

Regulation of neutral amino acid transport was studied using isolated plasma membrane vesicles derived from the bovine blood-brain barrier. Neutral amino acids cross the blood-brain barrier by facilitative transport system L1, which may allow both desirable and undesirable amino acids to enter the brain. The sodium-dependent amino acid systems A and Bo,+ are located exclusively on abluminal membranes, in a position to pump unwanted amino acids out. gamma-Glutamyl transpeptidase, the first enzyme of the gamma-glutamyl cycle, is an integral protein of the luminal membrane of the blood-brain barrier. We demonstrate that oxoproline, an intracellular product of the gamma-glutamyl cycle, stimulat…

ProlineBiologyBlood–brain barrierBiochemistrySystem aNeutral amino acid transportmedicineAnimalsAmino AcidsMolecular BiologyIntegral membrane proteinchemistry.chemical_classificationCell MembraneBiological TransportCell BiologyAmino acidCapillariesKineticsMembraneEnzymemedicine.anatomical_structureBiochemistrychemistryBlood-Brain BarrierCattleEndothelium VascularIntracellularThe Journal of biological chemistry
researchProduct

Dynamical properties of water in living cells

2018

With the aim of studying the effect of water dynamics on the properties of biological systems, in this paper, we present a quasi-elastic neutron scattering study on three different types of living cells, differing both in their morphological and tumor properties. The measured scattering signal, which essentially originates from hydrogen atoms present in the investigated systems, has been analyzed using a global fitting strategy using an optimized theoretical model that considers various classes of hydrogen atoms and allows disentangling diffusive and rotational motions. The approach has been carefully validated by checking the reliability of the calculation of parameters and their 99% confi…

Properties of waterScale (ratio)HydrogenPhysics and Astronomy (miscellaneous)chemistry.chemical_elementNeutron scattering010402 general chemistrySpace (mathematics)01 natural sciencesSignalchemistry.chemical_compoundOpticsquasi-elastic neutron scatteringwater structure and dynamicintracellular water0103 physical sciences010306 general physicsintracellular water; quasi-elastic neutron scattering; water structure and dynamics; Physics and Astronomy (miscellaneous)Physicsbusiness.industryScatteringSettore FIS/07 - Fisica Applicata(Beni Culturali Ambientali Biol.e Medicin)0104 chemical scienceswater structure and dynamicschemistryPicosecondbusinessBiological system
researchProduct

The N-glycan processing in HT-29 cells is a function of their state of enterocytic differentiation. Evidence for an atypical traffic associated with …

1991

International audience; When the human colon cancer cells HT-29 undergo enterocytic differentiation, they correctly process their N-glycans, whereas their undifferentiated counterpart are unable to process Man9-8-GlcNAc2 species, the natural substrate of alpha-mannosidase I. As this enzyme is fully active in both HT-29 cell populations, we hypothesize that N-glycoproteins are unable to reach the cis Golgi, the site where alpha-mannosidase I has been localized. We have demonstrated this point by using 1-deoxymannojirimycin, leupeptin, and monensin. In the presence of 1-deoxymannojirimycin, a specific inhibitor of alpha-mannosidase I, differentiated HT-29 cells, as expected, accumulate Man9-8…

Proteases1-DeoxynojirimycinColonLeupeptinsCellular differentiationCellIn Vitro TechniquesBiologyBiochemistry03 medical and health sciencessymbols.namesakechemistry.chemical_compoundPolysaccharidesalpha-Mannosidase[ CHIM.ORGA ] Chemical Sciences/Organic chemistryMannosidasesTumor Cells CulturedmedicineHumansMonensinMolecular Biology030304 developmental biologychemistry.chemical_classificationGlucosamine0303 health sciencesMembrane Glycoproteins[CHIM.ORGA]Chemical Sciences/Organic chemistryEndoplasmic reticulum030302 biochemistry & molecular biologyLeupeptinBiological TransportCell DifferentiationCell BiologyCompartment (chemistry)Golgi apparatus[CHIM.ORGA] Chemical Sciences/Organic chemistrymedicine.anatomical_structureBiochemistrychemistryColonic NeoplasmssymbolsGlycoproteinProtein Processing Post-Translational
researchProduct

Processing of tetanus and botulinum A neurotoxins in isolated chromaffin cells.

1995

Tetanus and botulinum A neurotoxins were introduced into the cytosol of chromaffin cells by means of an electric field in which the plasma membrane is forced to form pores of approximately 1 micron at the sites facing the electrodes. As demonstrated by electron microscopy, both [125I] and gold-labelled tetanus toxin (TeTx) diffuse through these transient openings. Dichain-TeTx, with its light chain linked to the heavy chain by means of a disulfide bond, causes the block of exocytosis to develop more slowly than does the purified light chain. The disulfide bonds, which in both toxins hold the subunits together, were cleaved by the intrinsic thioredoxin-reductase system. Single chain TeTx, in…

ProteasesBotulinum ToxinsCell Membrane PermeabilityProteolysisImmunoglobulin light chainmedicine.disease_causeExocytosisExocytosisTetanus ToxinmedicinePeptide bondAnimalsCells CulturedPharmacologymedicine.diagnostic_testToxinChemistryGeneral MedicineCytosolMicroscopy ElectronElectroporationBiochemistryAdrenal MedullaBiophysicsMicroscopy Electron ScanningCattleIntracellularNaunyn-Schmiedeberg's archives of pharmacology
researchProduct

Heat shock proteins in hematopoietic malignancies

2012

Inducible heat shock proteins are molecular chaperones whose expression is increased after many different types of stress. They have a protective function helping the cell to cope with lethal conditions. Their basal expression is low in nonstressed, normal and nontransformed cells. However, in cancer cells and particularly in hematological malignancies, they are surprisingly abundant. Malignant cells have to rewire their metabolic requirements and therefore have a higher need for chaperones. This cancer cell addiction for HSPs is the basis for the use of HSP inhibitors in cancer therapy. HSPs have been shown to interact with different key apoptotic proteins. As a result, HSPs can essentiall…

ProteasesCell SurvivalCellular differentiationCellHSP27 Heat-Shock ProteinsApoptosisModels Biological03 medical and health sciences0302 clinical medicineHeat shock proteinmedicineAnimalsHumansHSP70 Heat-Shock ProteinsHSP90 Heat-Shock ProteinsHeat-Shock ProteinsCaspaseCell Proliferation030304 developmental biology0303 health sciencesbiologyCell DifferentiationCell BiologyNeoplasm Proteins3. Good healthCell biologyHaematopoiesismedicine.anatomical_structureApoptosisHematologic NeoplasmsMyelodysplastic Syndromes030220 oncology & carcinogenesisCancer cellbiology.proteinProtein Processing Post-TranslationalMolecular ChaperonesSignal TransductionExperimental Cell Research
researchProduct

Morpholino knockdown of the ubiquitously expressed transmembrane serine protease TMPRSS4a in zebrafish embryos exhibits severe defects in organogenes…

2011

AbstractOver the past years the members of the type II transmembrane serine protease (TTSP) family have emerged as new players in mammalian biology. TMPRSS4 (transmembraneprotease/serine) is overexpressed in several human cancer tissues, promoting invasion, migration, and metastasis. However, the physiological function has not yet been elucidated. Here, we present morpholino knockdown studies targeting TMPRSS4a, a homolog of human TMPRSS4 in zebrafish embryos. By RT-PCR, we could demonstrate an expression of this protease already 5 h post-fertilization, suggesting important functions in the early stages of embryonic development. Indeed,in vivogene silencing caused severe defects in tissue d…

ProteasesEmbryo NonmammalianMorpholinoOrganogenesisCellular differentiationmedicine.medical_treatmentMolecular Sequence DataClinical BiochemistryBiologyBiochemistry03 medical and health sciences0302 clinical medicineCell AdhesionmedicineAnimalsHumansAmino Acid SequenceCell adhesionMolecular BiologyPhylogenyZebrafish030304 developmental biologySerine protease0303 health sciencesProteaseCell adhesion moleculeGene Expression ProfilingSerine EndopeptidasesProteolytic enzymesGene Expression Regulation DevelopmentalMembrane ProteinsCell DifferentiationZebrafish ProteinsMolecular biologyGene Knockdown Techniques030220 oncology & carcinogenesisbiology.proteinSequence AlignmentBiological Chemistry
researchProduct