Search results for "glycoproteins"

showing 10 items of 496 documents

Identification and isolation of the primary aggregation factor from the cell membrane of the sponge Geodia cydonium

1985

The primary aggregation factor (pAF) of sponge cells is a glycoprotein that is firmly associated with the cell membrane. Polyspecific antibodies (anti-GM) prepared from sera raised against membranes of cells from the siliceous sponge Geodia cydonium were found to inhibit initial aggregation of homologous cells. The inhibition of aggregation, caused by anti-GM was neutralized by pAF. The pAF had been successfully solubilized and enriched by affinity chromatography, gel filtration and density gradient centrifugation, if checked by polyacrylamide gel electrophoresis in the presence of urea. The Mr of the native pAF was approximately 40 000 as estimated by gel filtration; under denaturing condi…

Clinical BiochemistrySize-exclusion chromatographyBiologyCell membraneSpecies SpecificityAffinity chromatographymedicineAnimalsGeodiaMolecular BiologyPolyacrylamide gel electrophoresisCell AggregationGlycoproteinschemistry.chemical_classificationDifferential centrifugationCell MembraneMembrane ProteinsLectinCell BiologyGeneral Medicinebiology.organism_classificationMolecular biologyPoriferamedicine.anatomical_structurechemistryBiochemistrybiology.proteinlipids (amino acids peptides and proteins)GlycoproteinCell Adhesion MoleculesMolecular and Cellular Biochemistry
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Proliferation state and polo-like kinase1 dependence of tumorigenic colon cancer cells.

2012

Abstract Tumor-initiating cells are responsible for tumor maintenance and relapse in solid and hematologic cancers. Although tumor-initiating cells were initially believed to be mainly quiescent, rapidly proliferating tumorigenic cells were found in breast cancer. In colon cancer, the proliferative activity of the tumorigenic population has not been defined, although it represents an essential parameter for the development of more effective therapeutic strategies. Here, we show that tumorigenic colon cancer cells can be found in a rapidly proliferating state in vitro and in vivo, both in human tumors and mouse xenografts. Inhibitors of polo-like kinase1 (Plk1), a mitotic kinase essential fo…

Colorectal cancerCancer stem cellscolorectal cancercell proliferationcell cycle.Cell Cycle ProteinsMice0302 clinical medicineMice Inbred NODAC133 AntigenRNA Small Interfering0303 health scienceseducation.field_of_studyPteridinesCell CycleCell cycleImmunohistochemistry3. Good healthMitochondriaGene Expression Regulation Neoplastic030220 oncology & carcinogenesisColonic NeoplasmsMolecular MedicineFemaleStem cellPopulationTransplantation HeterologousCell Growth ProcessesBiologyProtein Serine-Threonine KinasesPLK103 medical and health sciencesCancer stem cellAntigens CDCell Line TumorProto-Oncogene ProteinsmedicineAnimalsHumanseducationProtein Kinase Inhibitors030304 developmental biologyGlycoproteinsSettore MED/04 - Patologia GeneraleCell growthCell Biologymedicine.diseaseTumor progressionImmunologyCancer researchPeptidesDevelopmental BiologyStem cells (Dayton, Ohio)
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Strong Cooperativity and Loose Geometry between CUB Domains Are the Basis for Procollagen C-Proteinase Enhancer Activity

2009

Procollagen C-proteinase enhancers (PCPE-1 and -2) specifically activate bone morphogenetic protein-1 (BMP-1) and other members of the tolloid proteinase family during C-terminal processing of fibrillar collagen precursors. PCPEs consist of two CUB domains (CUB1 and CUB2) and one NTR domain separated by one short and one long linker. It was previously shown that PCPEs can strongly interact with procollagen molecules, but the exact mechanism by which they enhance BMP-1 activity remains largely unknown. Here, we used a series of deletion mutants of PCPE-1 and two chimeric constructs with repetitions of the same CUB domain to study the role of each domain and linker. Out of all the forms teste…

CooperativityPlasma protein bindingTransfectionBinding CompetitiveBiochemistryBone morphogenetic protein 1Bone Morphogenetic Protein 1Cell LineHumansAmino Acid SequenceBinding siteEnhancerMolecular BiologyGlycoproteinsExtracellular Matrix ProteinsBinding SitesEnzyme Catalysis and RegulationChemistryCircular DichroismCell BiologyCUB domainKineticsProcollagen peptidaseBiochemistryMutationBiophysicsElectrophoresis Polyacrylamide GelLinkerProcollagenProtein BindingJournal of Biological Chemistry
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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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Inverse relationship of melanocyte differentiation antigen expression in melanoma tissues and CD8+ cytotoxic-T-cell responses: evidence for immunosel…

1996

Antigenic peptides derived from differentiation antigens of the melanocyte lineage were recently identified in human melanomas as targets for MHC-restricted cytotoxic T lymphocytes (CTL). CTL directed against peptides derived from the Melan A/MART-1, tyrosinase and gp100/Pmel17 antigens can be detected in melanoma patients and in healthy controls. The presence of defined antigenic peptides and corresponding precursor CTL in patients with metastatic melanoma opens perspectives for the development of antigen-specific tumor vaccines. In this study, we examined the expression of Melan A/MART-1, tyrosinase and gp100lPmel17 in fresh melanoma tissues of HLA-A2+ patients and the spontaneous CTL rea…

Cytotoxicity ImmunologicCancer ResearchTyrosinaseMolecular Sequence Data10050 Institute of Pharmacology and Toxicology610 Medicine & healthchemical and pharmacologic phenomenaBiologyMelanocyteCD8-Positive T-LymphocytesEpitopesImmune systemMART-1 AntigenAntigenMelanocyte differentiationAntigens NeoplasmmedicineTumor Cells CulturedCytotoxic T cellHumans1306 Cancer ResearchAmino Acid SequenceneoplasmsMelanomaDNA PrimersImmunity CellularMembrane GlycoproteinsBase SequenceMonophenol MonooxygenaseMelanomaProteinsCell Differentiationmedicine.diseaseNeoplasm ProteinsCTL*medicine.anatomical_structureOncologyImmunology570 Life sciences; biologyMelanocytes2730 Oncologygp100 Melanoma AntigenInternational 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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A novel epitope of N-CAM defines precursors of human adherent NK cells

2004

AbstractActivated, adherent natural killer (A-NK) cells represent a distinct subpopulation of interleukin (IL)-2-stimulated NK cells, which are selectively endowed with the increased expression of integrins and ability to adhere to solid surfaces, migrate into, infiltrate, and destroy cancerous tissues. The present study defines the phenotype and functions of precursors of A-NK (pre-A-NK) cells in humans. Peripheral blood pre-A-NK cells, in contrast to the rest of NK cells, express a novel epitope of CD56 neuronal cell adhesion molecule, termed ANK-1, and increased cell-surface levels of integrins. Pre-A-NK cells also express low levels of CD56 and CD161, and some express CD162 receptor, do…

Cytotoxicity ImmunologicIntegrinsLymphoid TissueImmunologyCell CountBiologyCD49bImmunophenotypingEpitopesInterleukin 21NK-92Cell AdhesionHumansImmunology and AllergyCell LineageLectins C-TypeAntigen-presenting cellCells CulturedCell ProliferationMembrane GlycoproteinsLymphokine-activated killer cellStem CellsJanus kinase 3Cell MembraneReceptors IgGAntibodies MonoclonalCell DifferentiationCell BiologyNatural killer T cellCD56 AntigenCell biologyKiller Cells NaturalChemotaxis LeukocyteAntigens SurfaceInterleukin 12Interleukin-2NK Cell Lectin-Like Receptor Subfamily BJournal of Leukocyte Biology
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P-selectin glycoprotein ligand-1 as a potential target for humoral immunotherapy of multiple myeloma.

2008

Monoclonal antibodies (mAbs), successfully adopted in the treatment of several haematological malignancies, have proved almost ineffective in multiple myeloma (MM), because of the lack of an appropriate antigen for targeting and killing MM cells. Here, we demonstrate that PSGL1, the major ligand of P-Selectin, a marker of plasmacytic differentiation expressed at high levels on normal and neoplastic plasma cells, may represent a novel target for mAb-mediated MM immunotherapy. The primary effectors of mAb-induced cell-death, complement-mediated lysis (CDC) and antibody-dependent cell-mediated cytotoxicity (ADCC), were investigated using U266B1 and LP1 cell-lines as models. Along with immunolo…

Cytotoxicity ImmunologicMembrane Glycoproteinsmieloma multiplo; ab therapy; PSGL-1ab therapyAntibody-Dependent Cell CytotoxicityDrug Evaluation PreclinicalAntibodies MonoclonalBone Marrow CellsSettore MED/08 - Anatomia Patologicamultiple myelomaDrug Delivery SystemsCell Line TumorHumanscomplementimmunotherapymieloma multiploPSGL-1ADCCComplement Activationmonoclonal antibodie
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