Search results for "FRAGMENTS"

showing 10 items of 422 documents

A tyrosinase peptide presented by HLA-B35 is recognized on a human melanoma by autologous cytotoxic T lymphocytes

1999

We previously described different cytotoxic T lymphocyte (CTL) clones isolated from the blood lymphocytes of a melanoma patient after in vitro stimulation with autologous tumor cells. These CTL clones recognized at least 2 distinct antigens on the melanoma cells. Here, we show that one of them consists of a peptide derived from tyrosinase and presented by HLA-B35. The peptide is 9 amino acids long and has the sequence LPSSADVEF. It can be presented by the 2 major B35 allelic subtypes, B*3501 and B*3503. As HLA-B35 is one of the most frequent HLA-B specificities, being present in about 20% of Caucasian individuals, it may be a useful target for peptide-based immunotherapy of melanoma.

Cytotoxicity ImmunologicHerpesvirus 4 HumanCancer Researchmedicine.medical_treatmentAntigen presentationTyrosinase PeptideBiologyTransfectionAntigenTumor Cells CulturedmedicineAnimalsHumansCytotoxic T cellAmino Acid SequenceMelanomaPeptide sequenceAllelesCell Line TransformedB-LymphocytesMonophenol MonooxygenaseMelanomaImmunotherapymedicine.diseasePeptide FragmentsRecombinant ProteinsCTL*OncologyCOS CellsImmunologyCancer researchHLA-B35 AntigenT-Lymphocytes CytotoxicInternational Journal of Cancer
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Inhibition of the NKp30 activating receptor by pp65 of human cytomegalovirus.

2005

Human cytomegalovirus, a chief pathogen in immunocompromised people, can persist in a healthy immunocompetent host throughout life without being eliminated by the immune system. Here we show that pp65, the main tegument protein of human cytomegalovirus, inhibited natural killer cell cytotoxicity by an interaction with the activating receptor NKp30. This interaction was direct and specific, leading to dissociation of the linked CD3zeta from NKp30 and, consequently, to reduced killing. Thus, pp65 is a ligand for the NKp30 receptor and demonstrates a unique mechanism by which an intracellular viral protein causes general suppression of natural killer cell cytotoxicity by specific interaction w…

Cytotoxicity ImmunologicHuman cytomegalovirusViral proteinvirusesImmunologyCytomegalovirusReceptors Cell SurfaceBiologymedicine.disease_causeNatural killer cellViral Matrix ProteinsMiceImmune systemmedicineAnimalsHumansImmunology and AllergyReceptors ImmunologicCytotoxicityReceptorCells CulturedMembrane GlycoproteinsNatural Cytotoxicity Triggering Receptor 3virus diseasesPhosphoproteinsmedicine.diseaseVirologyImmunoglobulin Fc FragmentsCell biologyKiller Cells NaturalNatural Cytotoxicity Triggering Receptor 3Kineticsmedicine.anatomical_structureGene Expression RegulationIntracellularProtein BindingNature immunology
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Impaired Transporter Associated with Antigen Processing (TAP) Function Attributable to a Single Amino Acid Alteration in the Peptide TAP Subunit TAP1

2003

Abstract The heterodimeric peptide transporter TAP belongs to the ABC transporter family. Sequence comparisons with the P-glycoprotein and cystic fibrosis transmembrane conductance regulator and the functional properties of selective amino acids in these ABC transporters postulated that the glutamic acid at position 263 and the phenylalanine at position 265 of the TAP1 subunit could affect peptide transporter function. To define the role of both amino acids, TAP1 mutants containing a deletion or a substitution to alanine at position 263 or 265 were generated and stably expressed in murine and human TAP1−/− cells. The different TAP1 mutants were characterized in terms of expression and funct…

Cytotoxicity ImmunologicMacromolecular SubstancesPhenylalanineImmunologyAntigen presentationGlutamic AcidATP-binding cassette transporterEndoplasmic ReticulumTransfectionCell LineMiceAdenosine TriphosphateATP Binding Cassette Transporter Subfamily B Member 3MHC class IAnimalsHumansImmunology and AllergyATP Binding Cassette Transporter Subfamily B Member 2Sequence DeletionAlaninechemistry.chemical_classificationAntigen PresentationbiologyHistocompatibility Antigens Class I3T3 CellsIntracellular MembranesTransporter associated with antigen processingMolecular biologyPeptide FragmentsCystic fibrosis transmembrane conductance regulatorAmino acidMice Inbred C57BLProtein SubunitsAmino Acid SubstitutionBiochemistrychemistryMutagenesis Site-Directedbiology.proteinATP-Binding Cassette TransportersTAP1Sequence AlignmentProtein BindingT-Lymphocytes CytotoxicThe Journal of Immunology
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H-2(d) mice born to and reared by HBeAg-transgenic mothers do not develop T cell tolerance toward the hepatitis B virus core gene products.

2000

The function of the secretory core gene product (HBeAg) of the human hepatitis B virus (HBV) is unknown. It has been proposed that this protein may be passed from the mother to her offspring at the perinatal stage where it might induce immune tolerance. In a previous study we have shown that the murine placenta presents an efficient barrier for the HBe protein and that H-2(b) mice born to HBeAg-positive transgenic mothers do not develop tolerance of specific cytotoxic T cells. In the present work we demonstrate that transgenic mice expressing high serum levels of HBeAg secrete only small amounts of this protein into their milk and excrete minute amounts of the viral gene product in their ur…

Cytotoxicity ImmunologicMaleHepatitis B virusT cellvirusesT-LymphocytesMothersMice TransgenicBiologymedicine.disease_causeLymphocyte ActivationImmune toleranceMiceImmune systemVirologymedicineImmune ToleranceCytotoxic T cellAnimalsHepatitis B e AntigensHepatitis B AntibodiesHepatitis B virusMice Inbred BALB CH-2 Antigensvirus diseasesT-Lymphocytes Helper-InducerHepatitis Bmedicine.diseaseHepatitis BVirologydigestive system diseasesPeptide Fragmentsmedicine.anatomical_structureMilkHBeAgAnimals NewbornImmunologyFemaleCD8T-Lymphocytes CytotoxicVirology
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Targeting positive regulatory domain I-binding factor 1 and X box-binding protein 1 transcription factors by multiple myeloma-reactive CTL.

2005

Abstract Growing evidence indicates that multiple myeloma (MM) and other malignancies are susceptible to CTL-based immune interventions. We studied whether transcription factors inherently involved in the terminal differentiation of mature B lymphocytes into malignant and nonmalignant plasma cells provide MM-associated CTL epitopes. HLA-A*0201 (A2.1) transgenic mice were used to identify A2.1-presented peptide Ag derived from the plasma cell-associated transcriptional regulators, positive regulatory domain I-binding factor 1 (PRDI-BF1) and X box-binding protein 1 (XBP-1). A2.1-restricted CTL specific for PRDI-BF1 and XBP-1 epitopes efficiently killed a variety of MM targets. PRDI-BF1- and X…

Cytotoxicity ImmunologicX-Box Binding Protein 1Cellular differentiationImmunologyEpitopes T-LymphocyteMice TransgenicRegulatory Factor X Transcription FactorsBiologyEpitopeMiceImmune systemCell Line TumorHLA-A2 AntigenImmunology and AllergyAnimalsHumansTranscription factorAntigen PresentationB-LymphocytesCell DeathT-cell receptorCell DifferentiationCytotoxicity Tests ImmunologicX-Box Binding Protein 1Molecular biologyPeptide FragmentsCell biologyDNA-Binding ProteinsMice Inbred C57BLRepressor ProteinsCTL*Self ToleranceNIH 3T3 CellsPositive Regulatory Domain I-Binding Factor 1Multiple MyelomaCD8T-Lymphocytes CytotoxicTranscription FactorsJournal of immunology (Baltimore, Md. : 1950)
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The sequence alteration associated with a mutational hotspot in p53 protects cells from lysis by cytotoxic T lymphocytes specific for a flanking pept…

1998

A high proportion of tumors arise due to mutation of the p53 tumor suppressor protein. A p53 hotspot mutation at amino acid position 273 from R to H, flanking a peptide epitope that spans residues 264–272, renders cells resistant to killing by human histocompatibility leukocyte antigen (HLA)-A*0201–restricted cytotoxic T lymphocytes (CTLs) specific for this epitope. Acquisition of the R to H mutation at residue 273 of the human p53 protein promotes tumor growth in vivo by selective escape from recognition by p53.264–272 peptide-specific CTLs. Synthetic 27-mer p53 polypeptides covering the antigenic nonamer region 264–272 of p53 were used as proteasome substrates to investigate whether the R…

Cytotoxicity Immunologicp53Epitopes T-LymphocyteEpitopeSubstrate SpecificityMice0302 clinical medicineTumor Cells CulturedImmunology and AllergyCytotoxic T cellPeptide sequence0303 health sciencesAntigen PresentationproteasomesHydrolysisArticles3. Good healthCysteine Endopeptidasestumor antigensCell DivisionProteasome Endopeptidase ComplexImmunologyAntigen presentationMolecular Sequence DataMice TransgenicBiologyArgininecytotoxic T lymphocytes03 medical and health sciencesAntigenMultienzyme Complexesantigen processingAnimalsHumansPoint MutationHistidineAmino Acid Sequence030304 developmental biologyBinding SitesLinear epitopeHLA-A AntigensPoint mutationCytotoxicity Tests ImmunologicMolecular biologyPeptide FragmentsCTL*Tumor Suppressor Protein p53Peptides030215 immunologyT-Lymphocytes CytotoxicThe Journal of experimental medicine
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The disintegrin ADAM9 indirectly contributes to the physiological processing of cellular prion by modulating ADAM10 activity

2005

The cellular prion protein (PrP(c)) is physiologically cleaved in the middle of its 106-126 amino acid neurotoxic region at the 110/111 downward arrow112 peptidyl bond, yielding an N-terminal fragment referred to as N1. We recently demonstrated that two disintegrins, namely ADAM10 and ADAM17 (TACE, tumor necrosis factor alpha converting enzyme) participated in both constitutive and protein kinase C-regulated generation of N1, respectively. These proteolytic events were strikingly reminiscent of those involved in the so-called "alpha-secretase pathway" that leads to the production of secreted sAPPalpha from betaAPP. We show here, by transient and stable transfection analyses, that ADAM9 also…

DNA ComplementaryADAM10Gene ExpressionTransfectionBiochemistryDNA AntisenseCell LineAmyloid beta-Protein PrecursorMice03 medical and health sciences0302 clinical medicineEndopeptidasesDisintegrinAnimalsAspartic Acid EndopeptidasesHumansPrPC Proteins[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyProtein kinase AMolecular Biology030304 developmental biologyMice Knockout0303 health sciencesbiologyHEK 293 cells030302 biochemistry & molecular biologyMembrane ProteinsTransfectionCell BiologyFibroblastsPeptide FragmentsADAM ProteinsBiochemistryCell culturebiology.proteinAdditions and CorrectionsAmyloid Precursor Protein SecretasesADAM9Amyloid precursor protein secretase030217 neurology & neurosurgery
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The glycosyltransferase activities of lysyl hydroxylase 3 (LH3) in the extracellular space are important for cell growth and viability.

2008

Abstract Lysyl hydroxylase (LH) isoform 3 is a post-translational enzyme possessing LH, collagen galactosyltransferase (GT) and glucosyltransferase (GGT) activities. We have demonstrated that LH3 is found not only intracellularly, but also on the cell surface and in the extracellular space, suggesting additional functions for LH3. Here we show that the targeted disruption of LH3 by siRNA causes a marked reduction of both glycosyltransferase activities, and the overexpression of LH3 in HT-1080 cells increases hydroxylation of lysyl residues and the subsequent galactosylation and glucosylation of hydroxylysyl residues. These data confirm the multi-functionality of LH3 in cells. Furthermore, t…

DNA ComplementaryGlycosylationCell SurvivalLysyl hydroxylaseCellhydroxylysyl glycosylationFluorescent Antibody Techniquelysyl hydroxylaseMicrotubulesPermeabilityCell LineGlycosyltransferasemedicineExtracellularAnimalsHumanscell growthViability assayRNA Small InterferingCell Shapecell viabilityCell ProliferationbiologyCell DeathCell growthProcollagen-Lysine 2-Oxoglutarate 5-Dioxygenasecollagen biosynthesisGlycosyltransferasesCell BiologyArticlesGalactosyltransferasesMolecular biologyPeptide FragmentsCulture MediaActin Cytoskeletonmedicine.anatomical_structurepost-translational modificationCell culturebiology.proteinMolecular MedicineGlucosyltransferaseExtracellular Spacehydroxylysyl glycosyltransferaseJournal of cellular and molecular medicine
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Analysis of expression of an alternative La (SS-B) cDNA and localization of the encoded N- and C-terminal peptides

1997

AbstractA deletion of an (A)-residue was detected in a cDNA encoding for the nuclear autoantigen La/SS-B. The cDNA was recently isolated from a cDNA library made from peripheral blood lymphocytes of a patient with primary Sjögren's Syndrome. The region, where the deletion occurred, represents a hot spot region in the La gene(s). It leads to a frame shift mutation and a premature stop codon eleven amino acids downstream of the deletion site within one of the protease sensitive regions of the La protein. In spite of the frame shift mutation expression of full length La protein occurred efficiently in E. coli. Full length La protein was also made in SF9 cells infected with recombinant baculovi…

DNA ComplementaryMolecular Sequence DataBiologyAutoantigensCell LineFrameshift mutationSingle-stranded binding proteinComplementary DNAEscherichia coliConsensus sequenceProtein biosynthesisHumansAmino Acid SequenceGeneMolecular BiologyBase SequencecDNA libraryCell BiologyMolecular biologyPeptide FragmentsSjogren's SyndromeRibonucleoproteinsCytoplasmMutationbiology.proteinBaculoviridaeGene DeletionBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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Therapeutic application of T cell receptor mimic peptides or cDNA in the treatment of T cell-mediated skin diseases

2000

An 8-amino acid peptide encoding a sequence of the transmembrane region of the T cell receptor alpha chain (TCR-alpha) was shown to inhibit T cell function by preventing functional assembly of the T cell receptor (mimic peptide). To avoid systemic immunosuppression by peptide application in vivo, we used a topical application of the peptide. In the system of murine contact sensitivity, topical application of the peptide inhibited the elicitation of contact sensitivity following application of a contact allergen in sensitized animals. Alternatively, when naked DNA encoding the peptide sequence was injected into skin before application of a contact allergen to sensitized animals, local immuno…

DNA ComplementaryReceptors Antigen T-Cell alpha-betaT-LymphocytesT cellGenetic enhancementPeptidePharmacologyBiologySkin DiseasesDermatitis AtopicMiceAntigenVaccines DNAGeneticsmedicineAnimalsHumansReceptorMolecular BiologyPeptide sequenceImmunosuppression Therapychemistry.chemical_classificationMice Inbred BALB CT-cell receptorAllergensPeptide Fragmentsmedicine.anatomical_structurechemistryNaked DNADermatitis Allergic ContactImmunologyMolecular MedicineGene Therapy
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