Search results for " glycoprotein"

showing 10 items of 430 documents

TLR3-induced activation of mast cells modulates CD8+ T-cell recruitment.

2005

AbstractMast cells play an important role in host defense against various pathogens, but their role in viral infection has not been clarified in detail. dsRNA, synthesized by various types of viruses and mimicked by polyinosinic-polycytidylic acid (poly(I:C)) is recognized by Toll-like receptor 3 (TLR3). In this study, we demonstrate that poly(I:C) injection in vivo potently stimulates peritoneal mast cells to up-regulate a number of different costimulatory molecules. Therefore, we examined the expression and the functional significance of TLR3 activation in mast cells. Mast cells express TLR3 on the cell surface and intracellularly. After stimulation of mast cells with poly(I:C) and Newcas…

Chemokinevirusesmedicine.medical_treatmentImmunologyNewcastle disease virusReceptors Cell SurfaceBiologyCD8-Positive T-LymphocytesBiochemistryMicemedicineCytotoxic T cellAnimalsMast CellsPhosphorylationPeritoneal CavityMice KnockoutInnate immune systemMembrane GlycoproteinsToll-Like ReceptorsCell BiologyHematologymedicine.diseaseMast cellImmunity InnateCell biologyToll-Like Receptor 3Up-RegulationMice Inbred C57BLChemotaxis Leukocytemedicine.anatomical_structureCytokinePoly I-CTLR3ImmunologyMast cell sarcomabiology.proteinCytokinesCD8Blood
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Endoplasmic reticulum‐resident chaperones modulate the inflammatory and angiogenic responses of endothelial cells

2015

SummaryBackground Wound healing depends on a well-balanced regulation of inflammation and angiogenesis. In chronic wounds the healing process is disturbed and inflammation persists. Regulation of wound closure is controlled by transmembrane and extracellular proteins, the folding and maturation of which occur in the endoplasmic reticulum (ER) by ER-resident chaperone machinery. Objectives To study the role of the ER-resident chaperones BiP/Grp78, its cochaperone Mdg1/ERdJ4, and Grp94 in chronic, nonhealing wounds. Methods Immunohistochemical staining of these chaperones in individual human biopsies and investigation of the possible role of BiP and Mdg1 in endothelial cells, focusing on thei…

Chronic woundChemokineAngiogenesisDown-RegulationNeovascularization PhysiologicInflammationDermatologyEndoplasmic ReticulumProinflammatory cytokinemedicineHumansEndoplasmic Reticulum Chaperone BiPCells CulturedHeat-Shock ProteinsInflammationWound HealingMembrane GlycoproteinsbiologyTumor Necrosis Factor-alphaEndoplasmic reticulumEndothelial CellsMembrane ProteinsHSP40 Heat-Shock ProteinsCell biologyChaperone (protein)Chronic Diseasebiology.proteinmedicine.symptomWound healingMolecular ChaperonesBritish Journal of Dermatology
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Optical studies on the specific interaction of dipyridamole with alpha 1-acid glycoprotein (orosomucoid).

1982

Abstract The interaction of dipyridamole with α1-acid glycoprotein was investigated by circular dichroism and ultraviolet absorbance measurements as well as by equilibrium dialysis experiments. Dipyridamole is bound to the protein via one site of extremely high affinity and by at least one site of considerably lower affinity. Only the association of dipyridamole with the high affinity site produces typical extrinsic Cotton effects. As a result of experimental observations it is concluded that the high affinity site is located in a hydrophobic protein structure of the glycoprotein.

Circular dichroismChemical PhenomenaStereochemistryProtein ConformationPharmaceutical ScienceOrosomucoidIn Vitro TechniquesProtein structuremedicineHumansPharmacologychemistry.chemical_classificationbiologyChemistry PhysicalCircular DichroismTryptophanDipyridamoleOrosomucoidUltraviolet absorbanceDipyridamoleLower affinitychemistryα1 acid glycoproteinbiology.proteinTyrosineSpectrophotometry UltravioletGlycoproteinDialysismedicine.drugProtein BindingThe Journal of pharmacy and pharmacology
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Roles of a conserved proline in the internal fusion peptide of Ebola glycoprotein

2004

AbstractThe structural determinants underlying the functionality of viral internal fusion peptides (IFPs) are not well understood. We have compared EBOwt (GAAIGLAWIPYFGPAAE), representing the IFP of the Ebola fusion protein GP, and EBOmut (GAAIGLAWIPYFGRAAE) derived from a non-functional mutant with conserved Pro537 substituted by Arg. P537R substitution did not abrogate peptide-membrane association, but interfered with the ability to induce bilayer destabilization. Structural determinations suggest that Pro537 is required to preserve a membrane-perturbing local conformation in apolar environments.

Circular dichroismEbola glycoproteinProtein insertion into membranesProlinePeptide conformationMutantMolecular Sequence DataBiophysicsBiochemistrySendai viruschemistry.chemical_compoundStructural BiologyGeneticsProlineAmino Acid SequenceMolecular BiologyPeptide sequencePOPCchemistry.chemical_classificationChemistryProteïnes de membranaCell BiologyEbolavirusFusion proteinPeptide FragmentsPeptide ConformationViral fusion peptideBiochemistryAvian Sarcoma VirusesLiposomesHIV-1PèptidsGlycoproteinPeptide–lipid interactionViral Fusion ProteinsFEBS Letters
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Binding of several phenothiazine neuroleptics to a common binding site of alpha 1-acid glycoprotein, orosomucoid.

1983

The interaction of several phenothiazine neuroleptics with alpha 1-acid glycoprotein was investigated using circular dichroism and equilibrium dialysis techniques. For chlorpromazine only, one high-affinity binding site of the protein was found. The binding of the drug to this single site generated typical polyphasic extrinsic Cotton effects. Since several other phenothiazine neuroleptics gave qualitatively comparable extrinsic Cotton effects in the presence of alpha 1-acid glycoprotein and potently inhibited the binding of chlorpromazine to the single site, it was concluded that all phenothiazine derivatives investigated bound preferentially to only one common binding site of the alpha 1-a…

Circular dichroismStereochemistryPharmaceutical ScienceOrosomucoidchemistry.chemical_compoundStructure-Activity RelationshipSingle sitePhenothiazinesPhenothiazinemedicineHumansBinding siteChlorpromazinechemistry.chemical_classificationBinding SitesbiologyChemistryCircular DichroismOrosomucoidBiochemistryα1 acid glycoproteinbiology.proteinGlycoproteinDialysismedicine.drugAntipsychotic AgentsProtein BindingJournal of pharmaceutical sciences
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Chemotactic migration of human diploid fibroblasts is inhibited by contactinhibin.

1992

Clinical BiochemistryBiologymedicineHumansFibroblastCell Line Transformedchemistry.chemical_classificationMembrane GlycoproteinsContact InhibitionChemotaxisContact inhibitionChemotaxisCell BiologyGeneral MedicineFibroblastsDiploidyCell biologyMembrane glycoproteinsmedicine.anatomical_structureBiochemistrychemistryCell culturebiology.proteinPloidyStem cellGlycoproteinDevelopmental BiologyIn vitro cellulardevelopmental biology : journal of the Tissue Culture Association
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Oral Glycoprotein IIb/IIa Antagonists for Unstable Angina — Is There Still a Chance for the Oral Substances?

2001

The intravenous glycoprotein IIb/IIIa antagonists abciximab, tirofiban and eptifibatide are well accepted for the therapy of patients with unstable angina and/or as concomitant medication during coronary interventions. Despite the fact that these drugs are not used in all patients presenting with unstable angina during coronary interventions, the scientific evidence is overwhelming including the substantial reduction in mortality 3 years after utilisation of abciximab for coronary interventions in patients with unstable angina. In addition to these two indications, intravenous glycoprotein IIb/IIIa antagonists are currently being investigated for use in patients undergoing carotid artery in…

Clinical Trials as Topicmedicine.medical_specialtyUnstable anginaFibrinogen receptorbusiness.industryAdministration OralPlatelet Glycoprotein GPIIb-IIIa ComplexHematologyTirofibanmedicine.diseaseAnginaInternal medicinemedicineAbciximabCardiologyEptifibatideHumansAngina UnstableMyocardial infarctionbusinessStrokePlatelet Aggregation Inhibitorsmedicine.drugThrombosis Research
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Ectodomain shedding of L1 adhesion molecule promotes cell migration by autocrine binding to integrins.

2001

The L1 adhesion molecule plays an important role in axon guidance and cell migration in the nervous system. L1 is also expressed by many human carcinomas. In addition to cell surface expression, the L1 ectodomain can be released by a metalloproteinase, but the biological function of this process is unknown. Here we demonstrate that membrane-proximal cleavage of L1 can be detected in tumors and in the developing mouse brain. The shedding of L1 involved a disintegrin and metalloproteinase (ADAM)10, as transfection with dominant-negative ADAM10 completely abolishes L1 release. L1-transfected CHO cells (L1-CHO) showed enhanced haptotactic migration on fibronectin and laminin, which was blocked …

CytoplasmIntegrinsL1; shedding; ADAM10; cell migration; integrinsADAM10IntegrinGene ExpressionCHO CellsBiologyArticle03 medical and health sciencesParacrine signallingMice0302 clinical medicineCell MovementCricetinaeEndopeptidasesTumor Cells CulturedAnimalsAspartic Acid EndopeptidasesHumansReceptors VitronectinFibrinolysinNeural Cell Adhesion Molecules030304 developmental biology0303 health sciencesBinding SitesMembrane GlycoproteinsCell adhesion moleculeCell MembraneAntibodies MonoclonalBrainCell migrationBiological TransportCell BiologyMolecular biologyPeptide FragmentsCell biologyFibronectinAutocrine CommunicationEctodomainSolubility030220 oncology & carcinogenesisbiology.proteinNeural cell adhesion moleculeAmyloid Precursor Protein SecretasesLeukocyte L1 Antigen ComplexOligopeptidesThe Journal of cell biology
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Differential expression of Cryptosporidium parvum genes encoding sporozoite surface antigens in infected HCT-8 host cells.

2006

Intracellular replication of Cryptosporidium parvum (Apicomplexa) involves the generation of several asexual and sexual forms of the parasite. During the stage conversions, complex mechanisms lead to differential structural and functional properties of the parasite. These require a well tuned gene transcription machinery. For the first time the gene expression of four surface proteins of C. parvum sporozoites, CP15, CP17, P23, and GP900 were analysed in parallel by reverse transcription polymerase chain reaction. In addition, CP17 and P23 antigens were detected in infected host cells by immunofluorescence using antisera raised against recombinant forms of the proteins. The results show that…

CytoplasmTime FactorsTranscription GeneticImmunologyGenes ProtozoanProtozoan ProteinsFluorescent Antibody TechniqueAntigens ProtozoanBiologyImmunofluorescenceMicrobiologyApicomplexaAntigenCell Line Tumorparasitic diseasesGene expressionmedicineAnimalsHumansRNA MessengerGeneCryptosporidium parvumMembrane Glycoproteinsmedicine.diagnostic_testReverse Transcriptase Polymerase Chain Reactionbiology.organism_classificationMolecular biologyAdaptation PhysiologicalReverse transcription polymerase chain reactionInfectious DiseasesReal-time polymerase chain reactionCryptosporidium parvumGene Expression RegulationAntigens SurfaceRNA ProtozoanMicrobes and infection
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Generation of tumor-reactive CTL against the tumor-associated antigen HER2 using retrovirally transduced dendritic cells derived from CD34+ hemopoiet…

2000

Abstract Ag-specific CD8+ CTL are crucial for effective tumor rejection. Attempts to treat human malignancies by adoptive transfer of tumor-reactive CTL have been limited due to the difficulty of generating and expanding autologous CTL with defined Ag specificity. The current study examined whether human CTL can be generated against the tumor-associated Ag HER2 using autologous dendritic cells (DC) that had been genetically engineered to express HER2. DC progenitors were expanded by culturing CD34+ hemopoietic progenitor cells in the presence of the designer cytokine HyperIL-6. Proliferating precursor cells were infected by a retroviral vector encoding the HER2 Ag and further differentiated…

Cytotoxicity ImmunologicAdoptive cell transferReceptor ErbB-2T cellRecombinant Fusion ProteinsImmunologyAntigen-Presenting CellsImmunoglobulinschemical and pharmacologic phenomenaAntigens CD34BiologyMajor histocompatibility complexLymphocyte ActivationViral vectorCell LineAntigens CDTransduction GeneticMHC class IHLA-A2 AntigenmedicineTumor Cells CulturedImmunology and AllergyHumansProgenitor cellskin and connective tissue diseasesAntigen PresentationMembrane GlycoproteinsInterleukin-6Cell DifferentiationDendritic CellsReceptors InterleukinHematopoietic Stem CellsMolecular biologyReceptors Interleukin-6Peptide FragmentsCell biologyClone CellsCTL*medicine.anatomical_structureRetroviridaebiology.proteinCD8Cell DivisionT-Lymphocytes CytotoxicJournal of immunology (Baltimore, Md. : 1950)
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