APICAL SECRETION OF HEPATITIS-B SURFACE-ANTIGEN FROM TRANSFECTED MADIN-DARBY CANINE KIDNEY-CELLS

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dc.contributor.authorGONZALEZ, A
dc.contributor.authorNICOVANI, S
dc.contributor.authorJUICA, F
dc.date.accessioned2024-01-10T12:04:16Z
dc.date.available2024-01-10T12:04:16Z
dc.date.issued1993
dc.description.abstractHepatitis B surface antigen (HBsAg), the major envelope component of human hepatitis B virus, during infection drives the assembly and basolateral secretion from hepatocytes of both virions and subviral lipoprotein particles into the bloodstream. We studied the sorting behavior of HBsAg in the heterologous epithelial Madin-Darby canine kidney cells permanently transformed with the hepatitis B virus S gene. These cells, forming tightly packed monolayers in permeable supports, secreted HBsAg apically through a mechanism not involving transcytosis. This suggests that molecular features acting as apical addressing information, seemingly unfunctional or less efficiently used by the exocytic machinery of hepatocytes, could be contained in short hydrophilic regions of HBsAg. Lipids also could play a role in this asymmetric sorting because HBsAg is known to be secreted by forming macromolecular lipoprotein complexes rather than as a soluble protein. Together with available data, our results would imply not only the existence of tissue-specific variations in handling constitutively secreted proteins but also that these variations are strikingly dependent on the kind of protein examined. On the other hand, pulse-chase experiments with tunicamycin showed that the expression of apical information in HBsAg particles does not require N-linked glycosylation, contrasting with the known gp80 Madin-Darby canine kidney-endogenous apical secretory marker. This is the first experimental evidence that carbohydrate moieties in secretory proteins do not hold domain-specific sorting signals, a fact previously shown exclusively for membrane proteins. Thus, HBsAg provides a novel model system for the analysis of the molecular mechanisms of constitutive apical secretion.
dc.fechaingreso.objetodigital2024-05-02
dc.format.extent6 páginas
dc.fuente.origenWOS
dc.identifier.eissn1083-351X
dc.identifier.issn0021-9258
dc.identifier.pubmedidMEDLINE:8454638
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/75744
dc.identifier.wosidWOS:A1993KT36800084
dc.information.autorucMedicina;Gonzalez L;S/I;52306
dc.issue.numero9
dc.language.isoen
dc.nota.accesoSin adjunto
dc.pagina.final6667
dc.pagina.inicio6662
dc.publisherAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
dc.revistaJOURNAL OF BIOLOGICAL CHEMISTRY
dc.rightsregistro bibliográfico
dc.subjectPOLARIZED EPITHELIAL-CELLS
dc.subjectPOLYMERIC IMMUNOGLOBULIN RECEPTOR
dc.subjectINFLUENZA-VIRUS HEMAGGLUTININ
dc.subjectPLASMA-MEMBRANE PROTEINS
dc.subjectMDCK CELLS
dc.subjectVIRAL GLYCOPROTEINS
dc.subjectCYTOPLASMIC DOMAIN
dc.subjectINTRACELLULAR-TRANSPORT
dc.subjectENVELOPE PROTEINS
dc.subjectMAMMALIAN-CELLS
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleAPICAL SECRETION OF HEPATITIS-B SURFACE-ANTIGEN FROM TRANSFECTED MADIN-DARBY CANINE KIDNEY-CELLS
dc.typeartículo
dc.volumen268
sipa.codpersvinculados52306
sipa.indexWOS
sipa.indexScopus
sipa.trazabilidadCarga SIPA;09-01-2024
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