Search results for "peptide fragments"

showing 10 items of 353 documents

Effects of alpha-melanotropin C-terminal tripeptide analogues on macrophage NO production.

2003

The C-terminal tripeptide of melanocyte-stimulating hormone, MSH (11-13) (Lys-Pro-Val), possesses strong anti-inflammatory actions, which are mediated via mechanisms that are not fully understood. To shed more light into these mechanisms we have here synthesised and evaluated the activities of L- and D-Val substituted cyclic modifications of MSH (11-13) on nitric oxide (NO) in macrophage RAW 264.7 cells, as well as on binding to melanocortin receptors (MCRs) in B16-F1 and MCR expressing insect cells, and for effects on cAMP. MSH (11-13) and its analogues did neither bind to MCRs nor stimulate cAMP in RAW 264.7 and B16-F1 cells, except H-, which showed a tendency to increase cAMP at high (10…

PhysiologyAnti-Inflammatory AgentsTripeptideBiologyNitric OxideBiochemistryNitric oxideCellular and Molecular Neurosciencechemistry.chemical_compoundMiceEndocrinologyCell Line TumorCyclic AMPStructure–activity relationshipAnimalsMelanocyte-Stimulating HormonesBinding siteReceptorBinding SitesMacrophagesStereoisomerismPeptide FragmentschemistryBiochemistryCell cultureMelanocortinSignal transductionSignal TransductionPeptides
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CD8+CD45RA+CD27-CD28-T-cell subset in PBL of cervical cancer patients representing CD8+T-cells being able to recognize cervical cancer associated ant…

2003

Objective In response to antigenic stimulation, naive MHC-class I restricted and antigen-specific CD8+CD45RA+CD28+T-cells undergo clonal expansion and differentiate into CD8+CD45RO+ memory T-cells. Upon re- encounter with the nominal antigen, CD45RO+ T-cells are able to convert to CD8+CD45RA+CD28-T-cells displaying potent immune effector functions, including TNF-alpha production. This T-cell subpopulation constitutes a minor population in healthy individuals. In the present study we are currently evaluating whether this particular T-cell subset in PBL represents CD8+T-cells which may be able to recognize cervical cancer associated antigens provided by HPV 16 E7. Material and methods Flow-cy…

PopulationUterine Cervical Neoplasmschemical and pharmacologic phenomenaCD8-Positive T-LymphocytesBiologyEpitopeImmune systemCD28 AntigensAntigenAntigens CDT-Lymphocyte SubsetsmedicineHumansCytotoxic T cellAmino Acid SequenceeducationAntigens ViralPapillomaviridaeNeoplasm Stagingeducation.field_of_studyHistocompatibility TestingObstetrics and GynecologyCD28Cancerhemic and immune systemsmedicine.diseasePeptide FragmentsTumor Necrosis Factor Receptor Superfamily Member 7Lymphatic MetastasisImmunologyCytokinesLeukocyte Common AntigensFemaleCD8Zentralblatt für Gynäkologie
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Effect of flupirtine on Bcl-2 and glutathione level in neuronal cells treated in vitro with the prion protein fragment (PrP106-126).

1997

Flupirtine, trade name Katadolon, is a centrally acting nonopioid analgesic that has recently been found to display cytoprotective activity in vitro and in vivo on neurons induced to undergo apoptosis. This report shows that the PrP106-126 fragment of the prion protein, which is the likely etiological agent for a series of encephalopathies, is toxic to cortical neurons in vitro. Simultaneously, PrP106-126 influences the molecular GSH content and the bcl-2 expression in neurons. Significant toxicity (32% reduction in cell viability) was observed at a concentration of 50 microM of the peptide after 9 days of incubation, while at higher concentrations toxicity increased to 70%. Neurotoxicity w…

PrionsMolecular Sequence DataAminopyridinesApoptosisPharmacologyBiologychemistry.chemical_compoundDevelopmental NeurosciencemedicineAnimalsAmino Acid SequenceRats WistarCytotoxicityCells CulturedNeuronsNeurotoxicityGlutathioneAnalgesics Non-Narcoticmedicine.diseaseGlutathioneIn vitroPeptide FragmentsGenes bcl-2RatsOxidative StressNeuroprotective AgentsNeurologychemistryGene Expression RegulationProto-Oncogene Proteins c-bcl-2ApoptosisCell cultureImmunologyToxicityFlupirtineOxidation-Reductionmedicine.drugExperimental neurology
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Functional characterization of two melanocortin (MC) receptors in lamprey showing orthology to the MC1 and MC4 receptor subtypes

2007

Abstract Background The melanocortin (MC) receptors have a key role in regulating body weight and pigmentation. They belong to the rhodopsin family of G protein-coupled receptors (GPCRs). The purpose of this study was to identify ancestral MC receptors in agnathan, river lamprey. Results We report cloning of two MC receptors from river lamprey. The lamprey receptors, designated MCa and MCb, showed orthology to the MC1 and MC4 receptor subtypes, respectively. The molecular clock analysis suggested that lamprey MC receptor genes were not duplicated recently and diverged from each other more than 400 MYR ago. Expression and pharmacological characterization showed that the lamprey MCa receptor …

Pro-OpiomelanocortinSecond Messenger SystemsGene DuplicationProtein Interaction MappingCyclic AMPPetromyzonReceptorPhylogenyCell Line TransformedSkinGeneticsbiologyReceptors MelanocortinMelanocortin 3 receptorCell biologyOrgan SpecificityRhodopsinReceptor Melanocortin Type 4HagfishesMelanocortinReceptor Melanocortin Type 1Protein BindingResearch ArticleEvolutionRecombinant Fusion ProteinsMolecular Sequence DataBinding CompetitivePeptides CyclicEvolution Moleculargamma-MSHAdrenocorticotropic HormoneSpecies SpecificityMelanocortin receptorbeta-MSHQH359-425AnimalsHumansAmino Acid SequenceEcology Evolution Behavior and SystematicsGene LibraryG protein-coupled receptorBinding SitesSequence Homology Amino AcidFuguLampreybiology.organism_classificationPeptide FragmentsVisceraalpha-MSHbiology.proteinCosyntropinSequence Alignmenthuman activitiesBMC Evolutionary Biology
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Specific processing of tenascin-C by the metalloprotease meprinβ neutralizes its inhibition of cell spreading

2009

The metalloprotease meprin has been implicated in tissue remodelling due to its capability to degrade extracellular matrix components. Here, we investigated the susceptibility of tenascin-C to cleavage by meprinbeta and the functional properties of its proteolytic fragments. A set of monoclonal antibodies against chicken and human tenascin-C allowed the mapping of proteolytic fragments generated by meprinbeta. In chicken tenascin-C, meprinbeta processed all three major splicing variants by removal of 10kDa N-terminal and 38kDa C-terminal peptides, leaving a large central part of subunits intact. A similar cleavage pattern was found for large human tenascin-C variant where two N-terminal pep…

Proteasesanimal structuresColonRecombinant Fusion ProteinsProtein subunitMolecular Sequence DataTenascinCleavage (embryo)Cell LineCrohn DiseaseCell AdhesionAnimalsHumansProtein IsoformsAmino Acid SequenceProtein Structure QuaternaryMolecular BiologyPeptide sequencebiologyAlternative splicingTenascin CMetalloendopeptidasesTenascinMolecular biologyPeptide FragmentsExtracellular MatrixFibronectinsFibronectinAlternative SplicingProtein Subunitsembryonic structuresbiology.proteinProtein MultimerizationChickensMatrix Biology
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Characterizing the N-terminal processing motif of MHC class I ligands.

2008

Abstract Most peptide ligands presented by MHC class I molecules are the product of an intracellular pathway comprising protein breakdown in the cytosol, transport into the endoplasmic reticulum, and successive N-terminal trimming events. The efficiency of each of these processes depends on the amino acid sequence of the presented ligand and its precursors. Thus, relating the amino acid composition N-terminal of presented ligands to the sequence specificity of processes in the pathway gives insight into the usage of ligand precursors in vivo. Examining the amino acid composition upstream the true N terminus of MHC class I ligands, we demonstrate the existence of a distinct N-terminal proces…

Proteasome Endopeptidase ComplexImmunologyAmino Acid MotifsEndoplasmic ReticulumLigandsAminopeptidaseAminopeptidasesCell LineMiceCytosolCell Line TumorMHC class IImmunology and AllergyAnimalsHumansAmino Acid SequenceATP Binding Cassette Transporter Subfamily B Member 2Peptide sequenceAntigen PresentationbiologyLigandEndoplasmic reticulumHistocompatibility Antigens Class ITransporter associated with antigen processingPeptide FragmentsN-terminusBiochemistryProteasomebiology.proteinATP-Binding Cassette TransportersPeptidesHeLa CellsProtein BindingJournal of immunology (Baltimore, Md. : 1950)
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Features of TAP-independent MHC class I ligands revealed by quantitative mass spectrometry.

2008

TAP is responsible for transferring cytosolic peptides into the ER, where they can be loaded onto MHC molecules. Deletion of TAP results in a drastic reduction of MHC class I surface expression and alters the presented peptide pattern. This key molecule in antigen processing is tackled by several viruses and lost in some tumors, rendering the altered cells less vulnerable to T cell-based immune surveillance. Using the TAP-deficient cell line LCL721.174 and its TAP-expressing progenitor cell line LCL721.45, we identified and quantified more than 160 HLA ligands, 50 of which were presented TAP-independently. Peptides which were predominantly presented on the TAP-deficient LCL721.174 cell line…

Proteasome Endopeptidase ComplexImmunologyAntigen presentationEpitopes T-LymphocyteGene ExpressionHuman leukocyte antigenCysteine Proteinase InhibitorsProtein Sorting SignalsMajor histocompatibility complexCell LineAntigenATP Binding Cassette Transporter Subfamily B Member 3HLA AntigensTandem Mass SpectrometryMHC class IHLA-A2 AntigenImmunology and AllergyHumansAmino Acid SequenceATP Binding Cassette Transporter Subfamily B Member 2Antigen PresentationbiologyHLA-A AntigensAntigen processingHistocompatibility Antigens Class IProteinsTransporter associated with antigen processingMHC restrictionMolecular biologyPeptide FragmentsCell biologyHLA-B AntigensIsotope Labelingbiology.proteinATP-Binding Cassette TransportersProteasome InhibitorsGene DeletionProtein BindingEuropean journal of immunology
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Proteasomes shape the repertoire of T cells participating in antigen-specific immune responses

2006

Differences in the cleavage specificities of constitutive proteasomes and immunoproteasomes significantly affect the generation of MHC class I ligands and therefore the activation of CD8-positive T cells. Based on these findings, we investigated whether proteasomal specificity also influences CD8-positive T cells during thymic selection by peptides derived from self proteins. We find that one of the self peptides responsible for positive selection of ovalbumin-specific OT-1 T cells, which is derived from the f-actin capping protein (Cpalpha1), is efficiently generated only by immunoproteasomes. Furthermore, OT-1 mice backcrossed onto low molecular mass protein 7 (LMP7)-deficient mice show a…

Proteasome Endopeptidase ComplexOvalbuminActin Capping ProteinsT-LymphocytesMolecular Sequence DataReceptors Antigen B-CellThymus GlandBiologyEpitopeInterleukin 21MiceImmune systemAntigenMultienzyme ComplexesMHC class ICytotoxic T cellT cell repertoire; selectionAnimalsIL-2 receptorAmino Acid SequenceAntigensSelection GeneticBone Marrow TransplantationMice KnockoutMultidisciplinaryBiological SciencesMolecular biologyPeptide FragmentsMice Inbred C57BLCTL*biology.proteinLymph Nodes
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Quantitative Analysis of Prion-Protein Degradation by Constitutive and Immuno-20S Proteasomes Indicates Differences Correlated with Disease Susceptib…

2004

Abstract The main part of cytosolic protein degradation depends on the ubiquitin-proteasome system. Proteasomes degrade their substrates into small peptide fragments, some of which are translocated into the endoplasmatic reticulum and loaded onto MHC class I molecules, which are then transported to the cell surface for inspection by CTL. A reliable prediction of proteasomal cleavages in a given protein for the identification of CTL epitopes would benefit immensely from additional cleavage data for the training of prediction algorithms. To increase the knowledge about proteasomal specificity and to gain more insight into the relation of proteasomal activity and susceptibility to prion diseas…

Proteasome Endopeptidase ComplexPrionsMolecular Sequence DataImmunologyCellProtein degradationPeptide MappingMultienzyme ComplexesMHC class ImedicineAnimalsHumansImmunology and AllergyAmino Acid SequencePeptide sequenceAllelesCell Line TransformedSheepbiologyHydrolysisMolecular biologyPeptide FragmentsRecombinant ProteinsCell biologyCysteine EndopeptidasesKineticsCytosolCTL*medicine.anatomical_structureProteasomeCell culturebiology.proteinDisease SusceptibilityThe Journal of Immunology
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Conformational clamping by a membrane ligand activates the EphA2 receptor

2021

AbstractThe EphA2 receptor is a promising drug target for cancer treatment, since EphA2 activation can inhibit metastasis and tumor progression. It has been recently described that the TYPE7 peptide activates EphA2 using a novel mechanism that involves binding to the single transmembrane domain of the receptor. TYPE7 is a conditional transmembrane (TM) ligand, which only inserts into membranes at neutral pH in the presence of the TM region of EphA2. However, how membrane interactions can activate EphA2 is not known. We systematically altered the sequence of TYPE7 to identify the binding motif used to activate EphA2. With the resulting six peptides, we performed biophysical and cell migratio…

Protein ConformationSequence HomologyTm ligandsPeptideMolecular Dynamics SimulationLigandsReceptor tyrosine kinaseArticleBimolecular fluorescence complementationProtein DomainsStructural BiologyCell MovementCell surface receptorTumor Cells CulturedHumansAmino Acid SequenceReceptorMolecular BiologyMelanomachemistry.chemical_classificationBinding SitesMembranesbiologyChemistryReceptor EphA2Membrane ProteinsLigand (biochemistry)Peptide FragmentsTransmembrane proteinTransmembrane domainMembranebiology.proteinBiophysicsProtein MultimerizationProtein Binding
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