Search results for " Biosynthesis"

showing 10 items of 317 documents

Transfection analysis of expression of mRNA isoforms encoding the nuclear autoantigen La/SS-B

1997

Transcription of the gene encoding for the nuclear autoantigen La resulted in La mRNA isoforms. A promoter switching combined with an alternative splicing pathway replaced the exon 1 with the exon 1'. The exon 1' contained GC-rich regions and an oligo(U) tail of 23 uridine residues. Moreover, it encoded for three open reading frames upstream of the La protein reading frame. Despite this unusual structure, when exon 1' La mRNAs were expressed in transfected cells, both exon 1 and 1' La mRNAs were translated to La protein, whereas the upstream open reading frames of the exon 1' were not translated. In addition to full-length exon 1' La mRNAs 5'-shortened exon 1' La mRNAs were detected. The ex…

GuanineTranscription GeneticBiologyTransfectionAutoantigensPolymerase Chain ReactionBiochemistryCell LineCytosineMiceOpen Reading FramesExonExon trappingTranscription (biology)AnimalsHumansRNA MessengerMolecular BiologyGeneDNA PrimersBase CompositionMessenger RNAAlternative splicingExonsCell BiologyTransfectionMolecular biologyAlternative SplicingOpen reading frameRibonucleoproteinsProtein BiosynthesisTranscription Factors
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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
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Sequence-Specific Repression of Cotranslational Translocation of the Hepatitis B Virus Envelope Proteins Coincides with Binding of Heat Shock Protein…

1997

AbstractThe large L envelope protein of the hepatitis B virus has the peculiar capacity to adopt two transmembrane topologies. The N-terminal preS domain of L initially remains in the cytosol while the S domain is cotranslationally inserted into the endoplasmic reticulum membrane. The preS region of about half of the L molecules is posttranslationally translocated to the lumenal space. We now demonstrate that the repression of cotranslational translocation of preS is conferred by a preS1-specific sequence. By analysis of L deletion mutants, the cytosolic anchorage determinant was mapped to amino acid sequence 70 to 94 of L. The intrinsic potential of this determinant to suppress cotranslati…

Hepatitis B virusHSC70 Heat-Shock ProteinsRecombinant Fusion ProteinsPlasma protein bindingBiologyGenes envCytosolViral Envelope ProteinsHeat shock proteinVirologyHumansHSP70 Heat-Shock ProteinsBinding sitePromoter Regions GeneticPeptide sequenceBinding SitesBase SequenceCell-Free SystemEndoplasmic reticulumHSC70 Heat-Shock ProteinsOligonucleotides AntisenseMolecular biologyTransmembrane proteinChaperone (protein)Protein Biosynthesisbiology.proteinMutagenesis Site-DirectedMetallothioneinCarrier ProteinsProtein BindingVirology
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Chaperones Involved in Hepatitis B Virus Morphogenesis

1999

Little is known about host cell factors necessary for hepatitis B virus (HBV) assembly which involves envelopment of cytosolic nucleocapsids by the S, M and L transmembrane viral envelope proteins and subsequent budding into intraluminal cisternae. Central to virogenesis is the L protein that mediates hepatocyte receptor binding and envelopment of capsids. To serve these topologically conflicting roles, L protein exhibits an unusual dual membrane topology, disposing its N-terminal preS domain inside and outside of the virion lipid envelope. The mixed topology is achieved by posttranslational preS translocation of about half of the L protein molecules across a post-endoplasmic reticulum memb…

Hepatitis B virusProtein FoldingCalnexinHSC70 Heat-Shock ProteinsClinical BiochemistryBiochemistryViral Matrix ProteinsCytosolViral Envelope ProteinsViral envelopeCalnexinMorphogenesisAnimalsHumansHSP70 Heat-Shock ProteinsProtein PrecursorsMolecular BiologyHepatitis B Surface AntigensViral matrix proteinbiologyChemistryCalcium-Binding ProteinsHSC70 Heat-Shock ProteinsBiological TransportVirologyTransmembrane proteinCell biologyProtein BiosynthesisMembrane topologyChaperone (protein)COS Cellsbiology.proteinProtein foldingCarrier ProteinsMolecular ChaperonesBiological Chemistry
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Mammalian BiP controls posttranslational ER translocation of the hepatitis B virus large envelope protein.

2008

AbstractThe hepatitis B virus L protein forms a dual topology in the endoplasmic reticulum (ER) via a process involving cotranslational membrane integration and subsequent posttranslational translocation of its preS subdomain. Here, we show that preS posttranslocation depends on the action of the ER chaperone BiP. To modulate the in vivo BiP activity, we designed an approach based on overexpressing its positive and negative regulators, ER-localized DnaJ-domain containing protein 4 (ERdj4) and BiP-associated protein (BAP), respectively. The feasibility of this approach was confirmed by demonstrating that BAP, but not ERdj4, destabilizes the L/BiP complex. Overexpressing BAP or ERdj4 inhibits…

Hepatitis B virusgenetic structuresBiPBiophysicsHemagglutinin (influenza)Chromosomal translocationmacromolecular substancesmedicine.disease_causeEndoplasmic ReticulumBiochemistryCell LineAdenosine TriphosphateViral Envelope ProteinsStructural BiologyIn vivoCalnexinHBVGeneticsmedicineHumansMolecular BiologyEndoplasmic Reticulum Chaperone BiPTranslocational regulationHeat-Shock ProteinsHepatitis B virusbiologyEndoplasmic reticulumMembrane ProteinsCell BiologyHSP40 Heat-Shock ProteinsMolecular biologyProtein Structure TertiaryProtein TransportDual topologyMembrane topologyProtein BiosynthesisMembrane topologybiology.proteinPosttranslational translocationMolecular ChaperonesFEBS letters
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Sequences in the 5′ Nontranslated Region of Hepatitis C Virus Required for RNA Replication

2001

ABSTRACT Sequences in the 5′ and 3′ termini of plus-strand RNA viruses harbor cis -acting elements important for efficient translation and replication. In case of the hepatitis C virus (HCV), a plus-strand RNA virus of the family Flaviviridae , a 341-nucleotide-long nontranslated region (NTR) is located at the 5′ end of the genome. This sequence contains an internal ribosome entry site (IRES) that is located downstream of an about 40-nucleotide-long sequence of unknown function. By using our recently developed HCV replicon system, we mapped and characterized the sequences in the 5′ NTR required for RNA replication. We show that deletions introduced into the 5′ terminal 40 nucleotides abolis…

Hepatitis C virusImmunologyRNA-dependent RNA polymeraseReplicationHepacivirusmedicine.disease_causeOrigin of replicationMicrobiologyVirologymedicineTumor Cells CulturedHumansRepliconGeneticsbiologyRNARNA virusbiology.organism_classificationVirologyNS2-3 proteaseInternal ribosome entry siteInsect ScienceProtein BiosynthesisRNA ViralReplicon5' Untranslated Regions
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Activation of oligodendroglial Fyn kinase enhances translation of mRNAs transported in hnRNP A2-dependent RNA granules.

2008

Central nervous system myelination requires the synthesis of large amounts of myelin basic protein (MBP) at the axon–glia contact site. MBP messenger RNA (mRNA) is transported in RNA granules to oligodendroglial processes in a translationally silenced state. This process is regulated by the trans-acting factor heterogeneous nuclear ribonucleoprotein (hnRNP) A2 binding to the cis-acting A2 response element (A2RE). Release of this repression of MBP mRNA translation is thus essential for myelination. Mice deficient in the Src family tyrosine kinase Fyn are hypomyelinated and contain reduced levels of MBP. Here, we identify hnRNP A2 as a target of activated Fyn in oligodendrocytes. We show that…

Heterogeneous nuclear ribonucleoproteinCell Adhesion Molecules NeuronalRecombinant Fusion ProteinsBiologyHeterogeneous ribonucleoprotein particleCytoplasmic GranulesProto-Oncogene Proteins c-fynResponse Elementsenvironment and public healthRNA TransportCell LineMiceFYNContactinsGenes ReporterReportHeterogeneous-Nuclear Ribonucleoprotein Group A-BProtein biosynthesisAnimalsRNA MessengerPhosphorylationLuciferasesNeural Cell Adhesion MoleculesResearch ArticlesMessenger RNARNATranslation (biology)Cell BiologyMolecular biologyMyelin basic proteinEnzyme ActivationOligodendroglianervous systemProtein Biosynthesisbiology.proteinProtein BindingThe Journal of cell biology
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Heterogeneous nuclear ribonucleoprotein (hnRNP) F is a novel component of oligodendroglial RNA transport granules contributing to regulation of myeli…

2011

Myelin basic protein (MBP) is a major component of central nervous system (CNS) myelin. The absence of MBP results in the loss of almost all compact myelin in the CNS. MBP mRNA is sorted into RNA granules that are transported to the periphery of oligodendrocytes in a translationally inactive state. A central mediator of this transport process is the trans-acting factor heterogeneous nuclear ribonucleoprotein (hnRNP) A2 that binds to the cis-acting A2-response element in the 3′UTR of MBP mRNA. Recently, we found that activation of the Src family nonreceptor tyrosine kinase Fyn in oligodendrocytes leads to phosphorylation of hnRNP A2 and to increased translation of MBP mRNA. Here, we identify…

Heterogeneous nuclear ribonucleoproteinRNA-binding proteinBiologyCytoplasmic GranulesProto-Oncogene Proteins c-fynBiochemistryenvironment and public healthMiceFYNNeurobiologyCompact myelinHeterogeneous-Nuclear Ribonucleoprotein Group A-BProtein biosynthesismedicineMRNA transportAnimalsHumansMolecular Biology3' Untranslated RegionsCells CulturedMyelin SheathHeterogeneous-Nuclear Ribonucleoprotein Group F-Hhemic and immune systemsBiological TransportMyelin Basic ProteinCell BiologyMolecular biologyOligodendrocyteMyelin basic proteinOligodendrogliamedicine.anatomical_structurenervous systemGene Expression Regulationembryonic structuresbiology.proteinbiological phenomena cell phenomena and immunityThe Journal of biological chemistry
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Human histidine-rich glycoprotein expressed in SF9 insect cells inhibits apatite formation

1997

Histidine-rich glycoprotein (HRG) is structurally related to the alpha2-HS glycoprotein/fetuin family of mammalian plasma proteins; both belong to the cystatin superfamily of proteins. We expressed recombinant human HRG and alpha2-HS in Sf9 insect cells for functional analysis. Recombinant HRG bound heparin and fibrinogen while alpha2-HS did not. Both proteins inhibited the formation of apatite, recombinant HRG (IC50 approximately 1 microM) with 2-fold lower molar activity than alpha2-HS (IC50 approximately 0.5 microM). The inhibition in vitro of apatite formation suggests a new function for plasma HRG protein, inhibition of phase separation in blood vessels.

Histidine-rich glycoproteinHistidine-rich glycoproteinalpha-2-HS-GlycoproteinBiophysicsSerum proteinSf9SpodopteraFibrinogenBiochemistryα2-HS-glycoproteinBone and BonesCell Linelaw.inventionStructural BiologylawApatitesCalcium homeostasisGeneticsmedicineAnimalsHumansMolecular Biologychemistry.chemical_classificationHeparinChemistryProteinsBlood ProteinsCell BiologyFetuinBlood proteinsRecombinant ProteinsIn vitroBiochemistryProtein BiosynthesisRecombinant DNAGlycoproteinProtein Bindingmedicine.drugFEBS Letters
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Arylpyridines, arylpyrimidines and related compounds as potential modulator agents of the VEGF, hTERT and c-Myc oncogenes.

2019

Twenty-four derivatives structurally related to honokiol have been synthesized and biologically evaluated. IC50 values were determined towards the HT-29, MCF-7 and HEK-293 cell lines. Some of these derivatives exhibited comparable or lower IC50 values than honokiol towards the HT-29 and MCF-7 cell lines or else higher selectivity indexes than the natural product. Twelve selected derivatives were evaluated for their ability to inhibit the expression of the VEGFA, hTERT and c-Myc genes and also to inhibit the production of total c-Myc protein and the secretion of the VEGF protein. One of the most promising compounds, 3-(2,4-dimethoxyphenyl)pyridine, may be a good candidate for further studies…

Honokiolantiproliferative activityVascular Endothelial Growth Factor APyridinesClinical Biochemistryaza and diazabiphenyl derivativesPharmaceutical ScienceDown-RegulationGene ExpressionAntineoplastic Agents01 natural sciencesBiochemistrygene targetingProto-Oncogene Proteins c-mycchemistry.chemical_compoundanticancer agentsCell Line TumorDrug DiscoveryGene expressionHumansSecretionTelomerase reverse transcriptaseMolecular BiologyTelomeraseCell ProliferationNatural product010405 organic chemistryOrganic ChemistryGene targeting0104 chemical sciences010404 medicinal & biomolecular chemistryVascular endothelial growth factor AHEK293 CellsPyrimidineschemistryCell cultureProtein BiosynthesisCancer researchMolecular MedicineBioorganicmedicinal chemistry
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