Search results for "Precursors"

showing 10 items of 151 documents

Urokinase Plasminogen Activator and Gelatinases Are Associated with Membrane Vesicles Shed by Human HT1080 Fibrosarcoma Cells

1997

Membrane vesicles are shed by tumor cells both in vivo and in vitro. Although their functions are not well understood, it has been proposed that they may play multiple roles in tumor progression. We characterized membrane vesicles from human HT1080 fibrosarcoma cell cultures for the presence of proteinases involved in tumor invasion. By gelatin zymography and Western blotting, these vesicles showed major bands corresponding to the zymogen and active forms of gelatinase B (MMP-9) and gelatinase A (MMP-2) and to the MMP-9. tissue inhibitor of metalloproteinase 1 complex. Both gelatinases appeared to be associated with the vesicle membrane. HT1080 cell vesicles also showed a strong, plasminoge…

GelatinasesMacromolecular SubstancesFibrosarcomaBlotting WesternCellGelatinase ABiologyBiochemistryTumor Cells CulturedmedicineHumansCollagenasesFibrinolysinMolecular BiologyGlycoproteinsUrokinaseEnzyme PrecursorsVesicleMetalloendopeptidasesTissue Inhibitor of MetalloproteinasesCell BiologyTissue inhibitor of metalloproteinaseUrokinase-Type Plasminogen ActivatorMolecular biologyExtracellular MatrixUrokinase receptorBloodmedicine.anatomical_structureMatrix Metalloproteinase 9GelatinasesMatrix Metalloproteinase 2HT1080medicine.drugJournal of Biological Chemistry
researchProduct

NAIP-deltaEx10-11: a novel splice variant of the apoptosis inhibitor NAIP differently expressed in drug-sensitive and multidrug-resistant HL60 leukem…

2002

Alterations of neuronal apoptosis inhibitory protein (NAIP), a member of the inhibitory of apoptosis protein (IAP) family of inhibitors of apoptosis, have been previously associated with different neurodegenerative disorders. This study indicated the existence of a novel NAIP splice variant. This isoform, NAIP-deltaEx10-11, was found in tumor cell lines of different origin and in normal adult brain. Analysis of the putative protein predicted that the NAIP variant lacks part of the third BIR domain as well as the COOH-terminal tail of regular NAIP. This might suggest that it is endowed with a reduced antiapoptotic activity. This view is supported by the fact that NAIP-deltaEx10-11 mRNA and p…

Gene isoformCancer ResearchApoptosis InhibitorHL60ApoptosisHL-60 CellsNerve Tissue ProteinsBiologyExonchemistry.chemical_compoundmedicineRNA PrecursorsTumor Cells CulturedHumansProtein IsoformsRNA NeoplasmSequence DeletionGeneticsBrain ChemistryAlternative splicingHematologyExonsmedicine.diseaseDrug Resistance MultipleNeuronal Apoptosis-Inhibitory ProteinNeoplasm ProteinsProtein Structure TertiaryLeukemiaAlternative SplicingOncologychemistryApoptosisDrug Resistance NeoplasmCancer researchNAIPLeukemia research
researchProduct

Dysbiosis and zonulin upregulation alter gut epithelial and vascular barriers in patients with ankylosing spondylitis

2017

BackgroundDysbiosis has been recently demonstrated in patients with ankylosing spondylitis (AS) but its implications in the modulation of intestinal immune responses have never been studied. The aim of this study was to investigate the role of ileal bacteria in modulating local and systemic immune responses in AS.MethodsIleal biopsies were obtained from 50 HLA-B27+ patients with AS and 20 normal subjects. Silver stain was used to visualise bacteria. Ileal expression of tight and adherens junction proteins was investigated by TaqMan real-time (RT)-PCR and immunohistochemistry. Serum levels of lipopolysaccharide (LPS), LPS-binding protein (LPS-BP), intestinal fatty acid-BP (iFABP) and zonulin…

Genetics and Molecular Biology (all)Fatty Acid-Binding ProteinAnkylosing SpondylitisMonocyteBiochemistryMonocytesTransgenic0302 clinical medicineIntestinal MucosaMembrane GlycoproteinsZonulinCadherinsAdherens JunctionUp-RegulationAntigenAcute DiseaseMembrane GlycoproteinRats TransgenicInfectionHumanAnkylosingImmunologyGeneral Biochemistry Genetics and Molecular BiologyArticlePermeabilityTight Junctions03 medical and health sciencesRheumatologyAntigens CDIleumAnti-Bacterial AgentHuman Umbilical Vein Endothelial CellsHumansRNA MessengerEndotheliumProtein PrecursorsAnkylosing SpondylitiBiochemistry Genetics and Molecular Biology (all)BacteriaAnimalmedicine.diseaseDysbiosiSettore MED/16 - Reumatologia030104 developmental biologychemistryCase-Control StudiesImmunologyRatCarrier ProteinsAcute-Phase ProteinsSpondylitis0301 basic medicineLipopolysaccharidesLipopolysaccharideMessengerAcute-Phase ProteinGene Expressionchemistry.chemical_compoundIntestinal mucosaImmunology and AllergyMembrane ProteinHLA-B27 AntigenCaco-2 CellTight junctionTight JunctionAdherens JunctionsIleitisIleitiAnti-Bacterial AgentsCDmedicine.anatomical_structureAnkylosing Spondylitis; Infections; Inflammation; Acute Disease; Acute-Phase Proteins; Adherens Junctions; Animals; Anti-Bacterial Agents; Antigens CD; Bacteria; Caco-2 Cells; Cadherins; Carrier Proteins; Case-Control Studies; Cholera Toxin; Chronic Disease; Dysbiosis; Endothelium; Fatty Acid-Binding Proteins; Gene Expression; HLA-B27 Antigen; Human Umbilical Vein Endothelial Cells; Humans; Ileitis; Ileum; Interleukin-8; Intestinal Mucosa; Junctional Adhesion Molecule A; Lipopolysaccharides; Membrane Glycoproteins; Membrane Proteins; Monocytes; Permeability; RNA Messenger; Rats; Rats Transgenic; Spondylitis Ankylosing; Tight Junctions; Up-Regulationmedicine.symptomCase-Control StudieCholera ToxinHuman Umbilical Vein Endothelial CellLipopolysaccharideInflammationInfectionsFatty Acid-Binding ProteinsAdherens junctionmedicineAnkylosing Spondylitis; Infections; Inflammation; Acute Disease; Acute-Phase Proteins; Adherens Junctions; Animals; Anti-Bacterial Agents; Antigens CD; Bacteria; Caco-2 Cells; Cadherins; Carrier Proteins; Case-Control Studies; Cholera Toxin; Chronic Disease; Dysbiosis; Endothelium; Fatty Acid-Binding Proteins; Gene Expression; HLA-B27 Antigen; Human Umbilical Vein Endothelial Cells; Humans; Ileitis; Ileum; Interleukin-8; Intestinal Mucosa; Junctional Adhesion Molecule A; Lipopolysaccharides; Membrane Glycoproteins; Membrane Proteins; Monocytes; Permeability; RNA Messenger; Rats; Rats Transgenic; Spondylitis Ankylosing; Tight Junctions; Up-Regulation; Immunology and Allergy; Rheumatology; Immunology; Biochemistry Genetics and Molecular Biology (all)AnimalsSpondylitis AnkylosingAntigensSpondyliti030203 arthritis & rheumatologyInflammationHaptoglobinsbusiness.industryMonocyteInterleukin-8Membrane ProteinsRatsJunctional Adhesion Molecule AChronic DiseaseCadherinDysbiosisRNACaco-2 CellsCarrier ProteinbusinessDysbiosis
researchProduct

Alterations of pre-mRNA splicing in cancer

2005

Recent genomewide analyses of alternative splicing (AS) indicate that up to 70% of human genes may have alternative splice forms, suggesting that AS together with various posttranslational modifications plays a major role in the production of proteome complexity. Splice-site selection under normal physiological conditions is regulated in the developmental stage in a tissue type-specific manner by changing the concentrations and the activity of splicing regulatory proteins. Whereas spliceosomal errors resulting in the production of aberrant transcripts rarely occur in normal cells, they seem to be an intrinsic property of cancer cells. Changes in splice-site selection have been observed in v…

GeneticsCancer ResearchRNA SplicingAlternative splicingExonic splicing enhancerIntronExonsBiologymedicine.disease_causeIntronsCell biologyExonTumor progressionRNA splicingRNA PrecursorsGeneticsmedicineHumansspliceCarcinogenesisGenes, Chromosomes and Cancer
researchProduct

Translation of hepatitis B virus (HBV) surface proteins from the HBV pregenome and precore RNAs in Semliki Forest virus-driven expression.

2004

Hepatitis B virus (HBV) pregenome RNA (pgRNA) serves as a translation template for the HBV core (HBc) protein and viral polymerase (Pol). HBV precore RNA (pcRNA) directs the synthesis of the precore (preC) protein, a precursor of the hepatitis B e antigen (HBeAg). pgRNA and pcRNA were expressed in the Semliki Forest virus (SFV) expression system. Besides the HBc and preC proteins, there was revealed the synthesis of all three forms of HBV surface (HBs) proteins: long (LHBs), middle (MHBs) and short (SHBs), the start codons of which are located more than 1000 nt downstream of the HBc and preC start codons. Moreover, other HBV templates, such as 3′-truncated pgRNA lacking 3′ direct repeat and…

HBV RNA encapsidation signal epsilonHepatitis B virusvirusesGene ExpressionLeaky scanningDNA-Directed DNA Polymerasemedicine.disease_causeSemliki Forest virusVirus ReplicationCell LineViral Envelope ProteinsVirologymedicineAnimalsHepatitis B e AntigensRNA MessengerCloning MolecularProtein PrecursorsHepatitis B virusHepatitis B Surface Antigensbiologyvirus diseasesRNA virusTemplates Geneticbiology.organism_classificationVirologyMolecular biologyHepatitis B Core AntigensImmunohistochemistrySemliki forest virusdigestive system diseasesGenetic translationHBeAgHepadnaviridaeProtein BiosynthesisRNA ViralThe Journal of general virology
researchProduct

Hepatic expression patterns of the large and middle hepatitis B virus surface proteins in viremic and nonviremic chronic hepatitis B.

1990

The envelope of hepatitis B virus consists of large, middle, and small hepatitis B surface proteins. Recent data from in vitro studies suggest that intracellular expression and distribution of the three polypeptides may be variable. These observations in artificial expression systems prompted this analysis of the occurrence and distribution of the three hepatitis B surface proteins in the liver tissue of substantial viremic (hepatitis B virus DNA- and hepatitis B e antigen-positive) and low-viremic or nonviremic (hepatitis B virus DNA-negative, anti-hepatitis B e antigen-positive) carriers by specific monoclonal antibodies against large, middle, and small proteins. Patients with an active f…

HBsAgHepatitis B virusHepatitis B virus DNA polymerasemedicine.disease_causeHepatitis B virus PRE betaImmunoenzyme Techniques03 medical and health sciences0302 clinical medicineViral Envelope ProteinsmedicineHumansViremiaProtein Precursors030304 developmental biologyHepatitis ChronicHepatitisHepatitis B virus0303 health sciencesHepatitis B Surface AntigensHepatologybiologyGastroenterologyAntibodies MonoclonalHepatitis Bmedicine.diseasebiology.organism_classificationHepatitis BVirologyMolecular biology3. Good healthHBeAgHepadnaviridaeLiverDNA Viral030211 gastroenterology & hepatologyGastroenterology
researchProduct

Fine-mapping of the B-cell epitope domain at the N-terminus of the preS2 region of the hepatitis B surface antigen

2002

In this study, we report the exact localization and substitutional characterization of a B-cell epitope domain at the N-terminus of the preS2 region of the hepatitis B surface antigen. A set of deletion variants containing preS2 sequences of different length was generated on the basis of frCP as a carrier. It was found after Western blot analysis that three monoclonal antibodies (MAbs) (2-11B1, 3-11C2, HB.OT10) recognized the linear preS2 sequence within the amino acid (aa) stretch 3-WNSTTFHQTLQDP-13. The importance of each aa residue of the epitope was proved by comparison of antibody binding to alanine-substituted peptides in both free-peptide and Pepscan variants.

HBsAgmedicine.drug_classBlotting WesternMolecular Sequence DataImmunologyMonoclonal antibodyEpitopeMiceViral Envelope ProteinsmedicineAnimalsImmunology and AllergyAmino Acid SequenceProtein PrecursorsPeptide sequenceHepatitis B Surface AntigensLinear epitopebiologyAntibodies MonoclonalMolecular biologyEpitope mappingPepscanbiology.proteinEpitopes B-LymphocyteAntibodyEpitope MappingJournal of Immunological Methods
researchProduct

Behavior of a Short preS1 Epitope on the Surface of Hepatitis B Core Particles

1999

The major immunodominant region of hepatitis B core particles is widely recognized as the most prospective target for the insertion of foreign epitopes, ensuring their maximal antigenicity and immunogenicity. This region was mapped around amino acid residues 79-81, which were shown by electron cryo-microscopy to be located on the tips of the spikes protruding from the surface of hepatitis B core shells. Here we tried to expose a model sequence, the short immunodominant hepatitis B preS1 epitope 31-DPAFR-35, onto the tip of the spike, with simultaneous deletion of varying stretches from the major immunodominant region of the HBc molecule. Accessibility to the monoclonal anti-preS1 antibody M…

Hepatitis B virusAntigenicityRecombinant Fusion ProteinsGenetic VectorsMolecular Sequence DataClinical BiochemistryAntigen presentationmedicine.disease_causeBiochemistryEpitopeMicemedicineAnimalsHumansAmino Acid SequenceProtein PrecursorsMolecular BiologyPeptide sequenceHepatitis B virusAntigen PresentationMice Inbred BALB CHepatitis B Surface AntigensbiologyImmunodominant EpitopesChemistryImmunogenicityHepatitis B Core AntigensVirologyPolyclonal antibodiesbiology.proteinEpitopes B-LymphocyteFemaleRabbitsAntibodyPlasmidsBiological Chemistry
researchProduct

Mosaic hepatitis B virus core particles presenting the complete preS sequence of the viral envelope on their surface

2004

The sequence of the preS domain of the hepatitis B virus (HBV, genotype D) envelope was inserted into the major immunodominant region (MIR) of the C-terminally truncated HBV core (HBc) protein. In Escherichia coli, the HBc–preS fusion protein was partially soluble and did not produce particles. Co-expression of the wild-type HBc as a helper protein along with the fusion protein led to the formation of mosaic HBc particles that exhibited HBc, preS1 and preS2 antigenicity. Two alternative combinations of medium- and high-copy plasmids were used for co-expression of fusion and helper proteins, in an attempt to improve mosaic particle production. However, the preS fusion content of the particle…

Hepatitis B virusAntigenicityvirusesAntibodies ViralProtein Engineeringmedicine.disease_causeVirusMiceViral Envelope ProteinsOrthohepadnavirusViral envelopeVirologyEscherichia colimedicineAnimalsProtein PrecursorsHepatitis B virusHepatitis B Surface AntigensbiologyViral Core Proteinsvirus diseasesProtein engineeringHepatitis Bbiology.organism_classificationVirologyFusion proteindigestive system diseasesHepadnaviridaeFemaleImmunizationReassortant VirusesPlasmidsJournal of General Virology
researchProduct

N-terminal myristoylation-dependent masking of neutralizing epitopes in the preS1 attachment site of hepatitis B virus

2011

The N-terminally myristoylated preS1 domain of the large hepatitis B surface protein (LHBs) mediates specific attachment of hepatitis B virus (HBV) to hepatocytes. Its B-cell epitopes leading to neutralization of infectivity are not yet characterized.We inserted C- and N-terminal preS1 peptides into the most immunogenic region of HBV core particles, therewith immunized Balb/c mice and determined binding properties and neutralization potential of resulting antibodies in vitro.The particles with preS1 inserts were highly immunogenic and the corresponding anti-preS antibodies strongly bound to HBV particles from chronic carriers infected with different HBV genotypes A-F. However, antibodies bi…

Hepatitis B virusHBsAgGenotypeMolecular Sequence DataIn Vitro TechniquesBiologymedicine.disease_causeMyristic AcidNeutralizationEpitopeMice03 medical and health sciencesHepatitis B Chronic0302 clinical medicinemedicineAnimalsHumansHepatitis B VaccinesAmino Acid SequenceHepatitis B AntibodiesProtein Precursors030304 developmental biologyHepatitis B virusInfectivityMice Inbred BALB C0303 health sciencesBinding SitesHepatitis B Surface AntigensSequence Homology Amino AcidHepatologyHepatitis Bmedicine.diseaseAntibodies NeutralizingVirology3. Good healthEpitope mappingbiology.proteinEpitopes B-Lymphocyte030211 gastroenterology & hepatologyAntibodyEpitope MappingJournal of Hepatology
researchProduct