Search results for "compatibility"

showing 10 items of 859 documents

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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The Transporter Associated With Antigen Processing (TAP): Structural Integrity, Expression, Function, and Its Clinical Relevance

2001

BACKGROUND: The transporter associated with antigen processing (TAP), a member of the family of ABC transporters, plays a crucial role in the processing and presentation of the major histocompatibility complex (MHC) class I restricted antigens. TAP transports peptides from the cytosol into the endoplasmic reticulum, thereby selecting peptides matching in length and sequence to respective MHC class I molecules. Upon loading on MHC class I molecules, the trimeric MHC class I/beta2-microglobulin/ peptide complex is then transported to the cell surface and presented to CD8+ cytotoxic T cells. Abnormalities in MHC class I surface expression have been found in a number of different malignancies, …

Protein ConformationAntigen processingAntigen presentationCD1Transporter associated with antigen processingBiologyMHC restrictionMajor histocompatibility complexModels BiologicalCell biologyGene Expression RegulationAntigenMHC class IGeneticsbiology.proteinHumansMolecular MedicineATP-Binding Cassette TransportersMolecular BiologyGenetics (clinical)Research ArticleMolecular Medicine
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Axolotl MHC architecture and polymorphism.

1999

The MHC of the urodele amphibian Ambystoma mexicanum consists of multiple polymorphic class I loci linked, so far as yet known, to a single class II B locus. This architecture is very different from that of the anuran amphibian Xenopus. The number of class I loci in the axolotl can vary from 6 to 21 according to the haplotypes as shown by cDNA analysis and Southern blot studies in families. These loci can be classified into seven sequence groups with features ranging from the class Ia to the class Ib type. All individuals express genes from at least three of the seven groups, and all individuals possess the class Ia-like type.

Protein ConformationImmunologyGenes MHC Class IIMolecular Sequence DataGenes MHC Class IMajor histocompatibility complexAmbystomaEvolution MolecularMajor Histocompatibility ComplexAxolotlPolymorphism (computer science)Complementary DNAHLA-A2 AntigenImmunology and AllergyAnimalsHumansAmino Acid SequenceAmbystoma mexicanumGeneConserved SequenceSouthern blotGeneticsPolymorphism GeneticbiologyHaplotypebiology.organism_classificationBlotting Southernbiology.proteinEuropean journal of immunology
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Processing requirements for the recognition of insulin fragments by murine T cells.

1988

In this study we investigated aspects of antigen processing using insulin and insulin A chain-derived fragments as model antigens in Ab alpha Ak beta-restricted T-cell stimulation. Similarly to other proteins, the immunodominant region of insulin recognized by these T cells is limited in size. It is located on the insulin A chain and encompasses a portion of the molecule that is represented faithfully by peptide A1-14(SSO3-)3. Efficient presentation of intact insulin and its entire A chain is dependent on uptake and processing by APC. Whereas peptides stemming from various globular proteins are known to be presented to T cells by APC without requiring processing, this is not the case with A…

Protein Denaturationmedicine.medical_treatmentT-LymphocytesImmunologyReceptors Antigen T-CellAntigen-Presenting CellsPeptideLymphocyte ActivationMajor Histocompatibility Complexchemistry.chemical_compoundEpitopesAntigenmedicineImmunology and AllergyAnimalsInsulinchemistry.chemical_classificationMHC class IIbiologyAntigen processingInsulinT-cell receptorTunicamycinClone CellsRatsBiochemistrychemistrybiology.proteinInsulin processingImmunological reviews
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Minimal Information About an Immuno-Peptidomics Experiment (MIAIPE)

2018

Minimal Information about an Immuno-Peptidomics Experiment (MIAIPE) is an initiative of the members of the Human Immuno-Peptidome Project (HIPP), an international program organized by the Human Proteome Organization (HUPO). The aim of the MIAIPE guidelines is to deliver technical guidelines representing the minimal information required to sufficiently support the evaluation and interpretation of immunopeptidomics experiments. The MIAIPE document has been designed to report essential information about sample preparation, mass spectrometric measurement and associated mass spectrometry (MS)-related bioinformatics aspects that are unique to immunopeptidomics and may not be covered by the genera…

Proteomics0301 basic medicineComputer scienceComputational biologyProteomicsBiochemistrySpecimen Handling03 medical and health sciencesStandardisation & GuidelinesHuman proteome projectHumansantigen processing and presentationDatabases ProteinMolecular Biology030102 biochemistry & molecular biologyHistocompatibility Antigens Class IHistocompatibility Antigens Class IIimmunopeptidomicsComputational BiologyMass spectrometricPeptide Fragmentsmajor histocompatibility complex3. Good health030104 developmental biologyComputational Biology/standards; Databases Protein; Histocompatibility Antigens Class I/analysis; Histocompatibility Antigens Class I/immunology; Histocompatibility Antigens Class I/metabolism; Histocompatibility Antigens Class II/analysis; Histocompatibility Antigens Class II/immunology; Histocompatibility Antigens Class II/metabolism; Humans; Peptide Fragments/analysis; Peptide Fragments/immunology; Peptide Fragments/metabolism; Proteomics/standards; Software; Specimen Handling/standards; antigen processing and presentation; immunopeptidomics; major histocompatibility complexSoftwareantigen processing and presentation; immunopeptidomics; major histocompatibility complex
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SANS (USH1G) regulates pre-mRNA splicing by mediating the intra-nuclear transfer of tri-snRNP complexes

2021

Abstract Splicing is catalyzed by the spliceosome, a compositionally dynamic complex assembled stepwise on pre-mRNA. We reveal links between splicing machinery components and the intrinsically disordered ciliopathy protein SANS. Pathogenic mutations in SANS/USH1G lead to Usher syndrome—the most common cause of deaf-blindness. Previously, SANS was shown to function only in the cytosol and primary cilia. Here, we have uncovered molecular links between SANS and pre-mRNA splicing catalyzed by the spliceosome in the nucleus. We show that SANS is found in Cajal bodies and nuclear speckles, where it interacts with components of spliceosomal sub-complexes such as SF3B1 and the large splicing cofact…

ProteomicsAcademicSubjects/SCI00010Ribonucleoprotein U4-U6 Small NuclearSF3B1 GeneMass Spectrometry0302 clinical medicineRNA Small NuclearRNA PrecursorsIn Situ Hybridization FluorescenceRibonucleoprotein0303 health sciencesChemistryRibonucleoproteins Small NuclearImmunohistochemistryCell biologyDNA-Binding Proteinsmedicine.anatomical_structureGene Knockdown TechniquesRNA splicingRNA Splicing FactorsUsher SyndromesSpliceosomeCoiled BodiesNerve Tissue ProteinsBiologyMinor Histocompatibility Antigens03 medical and health sciencesMicroscopy Electron TransmissionRNA and RNA-protein complexesGeneticsmedicineHumanssnRNPEye ProteinsGeneCell Proliferation030304 developmental biologyCell NucleusRNAmedicine.diseasePhosphoproteinsCiliopathyAlternative SplicingCell nucleusHEK293 CellsCajal bodyCytoplasmSpliceosomesNucleus030217 neurology & neurosurgeryTranscription FactorsNucleic Acids Research
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Complement proteins regulating macrophage polarisation on biomaterials

2019

[EN] One of the events occurring when a biomaterial is implanted in an host is the protein deposition onto its surface, which might regulate cell responses. When a biomaterial displays a compromised biocompatibility, distinct complement pathways can be activated to produce a foreign body reaction. In this article, we have designed different types of biomaterial surfaces to study the inflammation process. Here, we used different concentrations of (3-glycidoxypropyl)-trimethoxysilane (GPTMS), an organically-modified alkoxysilane as a precursor for the synthesis of various types of sol-gel materials functionalizing coatings for titanium implants to regulate biological responses. Our results sh…

ProteomicsCellBiocompatible Materials02 engineering and technology01 natural sciencesimmune responseMiceColloid and Surface ChemistryCIENCIA DE LOS MATERIALES E INGENIERIA METALURGICATitanium010304 chemical physicsChemistryhybrid sol-gelBiomaterialSurfaces and InterfacesGeneral MedicineSilanes021001 nanoscience & nanotechnologyInterleukin-10medicine.anatomical_structureReconstructive and regenerative medicine Radboud Institute for Molecular Life Sciences [Radboudumc 10]Rabbits0210 nano-technologyBiotechnologyComplement systemBiocompatibilitySurface PropertiesMacrophage polarizationmacrophage plasticityOsseointegrationHybrid sol-gelMacrophage plasticityImmune systemAll institutes and research themes of the Radboud University Medical Centerproteomicsdental implants0103 physical sciencesmedicineAnimalsSecretionParticle SizePhysical and Theoretical ChemistryImmune responsecomplement systemTibiaTumor Necrosis Factor-alphaMacrophagesDental implantsComplement System ProteinsComplement systemRAW 264.7 CellsBiophysics
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Vaccination with TAT-Antigen Fusion Protein Induces Protective, CD8+ T Cell-Mediated Immunity Against Leishmania Major

2010

In murine leishmaniasis, healing is mediated by IFN-γ-producing CD4 + and CD8 + T cells. Thus, an efficacious vaccine should induce Th1 and Tc1 cells. Dendritic cells (DCs) pulsed with exogenous proteins primarily induce strong CD4-dependent immunity; induction of CD8 responses has proven to be difficult. We evaluated the immunogenicity of fusion proteins comprising the protein transduction domain of HIV-1 TAT and the Leishmania antigen LACK ( Leishmania homolog of receptors for activated C kinase), as TAT-fusion proteins facilitate major histocompatibility complex class I-dependent antigen presentation. In vitro , TAT–LACK-pulsed DCs induced stronger proliferation of Leishmania -specific C…

Protozoan VaccinesAntigen presentationProtozoan ProteinsLeishmaniasis CutaneousAntigens ProtozoanDermatologyCD8-Positive T-LymphocytesBiologyMajor histocompatibility complexBiochemistryArticleMiceAntigenAnimalsCytotoxic T cellLeishmania majorMolecular BiologyLeishmania majorImmunogenicityDendritic CellsCell BiologyTh1 Cellsbiology.organism_classificationInterleukin-12Fusion proteinMice Mutant StrainsCell biologyMice Inbred C57BLImmunologybiology.proteintat Gene Products Human Immunodeficiency VirusViral Fusion ProteinsCD8Journal of Investigative Dermatology
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Nanometric ion pair complexes of tobramycin forming microparticles for the treatment of Pseudomonas aeruginosa infections in cystic fibrosis

2019

Abstract Sustained pulmonary delivery of tobramycin from microparticles composed of drug/polymer nanocomplexes offers several advantages against traditional delivery methods. Namely, in patients with cystic fibrosis, microparticle delivery can protect the tobramycin being delivered from strong mucoadhesive interactions, thus avoiding effects on its diffusion toward the infection site. Polymeric ion-pair complexes were obtained starting from two synthetic polyanions, through impregnation of their solid dissociated forms with tobramycin in aqueous solution. The structure of these polymeric systems was characterized, and their activities were examined against various biofilm-forming Pseudomona…

Pseudomonas aeruginosa infectionpseudomonas aeruginosa infectionsBiocompatibilityCystic FibrosisαPharmaceutical Science02 engineering and technologymedicine.disease_cause030226 pharmacology & pharmacyCystic fibrosisCell Line03 medical and health sciences0302 clinical medicineIon-pair complexmedicineTobramycinHumansPseudomonas InfectionsMicroparticleαβ-Poly-(N-2-hydroxyethyl)-dl-aspartamide (PHEA)β-Poly-(N-2-hydroxyethyl)-dl-aspartamide (PHEA)chemistry.chemical_classificationDrug CarriersAqueous solutionPseudomonas aeruginosaBiofilms; Cystic fibrosis artificial mucus (CF-AM); Ion-pair complex; Pseudomonas aeruginosa infections; Tobramycin; α; β-Poly-(N-2-hydroxyethyl)-dl-aspartamide (PHEA)BiofilmBiofilmPolymerBiofilms; cystic fibrosis artificial mucus (CF-AM); Ion-pair complex; pseudomonas aeruginosa infections; Tobramycin; αβ-Poly-(N-2-hydroxyethyl)-dl-aspartamide (PHEA)021001 nanoscience & nanotechnologymedicine.diseaseAnti-Bacterial AgentsMucuschemistryBiofilmsPseudomonas aeruginosaBiophysicsTobramycinNanoparticlescystic fibrosis artificial mucus (CF-AM)0210 nano-technologyPeptidesmedicine.drug
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