Search results for "Cellular membrane"

showing 10 items of 58 documents

Validation of brain extracellular glycerol as an indicator of cellular membrane damage due to free radical activity after traumatic brain injury.

2008

Following severe traumatic brain injury (TBI), increasing oxygen delivery to the brain has been advocated as a useful strategy to reverse mitochondrial dysfunction and improve neurological outcome. However, this might also promote overproduction of free radicals, responsible for lipid peroxidation and hence brain cell damage. Therefore, a method for monitoring this potential adverse effect in humans is desirable. Glycerol, an end product of phospholipid breakdown, easily detectable in the human brain by means of microdialysis, might represent a reliable indicator of free radical-induced cell membrane damage. Brain microdialysates were collected from 24 adult male Sprague-Dawley rats over a …

GlycerolMaleCellular membraneMicrodialysisFree RadicalsTraumatic brain injuryMicrodialysisPharmacologyAntioxidantsHead traumaCyclic N-OxidesRats Sprague-Dawleychemistry.chemical_compoundmedicineExtracellularGlycerolAnimalsbusiness.industryCell MembraneBrainExtracellular FluidMetabolismmedicine.diseaseRatsnervous systemchemistryAnesthesiaBrain InjuriesOxygen deliverySpin LabelsNeurology (clinical)businessJournal of neurotrauma
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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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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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Membrane-insertion fragments of Bcl-xL, Bax, and Bid.

2004

Apoptosis regulators of the Bcl-2 family associate with intracellular membranes from mitochondria and the endoplasmic reticulum, where they perform their function. The activity of these proteins is related to the release of apoptogenic factors, sequestered in the mitochondria, to the cytoplasm, probably through the formation of ion and/or protein transport channels. Most of these proteins contain a C-terminal putative transmembrane (TM) fragment and a pair of hydrophobic alpha helices (alpha5-alpha6) similar to the membrane insertion fragments of the ion-channel domain of diphtheria toxin and colicins. Here, we report on the membrane-insertion properties of different segments from antiapopt…

GlycosylationStereochemistryRecombinant Fusion ProteinsMolecular Sequence Databcl-X ProteinBcl-xLApoptosisBiochemistryProtein Structure SecondaryMembrane LipidsMiceProtein structureBcl-2-associated X proteinPredictive Value of TestsProto-Oncogene ProteinsProtein Interaction MappingAnimalsHumansAmino Acid SequencePeptide sequencebcl-2-Associated X ProteinbiologyIntracellular MembranesTransmembrane proteinPeptide FragmentsTransport proteinProtein TransportProto-Oncogene Proteins c-bcl-2Multigene FamilyHelixbiology.proteinBiophysicsCarrier ProteinsHydrophobic and Hydrophilic InteractionsAlpha helixBH3 Interacting Domain Death Agonist ProteinBiochemistry
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Digestive vacuole of Plasmodium falciparum released during erythrocyte rupture dually activates complement and coagulation.

2012

Abstract Severe Plasmodium falciparum malaria evolves through the interplay among capillary sequestration of parasitized erythrocytes, deregulated inflammatory responses, and hemostasis dysfunction. After rupture, each parasitized erythrocyte releases not only infective merozoites, but also the digestive vacuole (DV), a membrane-bounded organelle containing the malaria pigment hemozoin. In the present study, we report that the intact organelle, but not isolated hemozoin, dually activates the alternative complement and the intrinsic clotting pathway. Procoagulant activity is destroyed by phospholipase C treatment, indicating a critical role of phospholipid head groups exposed at the DV surfa…

HemeproteinsMalePain ThresholdErythrocytesImmunologyComplement Pathway AlternativePlasmodium falciparumVacuoleBiochemistryHemolysisMonocytesMicrobiologyHypesthesiaRats Sprague-DawleyPhagocytosisparasitic diseasesAnimalsHumansMalaria FalciparumBlood CoagulationLungbiologyPhospholipase CHemozoinDextran SulfatePlasmodium falciparumCell BiologyHematologyIntracellular Membranesbiology.organism_classificationComplement systemRatsAntibody opsonizationImmunologyVacuolesAlternative complement pathwaySpleenWaste disposalBlood
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Novel transmembrane topology of the hepatitis B virus envelope proteins.

1995

Abstract The small (S), middle (M) and large (L) envelope proteins of the hepatitis B virus (HBV) are initially synthesized as multispanning membrane proteins of the endoplasmic reticulum membrane. We now demonstrate that all envelope proteins synthesized in transfected cells or in a cell-free system adopt more than one transmembrane orientation. The L protein disposes its N-terminal preS domain both to the cytoplasmic and the luminal side of the membrane. This unusual topology does not depend on interaction with the viral nucleocapsid, but is preserved in secreted empty envelope particles. Pulse-chase analysis suggests a novel process of post-translational translocation leading to the non-…

Hepatitis B virusGlycosylationProtein ConformationBiologyEndoplasmic ReticulumTransfectionGeneral Biochemistry Genetics and Molecular Biologychemistry.chemical_compoundProtein structureViral Envelope ProteinsAnimalsMolecular BiologyGeneral Immunology and MicrobiologyGeneral NeuroscienceEndoplasmic reticulumViral nucleocapsidIntracellular MembranesMolecular biologyTransmembrane proteinCell biologychemistryMembrane proteinCytoplasmMembrane topologyProtein Processing Post-TranslationalResearch ArticleThe EMBO Journal
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At reduced temperature, endocytic membrane traffic is blocked in multivesicular carrier endosomes in rat cardiac myocytes.

1998

Temperatures around 20 degrees C are known to block degradation of endocytosed material by preventing its transport to lysosomes, accordingly reduced temperature has been widely used to define endosomes. Newer studies have revealed that the low temperature block is proximal to perinuclear late endosomes, but it is not clear whether the block is already in early endosomes, or whether the traffic proceeds to multivesicular carrier endosomes which mediate transport from early to late compartments. We have now focused on this problem using rat cardiac myocytes. First, cell fractionation on Percoll gradients showed that at reduced temperatures (22 degrees C and 26 degrees C), with prolonged chas…

HistologyEndosomeEndocytic cycleEndosomesBiologyEndocytosisPathology and Forensic MedicineAnimalsCells Culturedchemistry.chemical_classificationVesicleMyocardiumTemperatureCell BiologyGeneral MedicineIntracellular MembranesMembrane transportEmbryo MammalianEndocytosisRatsCold TemperaturechemistryBiochemistryMicroscopy FluorescenceTransferrinBiophysicsCell fractionationCarrier ProteinsPercollEuropean journal of cell biology
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Insertion of light-harvesting chlorophyll a/b protein into the thylakoid

2000

The major light-harvesting chlorophyll a/b-binding protein (Lhcb1,2) of photosystem II is inserted into the thylakoid via the signal recognition particle dependent pathway. However, the mechanism by which the protein enters the membrane is at this time unknown. In order to define some topographical restrictions for this process, we constructed several recombinant derivatives of Lhcb1 carrying hexahistidine tags at either protein terminus or in the stromal loop domain. Additionally, green fluorescent protein (GFP) was fused to either terminus. None of the modifications significantly impair the pigment-binding properties of the protein in the in vitro reconstitution of LHCII. With the excepti…

LightPhotosystem IIRecombinant Fusion ProteinsGreen Fluorescent ProteinsPhotosynthetic Reaction Center Complex ProteinsMutantLight-Harvesting Protein ComplexesBiologyThylakoidsBiochemistryInsert (molecular biology)Green fluorescent proteinLight-harvesting complexchemistry.chemical_compoundNickelHistidinePlant ProteinsSignal recognition particlePeasPhotosystem II Protein ComplexBiological TransportIntracellular MembranesPigments BiologicalMolecular WeightLuminescent ProteinschemistryBiochemistryChlorophyllThylakoidMutationBiophysicsCarrier ProteinsEuropean Journal of Biochemistry
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Early mitochondrial dysfunction, superoxide anion production, and DNA degradation are associated with non-apoptotic death of human airway epithelial …

2002

It has been shown that bacterial exoproducts may induce airway epithelium injury. During the epithelial repair process, the respiratory epithelial cells no more establish tight junctional intercellular complexes and may be particularly susceptible to bacterial virulence factors. In this study, we analyzed the effect of Pseudomonas aeruginosa exotoxin A (ETA) at different periods of time and concentrations on 16 HBE 14o(-) human bronchial epithelial cells in culture conditions inducing a phenotype of repairing cells. ETA treatment for 24 and 48 h led to the killing of 40.0 +/- 5.7% and 79.0 +/- 1.4% of the cells, respectively, as determined by the dimethylthiazole 2,5 diphenyl tetrazolium br…

MESH: Cell DeathMESH: ADP Ribose TransferasesMESH : DNAClinical BiochemistryCellApoptosisMESH : Dose-Response Relationship DrugMitochondrion[SDV.MHEP.PSR]Life Sciences [q-bio]/Human health and pathology/Pulmonology and respiratory tractMembrane PotentialsMESH: Dose-Response Relationship Drugchemistry.chemical_compoundSuperoxidesMESH: Intracellular MembraneMESH : DNA FragmentationRespiratory systemEnzyme InhibitorsCells CulturedADP Ribose TransferasesMESH : Cell SurvivalCell DeathSuperoxideMESH: DNAMESH: BronchiCaspase InhibitorsMESH : BronchiMitochondriaMESH : Epithelial Cellsmedicine.anatomical_structureMESH: Cell SurvivalMESH: Enzyme InhibitorsMESH: Epithelial CellsMESH : ADP Ribose TransferasesIntracellularMESH: Cells CulturedPulmonary and Respiratory MedicineProgrammed cell deathCell SurvivalVirulence FactorsBacterial ToxinsExotoxinsBronchiDNA FragmentationRespiratory MucosaBiologyMicrobiologyNecrosisNasal PolypsMESH : Cells CulturedmedicineHumansMESH: DNA FragmentationMESH : Intracellular MembraneMolecular BiologyMESH : Enzyme InhibitorsMESH: HumansMESH: CaspasesDose-Response Relationship DrugMESH: ApoptosisMESH : HumansEpithelial CellsCell BiologyDNAIntracellular MembranesMESH: ExotoxinschemistryMESH: Bacterial ToxinsApoptosisMESH : ExotoxinsMESH : Cell DeathMESH : Bacterial ToxinsRespiratory epithelium[SDV.MHEP.PSR] Life Sciences [q-bio]/Human health and pathology/Pulmonology and respiratory tractMESH : CaspasesMESH : Apoptosis[ SDV.MHEP.PSR ] Life Sciences [q-bio]/Human health and pathology/Pulmonology and respiratory tract
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