Search results for "Transmembrane"

showing 10 items of 299 documents

Extensive molecular analysis of patients bearing CFTR-related disorders.

2012

Cystic fibrosis transmembrane conductance regulator (CFTR)–related disorders (CFTR-RDs) may present with pancreatic sufficiency, normal sweat test results, and better outcome. The detection rate of mutations is lower in CFTR-RD than in classic CF: mutations may be located in genes encoding proteins that interact with CFTR or support channel activity. We tested the whole CFTR coding regions in 99 CFTR-RD patients, looking for gene mutations in solute carrier (SLC) 26A and in epithelial Na channel (ENaC) in 33 patients who had unidentified mutations. CFTR analysis revealed 28 mutations, some of which are rare. Of these mutations, RT-PCR demonstrated that the novel 1525-1delG impairs exon 10 s…

Epithelial sodium channelcongenital hereditary and neonatal diseases and abnormalitiesCystic fibrosis CFTR SLC26A SCNNCystic FibrosisAnion Transport ProteinsDNA Mutational Analysismolecular analysiCystic Fibrosis Transmembrane Conductance RegulatorGene mutationPathology and Forensic Medicinecongenital bilateral absence of vasa deferentesExonGene Frequencydisseminated bronchiectasiscongenital bilateral absence of vasa deferenteHumansTrypsinmolecular analysisEpithelial Sodium ChannelsGeneCells CulturedGenetic Association StudiesGeneticsbiologydisseminated bronchiectasiEpithelial Cellsrespiratory systemrecurrent pancreatitidigestive system diseasesCystic fibrosis transmembrane conductance regulatorrespiratory tract diseasesSolute carrier familyCFTR related disordersTrypsin Inhibitor Kazal PancreaticCase-Control StudiesRNA splicingMutationbiology.proteinMolecular MedicineCFTR related disorderSLC26 familyCarrier ProteinsNa channel ENaCMinigenerecurrent pancreatitis
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Expression of Active Streptolysin O in Escherichia coli as a Maltose-Binding-Protein-Streptolysin-O Fusion Protein. The N-Terminal 70 Amino Acids are…

1996

Streptolysin 0 (SLO) is the prototype of a family of cytolysins that consists of proteins which bind to cholesterol and form very large transmembrane pores. Structure/function studies on the pore-forming cytolysin SLO have been complicated by the proteolytic inactivation of a substantial portion of recombinant SLO (rSLO) expressed in Escherichia coli. To overcome this problem, translational fusions between the E. coli maltose-binding protein (MBP) gene and SLO were constructed, using the vectors pMAL-p2 and pMAL-c2. MBP-SLO fusion proteins were degraded if secreted into the E. coli periplasm, but intact, soluble MBP-SLO fusion proteins were produced at high levels in the cytoplasm. Active S…

ErythrocytesMonosaccharide Transport Proteinsgenetic structuresProtein ConformationStreptococcus pyogenesRecombinant Fusion ProteinsMolecular Sequence Datamedicine.disease_causeHemolysisBiochemistryMaltose-Binding ProteinsStructure-Activity RelationshipMaltose-binding proteinProtein structureBacterial ProteinsEscherichia colimedicineHumansCloning MolecularEscherichia coliSequence DeletionPore-forming toxinBase SequencebiologyEscherichia coli ProteinsFluoresceinsFusion proteineye diseasesTransmembrane proteinBiochemistryLiposomesStreptolysinsbiology.proteinATP-Binding Cassette TransportersStreptolysinsense organsCytolysinCarrier ProteinsSequence AnalysisEuropean Journal of Biochemistry
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Transmembrane beta-barrel of staphylococcal alpha-toxin forms in sensitive but not in resistant cells.

1997

Staphylococcal α-toxin is a 293-residue, single-chain polypeptide that spontaneously assembles into a heptameric pore in target cell membranes. To identify the pore-forming domain, substitution mutants have been produced in which single cysteine residues were introduced throughout the toxin molecule. By attaching the environmentally sensitive dye acrylodan to the sulfhydryl groups, the environment of individual amino acid side chains could be probed. In liposomes, a single 23-amino acid sequence (residues 118–140) was found to move from a polar to a nonpolar environment, indicating that this sequence forms the walls of the pore. However, periodicity in side chain environmental polarity coul…

ErythrocytesNeutrophilsStaphylococcusT-LymphocytesBacterial ToxinsLipid BilayersBiologyHemolysin ProteinsCell membraneHemolysin ProteinsAdenosine TriphosphatePhagocytosismedicineAnimalsHumansCysteineLipid bilayerchemistry.chemical_classificationLiposomeMultidisciplinaryCell MembraneBiological SciencesFlow CytometryTransmembrane proteinRecombinant ProteinsAmino acidmedicine.anatomical_structureBeta barrelchemistryBiochemistryAmino Acid SubstitutionMutagenesis Site-DirectedPotassiumRabbitsCysteine
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Oligomeric Sensor Kinase DcuS in the Membrane of Escherichia coli and in Proteoliposomes: Chemical Cross-linking and FRET Spectroscopy

2010

The DcuSR (dicarboxylate uptake sensor and regulator) system of Escherichia coli is a typical two-component system consisting of a membranous sensor kinase (DcuS) and a cytoplasmic response regulator (DcuR) (11, 26, 48). DcuS responds to C4-dicarboxylates like fumarate, malate, or succinate (19). In the presence of the C4-dicarboxlates, the expression of the genes of anaerobic fumarate respiration (dcuB, fumB, and frdABCD) and of aerobic C4-dicarboxylate uptake (dctA) is activated. DcuS is a histidine protein kinase composed of two transmembrane helices with an intermittent sensory PAS domain in the periplasm (PASP) that was also termed the PDC domain (for PhoQ/DcuS/DctB/CitA domain or fold…

Escherichia coli ProteinsProteolipidsCell MembraneGreen Fluorescent ProteinsHistidine kinaseAutophosphorylationBiologyMicrobiologyLuminescent ProteinsResponse regulatorTransmembrane domainSpectrometry FluorescenceProtein kinase domainBiochemistryPAS domainEscherichia coliFluorescence Resonance Energy TransferKinase activityProtein kinase AProtein KinasesMolecular BiologySignal TransductionJournal of Bacteriology
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Dynamic force sensing of filamin revealed in single-molecule experiments

2012

Mechanical forces are important signals for cell response and development, but detailed molecular mechanisms of force sensing are largely unexplored. The cytoskeletal protein filamin is a key connecting element between the cytoskeleton and transmembrane complexes such as integrins or the von Willebrand receptor glycoprotein Ib. Here, we show using single-molecule mechanical measurements that the recently reported Ig domain pair 20–21 of human filamin A acts as an autoinhibited force-activatable mechanosensor. We developed a mechanical single-molecule competition assay that allows online observation of binding events of target peptides in solution to the strained domain pair. We find that fi…

Filaminsta221IntegrinPlasma protein bindingImmunoglobulin domainactin-binding proteinta3111LigandsFilaminoptical tweezerContractile ProteinsHumansCytoskeletonMultidisciplinarybiologyChemistryMicrofilament Proteinsta1182Microfilament ProteinBiological SciencesfilaminTransmembrane proteinCell biologyOptical tweezersbiology.proteinmechanosensingProtein Binding
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CD133 Expression Is Not Synonymous to Immunoreactivity for AC133 and Fluctuates throughout the Cell Cycle in Glioma Stem-Like Cells.

2015

A transmembrane protein CD133 has been implicated as a marker of stem-like glioma cells and predictor for therapeutic response in malignant brain tumours. CD133 expression is commonly evaluated by using antibodies specific for the AC133 epitope located in one of the extracellular domains of membrane-bound CD133. There is conflicting evidence regarding the significance of the AC133 epitope as a marker for identifying stem-like glioma cells and predicting the degree of malignancy in glioma cells. The reasons for discrepant results between different studies addressing the role of CD133/AC133 in gliomas are unclear. A possible source for controversies about CD133/AC133 is the widespread assumpt…

G2 PhaseCell divisionlcsh:MedicineEpitopeS PhaseFlow cytometryEpitopes03 medical and health sciences0302 clinical medicinefluids and secretionsAntigens CDCell Line TumorGliomamedicineHumansAC133 Antigenlcsh:ScienceneoplasmsGlycoproteins030304 developmental biologychemistry.chemical_classification0303 health sciencesMultidisciplinarybiologymedicine.diagnostic_testlcsh:RGliomaCell cyclemedicine.diseaseCaco-2 cells; Cell cycle and cell division; Cell membranes; Cell staining; DAPI staining; Flow cytometry; Glioma cells; Membrane proteinsTransmembrane proteinCell biologyGene Expression Regulation Neoplasticcarbohydrates (lipids)chemistry030220 oncology & carcinogenesisembryonic structuresNeoplastic Stem Cellsbiology.proteincardiovascular systemlcsh:QCaco-2 CellsAntibodyPeptidesGlycoproteinCell DivisionResearch Article
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The transmembrane Bax inhibitor motif (TMBIM) containing protein family: Tissue expression, intracellular localization and effects on the ER CA2+-fil…

2015

Abstract Bax inhibitor-1 (BI-1) is an evolutionarily conserved pH-dependent Ca2+ leak channel in the endoplasmic reticulum and the founding member of a family of six highly hydrophobic mammalian proteins named transmembrane BAX inhibitor motif containing (TMBIM) 1-6 with BI-1 being TMBIM6. Here we compared the structure, subcellular localization, tissue expression and the effect on the cellular Ca2+ homeostasis of all family members side by side. We found that all TMBIM proteins possess the di-aspartyl pH sensor responsible for pH sensing identified in TMBIM6 and its bacterial homologue BsYetJ. TMBIM1-3 and TMBIM4-6 represent two phylogenetically distinct groups that are localized in the Go…

GHITMGAAPProtein familyEndoplasmic reticulumCell BiologyBiologyGolgi apparatusSubcellular localizationFAIM2Transmembrane proteinGHITMCell biologyTransmembrane domainsymbols.namesakeMICS1BiochemistryMembrane proteinGRINAsymbolsRECS1Molecular BiologyBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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Chloride, carboxylate and carbonate transport by ortho-phenylenediamine-based bisureas

2013

Highly potent but structurally simple transmembrane anion transporters are reported that function at receptor to lipid ratios as low as 1 : 1 000 000. The compounds, based on the simple ortho-phenylenediamine-based bisurea scaffold, have been studied for their ability to facilitate chloride/nitrate and chloride/bicarbonate antiport, and HCl symport processes using a combination of ion selective electrode and fluorescence techniques. In addition, the transmembrane transport of dicarboxylate anions (maleate and fumarate) by the compounds was examined. Molecular dynamics simulations showed that these compounds permeate the membrane more easily than other promising receptors corroborating the e…

GLUTAMATE TRANSPORTERSSTEROID-BASED RECEPTORSAntiporterBicarbonateMOLECULAR RECOGNITIONISOMERIC DICARBOXYLATE ANIONS010402 general chemistry01 natural sciencesChlorideIon selective electrodechemistry.chemical_compoundmedicineOrganic chemistryCarboxylate010405 organic chemistryGeneral ChemistryIN-VITROMembrane transportSELECTIVE DISCRIMINATIONTRANSMEMBRANE ANION TRANSPORTERSCombinatorial chemistryMEMBRANE TRANSPORTERS0104 chemical sciences3. Good healthMembranechemistryCONFORMATIONAL CONTROLINTRACELLULAR PHEffluxmedicine.drug
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Role of Human Sec63 in Modulating the Steady-State Levels of Multi-Spanning Membrane Proteins

2012

The Sec61 translocon of the endoplasmic reticulum (ER) membrane forms an aqueous pore, allowing polypeptides to be transferred across or integrated into membranes. Protein translocation into the ER can occur co- and posttranslationally. In yeast, posttranslational translocation involves the heptameric translocase complex including its Sec62p and Sec63p subunits. The mammalian ER membrane contains orthologs of yeast Sec62p and Sec63p, but their function is poorly understood. Here, we analyzed the effects of excess and deficit Sec63 on various ER cargoes using human cell culture systems. The overexpression of Sec63 reduces the steady-state levels of viral and cellular multi-spanning membrane …

Gastroenterology and hepatologylcsh:MedicineProtein SynthesisEndoplasmic ReticulumBiochemistryHepatitisViral Envelope ProteinsMolecular Cell BiologyTranslocaseRNA Small Interferinglcsh:ScienceIntegral membrane proteinEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsMultidisciplinarybiologyMembrane transport proteinReverse Transcriptase Polymerase Chain ReactionRNA-Binding ProteinsHepatitis BCellular StructuresCell biologyInfectious hepatitisCytochemistryMedicineInfectious diseasesResearch ArticleBlotting WesternViral diseasesReal-Time Polymerase Chain ReactionTransfectionCell LineSEC63Bacterial ProteinsHumansBiologyLiver diseasesDNA PrimersEndoplasmic reticulumlcsh:RCell MembraneMembrane ProteinsMembrane Transport ProteinsProteinsSEC61 TransloconChaperone ProteinsTransmembrane ProteinsLuminescent ProteinsMembrane proteinGene Expression RegulationMicroscopy FluorescenceSubcellular OrganellesChaperone (protein)Mutationbiology.proteinlcsh:QMolecular ChaperonesPLoS ONE
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The tetrameric α-helical membrane protein GlpF unfolds via a dimeric folding intermediate.

2011

Many membrane proteins appear to be present and functional in higher-order oligomeric states. While few studies have analyzed the thermodynamic stability of α-helical transmembrane (TM) proteins under equilibrium conditions in the past, oligomerization of larger polytopic monomers has essentially not yet been studied. However, it is vital to study the folding of oligomeric membrane proteins to improve our understanding of the general mechanisms and pathways of TM protein folding. To investigate the folding and stability of the aquaglyceroporin GlpF from Escherichia coli, unfolding of the protein in mixed micelles was monitored by steady-state fluorescence and circular dichroism spectroscopy…

Gel electrophoresisCircular dichroismProtein FoldingChemistryCircular DichroismEscherichia coli ProteinsMembrane ProteinsAquaporinsBiochemistryMicelleTransmembrane proteinProtein Structure SecondaryFolding (chemistry)CrystallographyKineticsMembrane proteinBiophysicsEscherichia coliProtein foldingChemical stabilityDimerizationProtein UnfoldingBiochemistry
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