Search results for "Carrier Proteins"

showing 10 items of 347 documents

Purification and structural characterisation of lipid transfer protein from red wine and grapes

2012

Lipid transfer proteins (LTP) play a major role in plant defence and are of particular interest due to their known ability to cause allergic reactions. These proteins are expressed in grapes and also remain detectable after vinification, especially in red wine. However, it remains unknown whether the protein undergoes any changes during the vinification process. Here, we present a purification method for LTPs from Dornfelder grapes and wine. By liquid-chromatography-mass spectroscopy (LC-MS/MS) we identified LTPs from two different species (Vitis vinifera and Vitis aestivalis). Additionally, the purified LTPs were characterised using spectrometric methods, confirming their high purity and s…

Vitis aestivalisProtein ConformationChemistryfungifood and beveragesWineFast protein liquid chromatographyGeneral MedicineTandem mass spectrometryAnalytical ChemistryProtein structureBiochemistryTandem Mass SpectrometrywineVitiswine.grape_varietyPurification methodsCarrier ProteinsPlant lipid transfer proteinsPolyacrylamide gel electrophoresisPlant ProteinsFood ScienceFood Chemistry
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Wee1 inhibition potentiates Wip1-dependent p53-negative tumor cell death during chemotherapy

2016

AbstractInactivation of p53 found in more than half of human cancers is often associated with increased tumor resistance to anti-cancer therapy. We have previously shown that overexpression of the phosphatase Wip1 in p53-negative tumors sensitizes them to chemotherapeutic agents, while protecting normal tissues from the side effects of anti-cancer treatment. In this study, we decided to search for kinases that prevent Wip1-mediated sensitization of cancer cells, thereby interfering with efficacy of genotoxic anti-cancer drugs. To this end, we performed a flow cytometry-based screening in order to identify kinases that regulated the levels of γH2AX, which were used as readout. Another criter…

Wip1ApoptosisCell Cycle ProteinsPharmacologyMESH: G2 Phase Cell Cycle CheckpointsHistonesMESH : PhosphorylationMiceMESH : Cell Cycle ProteinsMESH: AnimalsMESH: Tumor Suppressor Protein p53MESH: HistonesKinaseTp53 mutationsMESH : Mice Transgenic3. Good healthProtein Phosphatase 2CSurvival RateMESH : Antineoplastic AgentsH2ax phosphorylationP53 activationMESH: Protein Phosphatase 2CRNA InterferenceMESH : Colorectal NeoplasmsMESH : Carrier ProteinsHistone H2axMESH: MitochondriaImmunologyHuman fibroblastsMESH: Carrier ProteinsAntineoplastic AgentsMESH: Protein-Tyrosine KinasesMESH: Protein-Serine-Threonine KinasesMESH : Cisplatin03 medical and health sciencesMESH: Cell Cycle ProteinsGenotoxic stressMESH : Protein-Tyrosine KinasesHumansMESH : HistonesAnticancer TherapyMESH: DNA DamageCisplatinMESH: HumansMESH: Phosphorylation[ SDV.BC ] Life Sciences [q-bio]/Cellular BiologyMESH : HumansMESH : Nuclear Proteins030104 developmental biologyCancer cellMESH: Antineoplastic AgentsCisplatinCarrier ProteinsMESH: Nuclear ProteinsMESH : ApoptosisDna-damage response0301 basic medicineCancer ResearchMESH: Caspase 3MESH : Caspase 3PhosphorylationCytotoxicityMESH : DNA DamageSensitizationmedicine.diagnostic_testCaspase 3Nuclear ProteinsProtein-Tyrosine KinasesMESH : Survival RateMitochondriaG2 Phase Cell Cycle CheckpointsWee1medicine.anatomical_structureMESH : Protein Phosphatase 2COriginal ArticleMESH : MitochondriaColorectal Neoplasmsmedicine.drugMESH : Protein-Serine-Threonine KinasesMESH: Cell Line TumorMESH: Survival RateMESH: Mice TransgenicMESH: RNA InterferencePhosphataseMice Transgenic[SDV.BC]Life Sciences [q-bio]/Cellular BiologyBiologyProtein Serine-Threonine KinasesFlow cytometryCellular and Molecular NeuroscienceCell Line TumorMESH : MicemedicineAnimalsMESH: MiceMESH : Cell Line TumorMESH: ApoptosisCell BiologyMESH : Tumor Suppressor Protein p53MESH: CisplatinCancer researchbiology.proteinMESH : AnimalsMESH : G2 Phase Cell Cycle CheckpointsMESH : RNA InterferenceTumor Suppressor Protein p53MESH: Colorectal NeoplasmsDNA DamageCell Death & Disease
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Interactions in the network of Usher syndrome type 1 proteins

2004

International audience; Defects in myosin VIIa, harmonin (a PDZ domain protein), cadherin 23, protocadherin 15 and sans (a putative scaffolding protein), underlie five forms of Usher syndrome type I (USH1). Mouse mutants for all these proteins exhibit disorganization of their hair bundle, which is the mechanotransduction receptive structure of the inner ear sensory cells, the cochlear and vestibular hair cells. We have previously demonstrated that harmonin interacts with cadherin 23 and myosin VIIa. Here we address the extent of interactions between the five known USH1 proteins. We establish the previously suggested sans-harmonin interaction and find that sans also binds to myosin VIIa. We …

[SDV]Life Sciences [q-bio]Hearing Loss SensorineuralStereocilia (inner ear)PDZ domainCadherin Related ProteinsProtocadherinCell Cycle ProteinsNerve Tissue ProteinsCuticular plateMyosinsBiologyMiceTwo-Hybrid System TechniquesHair Cells AuditoryBone plateMyosinotorhinolaryngologic diseasesGeneticsAnimalsHumansProtein PrecursorsMolecular BiologyGenetics (clinical)GeneticsStereociliumDyneinsSyndromeGeneral MedicineCadherinsCell biologyCytoskeletal ProteinsMyosin VIIaMutationsense organsCarrier ProteinsRetinitis PigmentosaPCDH15HeLa CellsProtein BindingHuman Molecular Genetics
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A (1->3)-beta-D-glucan recognition protein from the sponge Suberites domuncula. Mediated activation of fibrinogen-like protein and epidermal growth f…

2004

Sponges (phylum Porifera) live in a symbiotic relationship with microorganisms, primarily bacteria. Until now, molecular proof for the capacity of sponges to recognize fungi in the surrounding aqueous milieu has not been available. Here we demonstrate, for the demosponge Suberites domuncula (Porifera, Demospongiae, Hadromerida), a cell surface receptor that recognizes (1--3)-beta-D-glucans, e.g. curdlan or laminarin. This receptor, the (1--3)-beta-D-glucan-binding protein, was identified and its cDNA analysed. The gene coding for the 45 kDa protein was found to be upregulated in tissue after incubation with carbohydrate. Simultaneously with the increased expression of this gene, two further…

beta-GlucansMolecular Sequence DataPinacodermGene Expression-BiochemistryDemospongeEpidermal growth factorComplementary DNALectinsAnimalsAmino Acid SequencePhosphorylationProtein PrecursorsGlucansHadromeridaPhylogenybiologyEpidermal Growth FactorFibrinogenbiology.organism_classificationRecombinant ProteinsPoriferaSuberites domunculaSpongeBiochemistryCarrier ProteinsTyrosine kinaseSequence Alignment
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REGULATION OF CATIONIC AMINO ACID TRANSPORT: The Story of the CAT-1 Transporter

2004

▪ Abstract  The discovery of the function of the receptor for the ecotropic retrovirus as a membrane transporter for the essential amino acids lysine and arginine was a landmark finding in the field of molecular nutrition. This finding indicated that cationic amino acid transporters (CATs) act pathologically as viral receptors. The importance of this transporter was further supported by knockout mice that were not viable after birth. CAT-1 was the first amino acid transporter to be cloned; several other CATs were later characterized biochemically and molecularly. These transporters mediate the bidirectional transport of cationic amino acids, thus supporting important metabolic functions, s…

chemistry.chemical_classificationNutrition and DieteticsArginine transportArginineLysineMedicine (miscellaneous)Biological TransportTransporterBiologyAmino acidGene Expression RegulationBiochemistrychemistryAmino Acid Transport Systems BasicAnimalsHumansRNA MessengerAmino acid transporterAmino AcidsCarrier ProteinsReceptorGeneAnnual Review of Nutrition
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Identification of a Functional Homolog of the Yeast Copper Homeostasis Gene ATX1 from Arabidopsis1

1998

Abstract A cDNA clone encoding a homolog of the yeast (Saccharomyces cerevisiae) gene Anti-oxidant 1(ATX1) has been identified from Arabidopsis. This gene, referred to as CopperCHaperone(CCH), encodes a protein that is 36% identical to the amino acid sequence of ATX1 and has a 48-amino acid extension at the C-terminal end, which is absent from ATX1 homologs identified in animals. ATX1-deficient yeast (atx1) displayed a loss of high-affinity iron uptake. Expression of CCH in the atx1 strain restored high-affinity iron uptake, demonstrating thatCCH is a functional homolog of ATX1. When overexpressed in yeast lacking the superoxide dismutase geneSOD1, both ATX1 and CCHprotected the cell from t…

endocrine systemDNA ComplementarySaccharomyces cerevisiae ProteinsPhysiologyMolecular Sequence DataSaccharomyces cerevisiaeSOD1ArabidopsisGene ExpressionSaccharomyces cerevisiaePlant ScienceFungal ProteinsGene productSuperoxide dismutaseOzoneCopper Transport ProteinsComplementary DNAArabidopsisGene expressionGeneticsHomeostasisAmino Acid SequenceCation Transport ProteinsBase SequenceSequence Homology Amino AcidbiologyArabidopsis ProteinsGenetic Complementation Testbiology.organism_classificationYeastOxidative StressBiochemistrybiology.proteinCarrier ProteinsCopperResearch ArticlePlant Physiology
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AMPA Receptor Auxiliary Proteins of the CKAMP Family

2019

α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors are assembled of four core subunits and several additional interacting proteins. Cystine-knot AMPA receptor-modulating proteins (CKAMPs) constitute a family of four proteins that influence the trafficking, subcellular localization and function of AMPA receptors. The four CKAMP family members CKAMP39/shisa8, CKAMP44/shisa9, CKAMP52/shisa6 and CKAMP59/shisa7 differ in their expression profile and their modulatory influence on AMPA receptor function. In this review, I report about recent findings on the differential roles of CKAMP family members.

glutamate receptorhippocampusGene ExpressionReviewAMPA receptorBiologySynaptic TransmissionCatalysisCell Linelcsh:ChemistryInorganic ChemistryLong term plasticitylateral geniculate nucleusAnimalsHumansAmino Acid SequenceReceptors AMPAAMPA receptorPhysical and Theoretical Chemistrysynaptic functionReceptorlcsh:QH301-705.5Molecular BiologySpectroscopyNeuronal Plasticitymusculoskeletal neural and ocular physiologyOrganic ChemistryGlutamate receptorGeniculate BodiesGeneral MedicineSubcellular localizationlong-term plasticityComputer Science ApplicationsCell biologyProtein TransportSynaptic functionlcsh:Biology (General)lcsh:QD1-999nervous systemauxiliary subunitMultigene FamilySynapsesCarrier ProteinsIon Channel Gatingshort-term plasticityFunction (biology)Protein BindingInternational Journal of Molecular Sciences
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Truncated recombinant light harvesting complex II proteins are substrates for a protein kinase associated with photosystem II core complexes

1998

AbstractPrevious studies directed towards understanding phosphorylation of the chlorophyll a/b binding proteins comprising light harvesting complex II (LHC II) have concentrated on a single phosphorylation site located close to the N-terminus of the mature proteins. Here we show that a series of recombinant pea Lhcb1 proteins, each missing an N-terminal segment including this site, are nevertheless phosphorylated by a protein kinase associated with a photosystem II core complex preparation. An Lhcb1 protein missing the first 58 amino acid residues is not, however, phosphorylated. The results demonstrate that the LHC II proteins are phosphorylated at one or more sites, the implications of wh…

inorganic chemicalsPhotosystem IIMacromolecular SubstancesMolecular Sequence DataPhotosynthetic Reaction Center Complex ProteinsLight-Harvesting Protein ComplexesBiophysicsmacromolecular substancesBiologyBiochemistryDNA-binding proteinProtein kinaseThylakoid membraneSubstrate Specificitylaw.inventionStructural BiologylawGeneticsProtein phosphorylationAmino Acid SequencePhosphorylationProtein kinase AMolecular BiologyPlant ProteinsKinasePeasPeaPhotosystem II Protein Complexfood and beveragesCell BiologySpinachPeptide FragmentsRecombinant Proteinsenzymes and coenzymes (carbohydrates)BiochemistryThylakoidRecombinant DNALight harvesting proteinPhosphorylationbacteriaCarrier ProteinsProtein KinasesFEBS Letters
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Identification and characterization of a monoclonal antibody to the membrane fatty acid binding protein

1992

A monoclonal antibody to the rat liver membrane fatty acid binding protein (MFABP) was prepared by immunizing mice with purified MFABP isolated from solubilized rat liver plasma membrane proteins by oleate-agarose affinity chromatography technique. The monoclonal antibody K15/6 identified a single 40 kDa protein in rat liver plasma membranes with pI values of 8.5, 8.8 and 9.0, which is identical to the authentic MFABP, but clearly distinct from rat mitochondrial GOT. The antibody K15/6 selectively inhibited cellular influx as well as membrane binding of fatty acids, but not of cholesterol or vitamin E. The same antibody was used in immunofluorescence, ELISA and Western blot analysis to dete…

medicine.drug_classBlotting WesternImmunoblottingBiophysicsFluorescent Antibody TechniqueEnzyme-Linked Immunosorbent AssayNerve Tissue ProteinsFatty Acid-Binding ProteinsMonoclonal antibodyBiochemistryFatty acid-binding proteinCell LineMiceEndocrinologyAffinity chromatographymedicineAnimalsHumanschemistry.chemical_classificationMice Inbred BALB CbiologyMembrane transport proteinTumor Suppressor ProteinsBinding proteinCell MembraneFatty AcidsAntibodies MonoclonalFatty acidMolecular biologyNeoplasm ProteinsRatsLiverchemistryMembrane proteinBiochemistrybiology.proteinElectrophoresis Polyacrylamide GelAntibodyCarrier ProteinsFatty Acid-Binding Protein 7Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism
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The role of the Thomsen-Friedenreich antigen as a tumor-associated molecule.

1990

The Thomsen-Friedenreich antigen (Gal-GalNAc) represents a tumor-associated molecule, which is assumed to be one of the few chemically well-defined antigens with a proven association with malignancy. In order to analyze the role of the carbohydrate structure Gal-GalNAc for gastrointestinal tumors, we immunized Balb/c mice with MCF-7 breast tumor cells together with synthetic Gal-GalNAc linked to a BSA carrier. One monoclonal antibody (82-A6) was established which recognizes the Thomsen-Friedenreich antigen according to the biochemical and serological analysis presented here. In contrast to the studies performed in the past, immunohistochemical results using this antibody 82-A6 did not exhib…

medicine.drug_classHealth Toxicology and MutagenesisDisaccharidesMonoclonal antibodyMalignancyAntibodiesEpitopeAntigenAntibody SpecificityAntigens NeoplasmTumor Cells CulturedmedicineHumansAntigens Tumor-Associated Carbohydratechemistry.chemical_classificationMolecular StructurebiologyThomsen-Friedenreich AntigenPublic Health Environmental and Occupational Healthmedicine.diseaseMolecular biologyMolecular Weightcarbohydrates (lipids)chemistrybiology.proteinImmunohistochemistryAntibodyCarrier ProteinsGlycoproteinResearch ArticleEnvironmental Health Perspectives
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