Search results for "TRANSMEMBRANE PROTEIN"

showing 10 items of 186 documents

Oro-gustatory perception of dietary lipids and calcium signaling in taste bud cells are altered in nutritionally obesity-prone Psammomys obesus.

2013

Since the increasing prevalence of obesity is one of the major health problems of the modern era, understanding the mechanisms of oro-gustatory detection of dietary fat is critical for the prevention and treatment of obesity. We have conducted the present study on Psammomys obesus, the rodent desert gerbil which is a unique polygenic natural animal model of obesity. Our results show that obese animals exhibit a strong preference for lipid solutions in a two-bottle test. Interestingly, the expression of CD36, a lipido-receptor, in taste buds cells (TBC), isolated from circumvallate papillae, was decreased at mRNA level, but remained unaltered at protein level, in obese animals. We further st…

CD36 AntigensMaleTasteAnatomy and PhysiologyCD36BiochemistryCalcium in biologyFatschemistry.chemical_compoundMolecular Cell BiologySignaling in Cellular ProcessesMembrane Receptor Signalingchemistry.chemical_classificationMultidisciplinarybiologyQRTaste PerceptionTaste BudsLipidsSensory SystemsLipid SignalingCytochemistryThapsigarginMedicinePsammomysDisease SusceptibilityIntracellularResearch ArticleSignal Transductionmedicine.medical_specialtyThapsigarginClinical Research DesignLinoleic acidScienceLinoleic AcidFood PreferencesInternal medicinemedicineAnimalsCalcium SignalingObesityAnimal Models of DiseaseBiologyNutritionCell MembraneFatty acidProteinsbiology.organism_classificationLipid MetabolismDietary FatsGustatory SystemTransmembrane ProteinsEndocrinologyMetabolismchemistryGene Expression Regulationbiology.proteinGerbillinaeMembrane CompositionNeurosciencePLoS ONE
researchProduct

The Role of Cadherins in Ca2+-Mediated Cell Adhesion and Inherited Photoreceptor Degeneration

2002

Cadherins are Ca2+-binding, transmembrane proteins involved in cell adhesion. Recently, three cadherin molecules, cadherin-23, protocadherin-15, and cadherin-3, were found to be defective in various human diseases, many of them with photoreceptor degeneration and/or sensorineural hearing loss as major features such Usher syndrome type 1D (USH1D), USH1F, and hypotrichosis with juvenile macular dystrophy. The process, by which mutations lead to photoreceptor degeneration is still not fully understood. Data from the inner ear phenotype of USH1 mouse models suggest that loss of cell adhesion is a crucial event.

CadherinUsher syndromeMacular dystrophyBiologymedicine.diseasePhenotypeTransmembrane proteinCell biologyRetinitis pigmentosaotorhinolaryngologic diseasesmedicineHypotrichosissense organsCell adhesion
researchProduct

The role of hydrophobic matching on transmembrane helix packing in cells

2017

Folding and packing of membrane proteins are highly influenced by the lipidic component of the membrane. Here, we explore how the hydrophobic mismatch (the difference between the hydrophobic span of a transmembrane protein region and the hydrophobic thickness of the lipid membrane around the protein) influences transmembrane helix packing in a cellular environment. Using a ToxRED assay in Escherichia coli and a Bimolecular Fluorescent Complementation approach in human-derived cells complemented by atomistic molecular dynamics simulations we analyzed the dimerization of Glycophorin A derived transmembrane segments. We concluded that, biological membranes can accommodate transmembrane homo-di…

Cancer ResearchPhysiologyCèl·luleslcsh:Medicine010402 general chemistry114 Physical sciences01 natural sciencesBiochemistry Genetics and Molecular Biology (miscellaneous)03 medical and health sciencesHydrophobic mismatchhydrophobic matchhelix packingLipid bilayerlcsh:QH301-705.5030304 developmental biology0303 health sciencesChemistrylcsh:RGlycophorin AProteïnes de membranaGlycophorin ABiological membranetransmembrane domain dimerizationmembrane protein foldingTransmembrane protein0104 chemical sciencesFolding (chemistry)Transmembrane domainMembranelcsh:Biology (General)Membrane proteinBiophysicsMolecular MedicinemismatchResearch ArticleCell Stress
researchProduct

Membrane protein oxidation determines neuronal degeneration

2015

Oxidative stress is an early hallmark in neurodegenerative disorders such as Alzheimer's and Parkinson's diseases. However, the critical biochemical effector mechanisms of oxidative neurotoxicity have remained surprisingly elusive. In screening various peroxides and potential substrates of oxidation for their effect on neuronal survival, we observed that intramembrane compounds were significantly more active than aqueous or amphiphilic compounds. To better understand this result, we synthesized a series of competitive and site-specific membrane protein oxidation inhibitors termed aminoacyllipids, whose structures were designed on the basis of amino acids frequently found at the protein-lipi…

Cell SurvivalBiologyProtein oxidationmedicine.disease_causeBiochemistryProtein Structure SecondaryRats Sprague-DawleyCellular and Molecular Neurosciencechemistry.chemical_compoundmedicineAnimalsLipid bilayerCells CulturedNeuronsSphingosineNeurodegenerationNeurotoxicityMembrane Proteinsmedicine.diseaseTransmembrane proteinRatsCell biologyOxidative StressMembrane proteinchemistryNerve DegenerationReactive Oxygen SpeciesOxidation-ReductionOxidative stressJournal of Neurochemistry
researchProduct

α-Secretase Activity of the Disintegrin Metalloprotease ADAM 10: Influences of Domain Structure

2001

Disintegrin metalloproteases from different organisms form the ADAM (a disintegrin and metalloprotease) family. All members display a common domain organization and possess four potential functions: proteolysis, cell adhesion, cell fusion, and cell signaling. Members of the ADAM family are responsible for the proteolytic cleavage of transmembrane proteins and release of their extracellular domain. The proteolytic process is referred to as ectodomain shedding, which is activated by phorbol esters and inhibited by hydroxamic acid-based inhibitors. We have shown that the disintegrin metalloprotease ADAM 10 has both constitutive and regulated alpha-secretase activity. Expression of a dominant n…

Cell signalingDisintegrinsMolecular Sequence DataProtein domainBiologyGeneral Biochemistry Genetics and Molecular BiologyADAM10 ProteinAmyloid beta-Protein PrecursorHistory and Philosophy of ScienceEndopeptidasesDisintegrinAnimalsAspartic Acid EndopeptidasesHumansProtease InhibitorsAmino Acid SequenceCell adhesionMetalloproteinaseGeneral NeuroscienceHEK 293 cellsMembrane ProteinsMetalloendopeptidasesRecombinant ProteinsTransmembrane proteincarbohydrates (lipids)ADAM ProteinsBiochemistryEctodomainbiology.proteinAmyloid Precursor Protein SecretasesProtein Processing Post-TranslationalAnnals of the New York Academy of Sciences
researchProduct

Nanoscale Mapping of the Physical Surface Properties of Human Buccal Cells and Changes Induced by Saliva

2019

International audience; The mucosal pellicle, also called salivary pellicle, is a thin biological layer made of salivary and epithelial constituents, lining oral mucosae. It contributes to their protection against microbiological, chemical, or mechanical insults. Pellicle formation depends on the cells’ surface properties, and in turn the pellicle deeply modifies such properties. It has been reported that the expression of the transmembrane mucin MUC1 in oral epithelial cells improves the formation of the mucosal pellicle. Here, we describe an approach combining classical and functionalized tip atomic force microscopy and scanning microwave microscopy to characterize how MUC1 induces change…

Cell typeSalivaSurface Properties[SDV]Life Sciences [q-bio]Cellhuman buccal cells02 engineering and technology010402 general chemistry01 natural sciences[SPI]Engineering Sciences [physics]MicroscopyElectrochemistrymedicineElectric ImpedanceHumansNanotechnologyGeneral Materials ScienceSpectroscopyMUC1hydrophobicity[PHYS]Physics [physics]MouthsalivaChemistryMucinSurfaces and Interfaces021001 nanoscience & nanotechnologyCondensed Matter PhysicsTransmembrane protein0104 chemical sciencesScanning Microwave Microscopy SMMmedicine.anatomical_structureChemical force microscopydielectric propertiesBiophysicsChemical Force Microscopyfuntionalization0210 nano-technologyHydrophobic and Hydrophilic Interactions
researchProduct

Increased stability of the TM helix oligomer abrogates the apoptotic activity of the human Fas receptor

2021

Human death receptors control apoptotic events during cell differentiation, cell homeostasis and the elimination of damaged or infected cells. Receptor activation involves ligand-induced structural reorganizations of preformed receptor trimers. Here we show that the death receptor transmembrane domains only have a weak intrinsic tendency to homo-oligomerize within a membrane, and thus these domains potentially do not significantly contribute to receptor trimerization. However, mutation of Pro183 in the human CD95/Fas receptor transmembrane helix results in a dramatically increased interaction propensity, as shown by genetic assays. The increased interaction of the transmembrane domain is co…

Cellular differentiationBiophysicsApoptosisLigandsmedicine.disease_causeBiochemistryProtein DomainsmedicineHomeostasisHumansfas ReceptorReceptorMutationChemistryCell DifferentiationReceptors Death DomainCell BiologyFas receptorTransmembrane proteinCell biologyTransmembrane domainApoptosisMutationProtein MultimerizationSignal transductionSignal TransductionBiochimica et Biophysica Acta (BBA) - Biomembranes
researchProduct

Gray Matter NG2 Cells Display Multiple Ca2+-Signaling Pathways and Highly Motile Processes

2011

NG2 cells, the fourth type of glia in the mammalian CNS, receive synaptic input from neurons. The function of this innervation is unknown yet. Postsynaptic changes in intracellular Ca(2+)-concentration ([Ca(2+)](i)) might be a possible consequence. We employed transgenic mice with fluorescently labeled NG2 cells to address this issue. To identify Ca(2+)-signaling pathways we combined patch-clamp recordings, Ca(2+)-imaging, mRNA-transcript analysis and focal pressure-application of various substances to identified NG2-cells in acute hippocampal slices. We show that activation of voltage-gated Ca(2+)-channels, Ca(2+)-permeable AMPA-receptors, and group I metabotropic glutamate-receptors provo…

Central Nervous SystemAnatomy and PhysiologyVesicular glutamate transporter 1Glycobiologylcsh:MedicineHippocampal formationBiochemistryIon ChannelsTransmembrane Transport ProteinsMice0302 clinical medicinePostsynaptic potentialBiomacromolecule-Ligand Interactionslcsh:ScienceCells CulturedMembrane potential0303 health sciencesMultidisciplinarybiologyReverse Transcriptase Polymerase Chain ReactionDepolarizationNeurochemistryNeurotransmittersCell biologyElectrophysiologymedicine.anatomical_structureNeurologyNeurogliaMedicineProteoglycansNeurochemicalsGlutamateNeurogliaResearch ArticleNervous System PhysiologySignal TransductionCell PhysiologyMotilityNeuroimagingMice TransgenicNeurological System03 medical and health sciencesNeuropharmacologymedicineAnimalsHumansddc:610Biology030304 developmental biologyEndoplasmic reticulumlcsh:RProteinsGamma-Aminobutyric AcidTransmembrane ProteinsLuminescent ProteinsMicroscopy Electronnervous systemMicroscopy FluorescenceSynapsesVesicular Glutamate Transport Protein 1biology.proteinNervous System Componentslcsh:QCalciumPhysiological Processes030217 neurology & neurosurgeryNeurosciencePLoS ONE
researchProduct

The Process-inducing Activity of Transmembrane Agrin Requires Follistatin-like Domains

2009

Clustering or overexpression of the transmembrane form of the extracellular matrix proteoglycan agrin in neurons results in the formation of numerous highly motile filopodia-like processes extending from axons and dendrites. Here we show that similar processes can be induced by overexpression of transmembrane-agrin in several non-neuronal cell lines. Mapping of the process-inducing activity in neurons and non-neuronal cells demonstrates that the cytoplasmic part of transmembrane agrin is dispensable and that the extracellular region is necessary for process formation. Site-directed mutagenesis reveals an essential role for the loop between beta-sheets 3 and 4 within the Kazal subdomain of t…

Central Nervous SystemFollistatinanimal structuresBiologyCytoplasmic partPC12 CellsBiochemistryProtein Structure SecondaryNeuromuscular junctionCell membraneExtracellular matrixMolecular Basis of Cell and Developmental BiologyProtein structureChlorocebus aethiopsmedicineAnimalsHumansAgrinMolecular BiologyNeuronsAgrinCell MembraneCell BiologyTransmembrane proteinProtein Structure TertiaryRatsCell biologymedicine.anatomical_structurenervous systemProteoglycanBiochemistryCOS CellsMutagenesis Site-Directedbiology.proteinFemaleChickenshormones hormone substitutes and hormone antagonistsJournal of Biological Chemistry
researchProduct

Regulation of Plant Transporters by Lipids and Microdomains

2010

Transporters in the broad sense, that is, carriers, pumps, and channels, are proteins inserted in a lipid bilayer separating two cellular compartments. This lipid bilayer is not only the physical support of such proteins, but also a powerful way to regulate their activity. This chapter will first summarize the different means by which lipids can regulate the activity of transmembrane proteins (including the physical properties of the bilayer, its dynamic lateral compartmentalization, and the presence of particular lipid species acting as cofactors). It will then illustrate these general rules with examples of such regulations found in plant literature and, as a reference, in animal studies.

ChemistryBilayerBiophysicsMembrane raftTransporterCompartmentalization (psychology)Lipid bilayerLipid raftTransmembrane proteinCellular compartment
researchProduct