Search results for "Intracellular"

showing 10 items of 821 documents

Centrins in retinal photoreceptor cells: regulators in the connecting cilium.

2008

Changes in the intracellular Ca2+ concentration regulate the visual signal transduction cascade directly or more often indirectly through Ca2+-binding proteins. Here we focus on centrins, which are members of a highly conserved subgroup of the EF-hand superfamily of Ca2+-binding proteins in photoreceptor cells of the vertebrate retina. Centrins are commonly associated with centrosome-related structures. In mammalian retinal photoreceptor cells, four centrin isoforms are expressed as prominent components in the connecting cilium linking the light-sensitive outer segment compartment with the metabolically active inner segment compartment. Our data indicate that Ca2+-activated centrin isoforms…

Gene isoformgenetic structuresChromosomal Proteins Non-HistoneBiologyContractile ProteinsHeterotrimeric G proteinmedicineCompartment (development)AnimalsHumansCiliaEye ProteinsVision OcularRetinaCalcium-Binding ProteinsSensory SystemsCell biologyOphthalmologymedicine.anatomical_structureCentrinCalciumsense organsTransducinSignal transductionIntracellularPhotoreceptor Cells VertebrateProgress in retinal and eye research
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GroEL and the maintenance of bacterial endosymbiosis

2004

Many eukaryotic organisms have symbiotic associations with obligate intracellular bacteria. The clonal transmission of endosymbionts between host generations should lead to the irreversible fixation of slightly deleterious mutations in their non-recombinant genome by genetic drift. However, the stability of endosymbiosis indicates that some mechanism is involved in the amelioration of the effects of these mutations. We propose that the chaperone GroEL was involved in the acquisition of an endosymbiotic lifestyle not only by means of its over-production, as proposed by Moran, but also by its adaptive evolution mediated by positive selection to improve the interaction with the unstable endosy…

GeneticsEndosymbiosisIntracellular parasiteChaperonin 60BiologyBacterial Physiological PhenomenaGenomeGroELSymbiosisGenetic driftChaperone (protein)ProteomeGeneticsbiology.proteinSymbiosisBiologyTrends in Genetics
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GroEL buffers against deleterious mutations

2002

GroEL, a heat-shock protein that acts as a molecular chaperone1, is overproduced in endosymbiotic but not in free-living bacteria2,3,4, presumably to assist in the folding of conformationally damaged proteins. Here we show that the overproduction of GroEL in Escherichia coli masks the effects of harmful mutations that have accumulated during a simulated process of vertical transmission. This molecular mechanism, which may be an adaptation to the bacterium's intracellular lifestyle, is able to rescue lineages from a progressive fitness decline resulting from the fixation of deleterious mutations under strong genetic drift5,6.

GeneticsMutationMultidisciplinarybiologybiology.organism_classificationmedicine.disease_causeEnterobacteriaceaeGroELHeat shock proteinmedicineOverproductionEscherichia coliBacteriaIntracellularNature
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Establishment of a quantitative RT-pCR for detection of vascular cell adhesion molecule-1 transcripts in endothelial cells after stimulation with adv…

1998

Advanced glycation endproducts (AGE) are supposed to increase endothelial expression of adhesion molecules like vascular cell adhesion molecule-1 (VCAM-1) by inducing an intracellular stress with subsequent activation of nuclear transcription factor NF-kappa-B. Quantitative analysis of VCAM-1-transcription has not been demonstrated concerning this topic. Thus, the aim of this study was to establish quantitative reverse transcription polymerase chain reaction (RT-PCR) assays using a spacer gene in order to measure the amounts of specific mRNA for VCAM-1 in human umbilical vein endothelial cells (HUVEC) which were stimulated with AGE-albumin (AGE-BSA). A recombinant RNA-standard was synthesiz…

Glycation End Products AdvancedCell adhesion moleculeReverse Transcriptase Polymerase Chain ReactionCellEndothelial CellsReproducibility of ResultsVascular Cell Adhesion Molecule-1Serum Albumin BovineGeneral MedicineCell cycleBiologyUmbilical veinCell biologyReverse transcription polymerase chain reactionReal-time polymerase chain reactionmedicine.anatomical_structureGeneticsmedicineHumansEndothelium VascularRNA MessengerCell adhesionIntracellularCells CulturedInternational journal of molecular medicine
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Specific stress-induced storage of trehalose, glycerol and D-arabitol in response to oxidative and osmotic stress in Candida albicans.

2012

Candida albicans exponential yeast cells are able to face environmental challenges by mounting a rapid and efficient "general stress response". Here we show that one of the main components of this response consists of the intracellular protective accumulation of the non-reducing disaccharide trehalose and two polyols, glycerol and D-arabitol, an accumulation that occurs in a stress-specific dependent manner. Thus, oxidative exposures promoted a marked increase in both trehalose and D-arabitol in the wild type strain, RM-100, whereas the glycerol content remained virtually unaffected with respect to basal levels. In contrast, osmotic challenges induced the significant storage of glycerol acc…

GlycerolOsmotic shockBiophysicsOxidative phosphorylationBiologyBiochemistrychemistry.chemical_compoundSugar AlcoholsOsmotic PressureCandida albicansGlycerolCandida albicansMolecular BiologyTrehaloseCell Biologybiology.organism_classificationTrehaloseYeastOxidative StresschemistryBiochemistryMitogen-activated protein kinasebiology.proteinMitogen-Activated Protein KinasesOxidation-ReductionIntracellularBiochemical and biophysical research communications
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The yeast osmosensitive mutant fps1Δ transformed by the cauliflower BobTIP1;1 aquaporin withstand a hypo-osmotic shock

2005

AbstractOsmoregulation plays an important role in cellular responses to osmotic stress in plants and in yeast. Aquaporins contribute to osmotic adjustment by facilitating transport of water or solutes across membranes. The tonoplastic water channel BobTIP1;1 (original name BobTIP26-1) genes are upregulated during dessication stress in cauliflower meristematic tissue. To investigate the physiological importance of BobTIP1;1, we expressed it in a Saccharomyces cerevisiae osmosensitive mutant fps1Δ. We showed that the defect in the yeast glycerol plasma membrane transporter is complemented by a plant cDNA encoding the aquaporin BobTIP1;1 which is localized in the vacuolar membrane of the compl…

GlycerolOsmotic stressOsmosisDNA ComplementarySaccharomyces cerevisiae ProteinsTime FactorsOsmotic shockSaccharomyces cerevisiaeMutantBlotting WesternGenes FungalBiophysicsAquaporinBrassicaSaccharomyces cerevisiaeOsmosisAquaporinsGenes PlantBiochemistryPolymerase Chain ReactionStructural BiologyGeneticsCloning MolecularFluorescent Antibody Technique Indirectγ-TIPMolecular BiologyPlant ProteinsbiologyAquaporinCell MembraneGenetic Complementation TestMembrane ProteinsWaterVacuolar membraneCell BiologyIntracellular Membranesbiology.organism_classificationYeastHypo-osmotic shockKineticsMembranePhenotypeBiochemistryGene Expression RegulationMutationVacuolesOsmoregulationElectrophoresis Polyacrylamide GelFEBS Letters
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Msb2 is a Ste11 membrane concentrator required for full activation of the HOG pathway.

2015

The high osmolarity glycerol (HOG) pathway, composed of membrane-associated osmosensors, adaptor proteins and core signaling kinases, is essential for the survival of yeast cells under hyper-osmotic stress. Here, we studied how the MAPKKK Ste11 might change its protein interaction profile during acute stress exposure, with an emphasis on the sensory system of the so-called Sho1/Msb2 signaling branch. To characterize the transience of protein-protein interactions we utilized a recently described enzymatic in vivo protein proximity assay (M-track). Accordingly, interaction signals between Ste11 and many of its signaling partners can already be detected even under basal conditions. In most cas…

GlycerolSaccharomyces cerevisiae ProteinsOsmotic shockBiophysicsSaccharomyces cerevisiaeBiologyBiochemistryStructural BiologyOsmotic PressureNegative feedbackGeneticsProtein Interaction MapsMolecular Biologychemistry.chemical_classificationFeedback PhysiologicalMAP kinase kinase kinaseKinaseOsmolar ConcentrationIntracellular Signaling Peptides and ProteinsSignal transducing adaptor proteinMembrane ProteinsMAP Kinase Kinase KinasesYeastCell biologyEnzymechemistryFunction (biology)Signal TransductionBiochimica et biophysica acta
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The role of glycerol transporters in yeast cells in various physiological and stress conditions.

2015

Small and uncharged glycerol is an important molecule for yeast metabolism and osmoadaptation. Using a series of S. cerevisiae BY4741-derived mutants lacking genes encoding a glycerol exporter (Fps1p) and/or importer (Stl1p) and/or the last kinase of the HOG pathway (Hog1p), we studied their phenotypes and various physiological characteristics with the aim of finding new roles for glycerol transporters. Though the triple mutant hog1Δ stl1Δ fps1Δ was viable, it was highly sensitive to various stresses. Our results showed that the function of both Stl1p and Fps1p transporters contributes to the cell ability to survive during the transfer into the state of anhydrobiosis, and that the deletion …

GlycerolSaccharomyces cerevisiae ProteinsOsmotic shockIntracellular pHMutantSaccharomyces cerevisiaeGlycerol transportSaccharomyces cerevisiaeBiologyMicrobiologyCell membranechemistry.chemical_compoundStress PhysiologicalGeneticsmedicineGlycerolMolecular BiologyCell MembraneMembrane ProteinsMembrane Transport ProteinsBiological Transportbiology.organism_classificationYeastCell biologymedicine.anatomical_structurePhenotypeBiochemistrychemistryMutationFEMS microbiology letters
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The catalytic activity of the endoplasmic reticulum-resident protein microsomal epoxide hydrolase towards carcinogens is retained on inversion of its…

1996

Diol epoxides formed by the sequential action of cytochrome P-450 and the microsomal epoxide hydrolase (mEH) in the endoplasmic reticulum (ER) represent an important class of ultimate carcinogenic metabolites of polycyclic aromatic hydrocarbons. The role of the membrane orientation of cytochrome P-450 and mEH relative to each other in this catalytic cascade is not known. Cytochrome P-450 is known to have a type I topology. According to the algorithm of Hartman, Rapoport and Lodish [(1989) Proc. Natl. Acad. Sci. U.S.A. 86, 5786–5790], which allows the prediction of the membrane topology of proteins, mEH should adopt a type II membrane topology. Experimentally, mEH membrane topology has been …

GlycosylationGlycosylation1303 BiochemistryCytochromeStereochemistryMolecular Sequence Data10050 Institute of Pharmacology and Toxicology610 Medicine & healthEndoplasmic ReticulumBiochemistryCatalysis1307 Cell Biologychemistry.chemical_compoundEndoglycosidase H1312 Molecular BiologyAnimalsAmino Acid SequenceBenzopyrenesMolecular BiologyEpoxide HydrolasesbiologyEndoplasmic reticulumCell BiologyIntracellular MembranesRecombinant ProteinsRatsCytosolMembranechemistryMicrosomal epoxide hydrolaseMembrane topologyCOS Cellsbiology.proteinCarcinogensMutagenesis Site-Directed570 Life sciences; biologyResearch Article
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Different conformations of nascent polypeptides during translocation across the ER membrane

2000

Abstract Background In eukaryotic cells, proteins are translocated across the ER membrane through a continuous ribosome-translocon channel. It is unclear to what extent proteins can fold already within the ribosome-translocon channel, and previous studies suggest that only a limited degree of folding (such as the formation of isolated α-helices) may be possible within the ribosome. Results We have previously shown that the conformation of nascent polypeptide chains in transit through the ribosome-translocon complex can be probed by measuring the number of residues required to span the distance between the ribosomal P-site and the lumenally disposed active site of the oligosaccharyl transfer…

GlycosylationProlineProtein ConformationAmino Acid MotifsMolecular Sequence DataEndoplasmic ReticulumPeptide MappingDogsLeucineMicrosomesAnimalsAmino Acid Sequencelcsh:QH573-671Alaninelcsh:CytologyCèl·lules eucariotesMembrane Transport ProteinsValineIntracellular MembranesProtein TransportAminoàcidsPèptidsRibosomesSignal Recognition ParticleResearch Article
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