Search results for "complex mixtures"

showing 5 items of 825 documents

Heat Shock Protein 60 in Hepatocellular Carcinoma: Insights and Perspectives

2020

Heat shock protein 60 (HSP60) is a mitochondrial chaperone that is implicated in physiological and pathological processes. For instance, it contributes to protein folding and stability, translocation of mitochondrial proteins, and apoptosis. Variations in the expression levels of HSP60 have been correlated to various diseases and cancers, including hepatocellular carcinoma (HCC). Unlike other HSPs which clearly increase in some cancers, data about HSP60 levels in HCC are controversial and difficult to interpret. In the current review, we summarize and simplify the current knowledge about the role of HSP60 in HCC. In addition, we highlight the possibility of its targeting, using chemical com…

therapeutic resistancechaperoninanimal structureslcsh:Biology (General)fungiheat shock proteinscancer therapychaperoneschemical and pharmacologic phenomenahepatocellular carcinomacomplex mixtureslcsh:QH301-705.5digestive system diseasesFrontiers in Molecular Biosciences
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Binding and internalization of human papillomavirus type 33 virus-like particles by eukaryotic cells

1995

Infection of cells by human papillomaviruses (HPVs) associated with malignant genital lesions has not been studied because of the lack of an in vitro system and the unavailability of virions. We have now used virus-like particles (VLPs) of HPV type 33 to analyze the initial events in the interaction of the HPV capsid with cell lines. Binding of VLPs to HeLa cells was observed in biochemical assays and by immunofluorescence. VLP binding was inhibited by antisera raised against VLPs but not by monoclonal antibodies recognizing either L1 or L2 epitopes accessible on VLPs. Under saturating conditions, approximately 2 x 10(4) VLPs were bound per cell, with a dissociation constant of about 100 pM…

virusesImmunoelectron microscopyImmunologyBiologyAntibodies ViralMembrane Fusioncomplex mixturesMicrobiologyVirusEpitopeCell LineMiceVirologyAnimalsHumansMicroscopy ImmunoelectronPapillomaviridaeCapsomereVirionMembrane Proteinsvirus diseasesLipid bilayer fusionbiochemical phenomena metabolism and nutritionMolecular biologyEndocytosisEndocytic vesicleCapsidCell cultureInsect ScienceResearch ArticleJournal of Virology
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Generation and neutralization of pseudovirions of human papillomavirus type 33

1997

Since human papillomaviruses (HPV) cannot be propagated in cell culture, the generation of infectious virions in vitro is a highly desirable goal. Here we report that pseudovirions can be generated by the assembly of virus-like particles (VLPs) in COS-7 cells containing multiple copies of a marker plasmid. Using recombinant vaccinia viruses, we have obtained spherical VLPs of HPV type 33 (HPV-33) which fractionate into heavy and light VLPs in cesium chloride density gradients. VLPs in the heavy fraction (1.31 g/cm3) carry the plasmid in DNase-resistant form and are capable of transferring the genetic marker located on the plasmid to COS-7 cells in a DNase-resistant way (pseudoinfection). Th…

virusesImmunologyBiologyAntibodies Viralcomplex mixturesMicrobiologyNeutralizationlaw.inventionchemistry.chemical_compoundCapsidPlasmidNeutralization TestslawVirologyAnimalsDeoxyribonuclease IHumansAntigens ViralPapillomaviridaeAntiserumVirus AssemblyVirionvirus diseasesOncogene Proteins ViralVirologyMolecular biologyIn vitroTiterchemistryCapsidInsect ScienceCOS CellsDNA ViralRecombinant DNACapsid ProteinsDNAResearch ArticleJournal of Virology
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Papillomavirus assembly requires trimerization of the major capsid protein by disulfides between two highly conserved cysteines.

1998

ABSTRACT We have used viruslike particles (VLPs) of human papillomaviruses to study the structure and assembly of the viral capsid. We demonstrate that mutation of either of two highly conserved cysteines of the major capsid protein L1 to serine completely prevents the assembly of VLPs but not of capsomers, whereas mutation of all other cysteines leaves VLP assembly unaffected. These two cysteines form intercapsomeric disulfides yielding an L1 trimer. Trimerization comprises about half of the L1 molecules in VLPs but all L1 molecules in complete virions. We suggest that trimerization of L1 is indispensable for the stabilization of intercapsomeric contacts in papillomavirus capsids.

virusesImmunologyTrimerBiologymedicine.disease_causeMicrobiologycomplex mixturesSerineCapsidVirologyAnimal VirusesmedicineCysteineDisulfidesPapillomaviridaeMutationVirus AssemblyCapsomereVirionvirus diseasesbiochemical phenomena metabolism and nutritionMolecular biologyCapsidInsect ScienceMutationBiophysicsCysteineJournal of virology
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α-Conotoxins EpI and AuIB switch subtype selectivity and activity in native versus recombinant nicotinic acetylcholine receptors

2003

The Xenopus laevis oocyte expression system was used to determine the activities of alpha-conotoxins EpI and the ribbon isomer of AuIB, on defined nicotinic acetylcholine receptors (nAChRs). In contrast to previous findings on intracardiac ganglion neurones, alpha-EpI showed no significant activity on oocyte-expressed alpha3beta4 and alpha3beta2 nAChRs but blocked the alpha7 nAChR with an IC50 value of 30 nM. A similar IC50 value (103 nM) was obtained on the alpha7/5HT3 chimeric receptor stably expressed in mammalian cells. Ribbon AuIB maintained its selectivity on oocyte-expressed alpha3beta4 receptors but unlike in native cells, where it was 10-fold more potent than native alpha-AuIB, had…

α7 nicotinic acetylcholine receptorα-Conotoxin AuIBRecombinant Fusion ProteinsBiophysicsXenopusNicotinic AntagonistsReceptors NicotinicPharmacologyTransfectionBiochemistrycomplex mixturesSubstrate SpecificityInhibitory Concentration 50Xenopus laevisStructural BiologyGeneticsmedicineAnimalsConotoxinNicotinic AntagonistReceptorMolecular BiologyAcetylcholine receptorbiologyα-Conotoxin EpICell Biologybiology.organism_classificationRatsCell biologyProtein SubunitsNicotinic acetylcholine receptorNicotinic agonistnervous systemIntracardiac gangliaOocytessense organsReceptors Serotonin 5-HT3ConotoxinsAcetylcholineXenopus laevis oocytemedicine.drugFEBS Letters
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