Search results for "Intracellular"

showing 10 items of 821 documents

Glial ion transport and volume control.

1991

K(+)-induced glial swelling results from an intricate interaction of transport and diffusion processes and metabolic stimulation, with many open questions remaining. Our concept of the major mechanisms involved can be summarized as follows: high extracellular K+ causes a burst-like stimulation of Na+/K+ ATPase and, hence, increases the metabolic demands. Lactate is produced; the cell is slightly acidified. To maintain a normal intracellular pH, the Na+/K+ antiporter extrudes protons and supplies Na+ for further Na+/K+ exchange. In addition, K+ ions enter the cell via membrane channels or furosemide-inhibitable transport. K+, Cl-, and lactate- ions accumulate as the osmotic basis for cell sw…

IonsbiologyChemistryGeneral NeuroscienceATPaseAntiporterIntracellular pHStimulationBiological TransportFlow CytometryGeneral Biochemistry Genetics and Molecular BiologyHistory and Philosophy of ScienceBody WaterExtracellularbiology.proteinBiophysicsPotassiumTumor Cells CulturedMembrane channelQuercetinNeurogliaHomeostasisIon transporterAnnals of the New York Academy of Sciences
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Iron, oxidative stress, and redox signaling in the cardiovascular system.

2014

The redox state of the cell is predominantly dependent on an iron redox couple and is maintained within strict physiological limits. Iron is an essential metal for hemoglobin synthesis in erythrocytes, for oxidation-reduction reactions, and for cellular proliferation. The maintenance of stable iron concentrations requires the coordinated regulation of iron transport into plasma from dietary sources in the duodenum, from recycled senescent red cells in macrophages, and from storage in hepatocytes. The absorption of dietary iron, which is present in heme or nonheme form, is carried out by mature villus enterocytes of the duodenum and proximal jejunum. Multiple physiological processes are invo…

Iron Overloadmedicine.disease_causeRedoxCardiovascular Systemchemistry.chemical_compound[SDV.MHEP.CSC]Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular systemHepcidinExtracellularmedicineAnimalsHumansHemeTranscription factorComputingMilieux_MISCELLANEOUSchemistry.chemical_classificationReactive oxygen speciesbiologyOxidants[SDV.MHEP.CSC] Life Sciences [q-bio]/Human health and pathology/Cardiology and cardiovascular systemOxidative StresschemistryBiochemistryCardiovascular Diseasesbiology.proteinOxidation-ReductionIntracellularOxidative stressIron DietaryFood ScienceBiotechnologySignal TransductionMolecular nutritionfood research
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O2 as the regulatory signal for FNR-dependent gene regulation in Escherichia coli

1996

With an oxystat, changes in the pattern of expression of FNR-dependent genes from Escherichia coli were studied as a function of the O2 tension (pO2) in the medium. Expression of all four tested genes was decreased by increasing O2. However, the pO2 values that gave rise to half-maximal repression (pO(0.5)) were dependent on the particular promoter and varied between 1 and 5 millibars (1 bar = 10(5) Pa). The pO(0.5) value for the ArcA-regulated succinate dehydrogenase genes was in the same range (pO(0.5) = 4.6 millibars). At these pO2 values, the cytoplasm can be calculated to be well supplied with O2 by diffusion. Therefore, intracellular O2 could provide the signal to FNR, suggesting that…

Iron-Sulfur ProteinsCellular respirationRepressorBiologymedicine.disease_causeMicrobiologyElectron TransportBacterial ProteinsGenes RegulatorEscherichia colimedicineAnaerobiosisMolecular BiologyEscherichia coliRegulation of gene expressionchemistry.chemical_classificationEscherichia coli ProteinsSuccinate dehydrogenaseMembrane ProteinsGene Expression Regulation BacterialElectron transport chainAerobiosisOxygenRepressor ProteinsSuccinate DehydrogenaseEnzymeLac OperonchemistryBiochemistryGenes BacterialMutationbiology.proteinOxidation-ReductionProtein KinasesIntracellularBacterial Outer Membrane ProteinsSignal TransductionResearch ArticleJournal of Bacteriology
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Yeast Dun1 Kinase Regulates Ribonucleotide Reductase Inhibitor Sml1 in Response to Iron Deficiency

2014

Iron is an essential micronutrient for all eukaryotic organisms because it participates as a redox-active cofactor in many biological processes, including DNA replication and repair. Eukaryotic ribonucleotide reductases (RNRs) are Fe-dependent enzymes that catalyze deoxyribonucleoside diphosphate (dNDP) synthesis. We show here that the levels of the Sml1 protein, a yeast RNR large-subunit inhibitor, specifically decrease in response to both nutritional and genetic Fe deficiencies in a Dun1-dependent but Mec1/Rad53- and Aft1-independent manner. The decline of Sml1 protein levels upon Fe starvation depends on Dun1 forkhead-associated and kinase domains, the 26S proteasome, and the vacuolar pr…

Iron-Sulfur ProteinsProteasome Endopeptidase ComplexSaccharomyces cerevisiae ProteinsDeoxyribonucleoside triphosphateRibonucleotideIronDeoxyribonucleotidesGenes FungalSaccharomyces cerevisiaeCell Cycle ProteinsSaccharomyces cerevisiaeRibonucleotide reductase inhibitorProtein Serine-Threonine KinasesBiologyProtein degradationchemistry.chemical_compoundTristetraprolinRibonucleotide ReductasesAspartic Acid EndopeptidasesPhosphorylationMolecular BiologyCheckpoint Kinase 2Binding SitesKinaseIntracellular Signaling Peptides and ProteinsArticlesCell Biologybiology.organism_classificationDNA-Binding ProteinsDeoxyribonucleosideCheckpoint Kinase 2chemistryBiochemistryProteolysisGene DeletionTranscription FactorsMolecular and Cellular Biology
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cFLIPL Inhibits Tumor Necrosis Factor-related Apoptosis-inducing Ligand-mediated NF-κB Activation at the Death-inducing Signaling Complex in Human Ke…

2004

Human keratinocytes undergo apoptosis following treatment with tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) via surface-expressed TRAIL receptors 1 and 2. In addition, TRAIL triggers nonapoptotic signaling pathways including activation of the transcription factor NF-kappaB, in particular when TRAIL-induced apoptosis is blocked. The intracellular protein cFLIP(L) interferes with TRAIL-induced apoptosis at the death-inducing signaling complex (DISC) in many cell types. To study the role of cFLIP(L) in TRAIL signaling, we established stable HaCaT keratinocyte cell lines expressing varying levels of cFLIP(L). Functional analysis revealed that relative cFLIP(L) levels correlat…

KeratinocytesCytoplasmReceptor complexCell SurvivalCASP8 and FADD-Like Apoptosis Regulating ProteinApoptosisCell SeparationBiologyCaspase 8Sensitivity and SpecificityBiochemistryProinflammatory cytokineTNF-Related Apoptosis-Inducing LigandRibonucleasesCell Line TumorHumansEnzyme InhibitorsMolecular BiologyTranscription factorSkinInflammationCaspase 8Membrane GlycoproteinsTumor Necrosis Factor-alphaIntracellular Signaling Peptides and ProteinsNF-kappa BCell BiologyFlow CytometryRecombinant ProteinsCell biologyRetroviridaeApoptosisCaspasesDeath-inducing signaling complexRNATumor necrosis factor alphaSignal transductionApoptosis Regulatory ProteinsPropidiumProtein BindingSignal TransductionJournal of Biological Chemistry
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Exosomes released by keratinocytes modulate melanocyte pigmentation

2015

Cells secrete extracellular vesicles (EVs), exosomes and microvesicles, which transfer proteins, lipids and RNAs to regulate recipient cell functions. Skin pigmentation relies on a tight dialogue between keratinocytes and melanocytes in the epidermis. Here we report that exosomes secreted by keratinocytes enhance melanin synthesis by increasing both the expression and activity of melanosomal proteins. Furthermore, we show that the function of keratinocyte-derived exosomes is phototype-dependent and is modulated by ultraviolet B. In sum, this study uncovers an important physiological function for exosomes in human pigmentation and opens new avenues in our understanding of how pigmentation is…

KeratinocytesProteomicsUltraviolet RaysGeneral Physics and AstronomyBiologyMelanocyteProteomicsExosomesReal-Time Polymerase Chain ReactionGeneral Biochemistry Genetics and Molecular BiologyArticleTandem Mass SpectrometrymedicineHumansSecretionRNA MessengerCells CulturedMelanosomeRegulation of gene expressionMelaninsMultidisciplinaryMelanosomesEpidermis (botany)PigmentationGeneral ChemistryMicrovesiclesCell biologyMicroscopy Electronmedicine.anatomical_structureGene Expression RegulationMicroscopy FluorescenceMelanocytesEpidermisIntracellularChromatography LiquidNature Communications
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A model integrating the cerebellar granule neuron excitability and calcium signaling pathways

2004

Abstract The activation of various intracellular biochemical pathways is influenced by the electroresponsiveness of the neuron. There exists a close and constant co-operation between the membrane-bound cellular functions and intracellular signaling. This work aims at integrating the biophysical and biochemical data available for the cultured cerebellar granule neuron. The models of calcium-protein kinase C signaling pathways are combined with the model of the granule neuron excitability. The latter model can be used to provide the realistic stimulus for the signaling pathway models. The integrated model makes it possible to explore the participation of intracellular mechanisms in the neuron…

KinaseChemistryCognitive NeuroscienceCellular functionsStimulus (physiology)Computer Science Applicationsmedicine.anatomical_structureGranular cellnervous systemArtificial IntelligencemedicineNeuronSignal transductionNeuroscienceIntracellularCalcium signalingNeurocomputing
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Structure–activity relationships, and drug metabolism and pharmacokinetic properties for indazole piperazine and indazole piperidine inhibitors of RO…

2007

ROCK has been implicated in many diseases ranging from glaucoma to spinal cord injury and is therefore an important target for therapeutic intervention. In this study, we have designed a series of 1-(4-(1H-indazol-5-yl)piperazin-1-yl)-2-hydroxy(or 2-amino) analogs and a series of 1-(4-(1H-indazol-5-yl amino)piperidin-1-yl)-2-hydroxy(or 2-amino) inhibitors of ROCK-II. SR-1459 has IC50 = 13 nM versus ROCK-II while the IC50s for SR-715 and SR-899 are 80 nM and 100 nM, respectively. Many of these inhibitors, especially the 2-amino substituted analogs for both series, are modest/potent CYP3A4 inhibitors as well. However, a few of these inhibitors (SR-715 and SR-899) show strong selectivity for R…

KinaseIndazolesInhibitorStereochemistryClinical BiochemistryPharmaceutical ScienceProtein Serine-Threonine KinasesPharmacologyBiochemistryPiperazinesInhibitory Concentration 50Structure-Activity Relationshipchemistry.chemical_compoundDrug StabilityPiperidinesIn vivoDrug DiscoveryAnimalsCytochrome P-450 CYP3ACytochrome P-450 Enzyme InhibitorsHumansStructure–activity relationshipPharmacokineticsRho-kinaseProtein Kinase InhibitorsMolecular BiologyCytochrome P-450 Enzyme Inhibitorsrho-Associated KinasesIndazoleCYP3A4Organic ChemistryIntracellular Signaling Peptides and ProteinsROCK-IIRatsPiperazinePharmaceutical PreparationschemistryMolecular MedicinePiperidineDrug metabolismBioorganic & Medicinal Chemistry Letters : a tetrahedron publication for the rapid dissemination of preliminary communication and all aspects of bioorganic chemistry, medicinal chemistry and related disciplines
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Inhibition of lactate export by quercetin acidifies rat glial cells in vitro

1997

The relationship between glial lactate release and glial intracellular pH (pH i) regulation is studied using C6 glioma cells and rat astrocytes in vitro, and the lactate transport inhibitors quercetin and a-cyano-4-hydroxycinnamate (CHC). pHi is measured using 2′,7′bis(carboxyethyl)-5,6-carboxyfluorescein (BCECF). The results show that lactate release is mediated partly by a specific lactate transport system inhibitable by quercetin (50 mM), but not by CHC (5 mM). Inhibition by quercetin results in a significant 3‐4-fold increase of intracellular lactate and a decrease of intracellular pH to 6.9. A participation of quercetin-inhibitable lactate transport in glial pHi-regulation is suggested…

Lactate transportIntracellular pHBiologychemistry.chemical_compoundTumor Cells CulturedmedicineAnimalsheterocyclic compoundsLactic AcidFluorescent DyesGeneral NeuroscienceBiological TransportHydrogen-Ion ConcentrationFluoresceinsIn vitroRatsLactic acidmedicine.anatomical_structurechemistryBiochemistryCell cultureNeurogliaQuercetinQuercetinAcidsNeurogliaIntracellularNeuroscience Letters
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Immunohistochemical expression and distribution of orexin, orphanin and leptin in the major salivary glands of some mammals

2012

Abstract: The aim of the study was to assess the involvement of apoptotic factors, cytokeratins and metalloproteinase- 9 in the histogenesis of both Epithelialized Gingival Lesions (EGL) and Periapical Lesions (PAL). 55 consecutive patients, 30 with PAL and 25 with EGL, were selected for the study after clinical and radiological examinations. The PAL patients had severe periapical lesions and tooth decay with exposure of the pulp chamber. All PAL and EGL biopsies were surgically extracted, fixed in 10% buffered formalin, and processed for routine light microscopy. Ten biopsies of each category were processed for immunohistochemistry (IHC). Serial paraffin sections were stained by IHC with a…

LeptinKey words: cytokeratins MMP-9 caspase-3 caspase-9 perapical lesions epithelial gingival lesions apoptosis IHC PCNA TUNELSettore BIO/17 - Istologiamedicine.medical_specialtyHistologySubmandibular Glandcytokeratins MMP-9 caspase-3 caspase-9 perapical lesions epithelial gingival lesions apoptosis IHC PCNA TUNEL [Key words]major salivary glands orphanin FQ nociception orexin leptin IHC rat sheep cowBiologySalivary GlandsPathology and Forensic MedicineOrexin-ASublingual Glandstomatognathic systemInternal medicineMajor Salivary GlandOrexigenicmedicineEndocrine systemAnimalsParotid GlandMammalsOrexinsSheepSalivary glandNeuropeptidesConnective tissue stromaIntracellular Signaling Peptides and ProteinsGeneral MedicineImmunohistochemistryEpitheliumOrexinRatsmedicine.anatomical_structureEndocrinologyOpioid PeptidesCattlemedicine.drug
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