PHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE-C SOLUBILIZED G2 ACETYLCHOLINESTERASE FROM PLASMA-MEMBRANES OF CHROMAFFIN CELLS

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dc.contributor.authorPRIETO, AL
dc.contributor.authorFUENTES, ME
dc.contributor.authorARQUEROS, L
dc.contributor.authorINESTROSA, NC
dc.date.accessioned2025-01-23T19:23:38Z
dc.date.available2025-01-23T19:23:38Z
dc.date.issued1989
dc.description.abstractUsing whole homogenates and defined subcellular fractions of bovine adrenal medulla, we investigated the properties of the dimeric G2 molecular form of acetylcholinesterase (AChE), its distribution, and the mode of attachment to chromaffin cells. Our studies indicate that a substantial fraction of the G2 form is specifically susceptible to solubilization by phosphatidylinositol-specific phospholipase C (PIPLC) from subcellular fractions enriched with plasma membrane fragments. The results suggest that the G2 form of AChE is anchored in the plasma membrane to a glycolipid domain that contains phosphatidylinositol. Since a Ca+2-dependent PIPLC has been previously described in chromaffin granules, it is possible that the adrenal AChE could be released by a system reminiscent of that involved in the case of the surface glycoprotein of Trypanosoma brucei.
dc.fuente.origenWOS
dc.identifier.eissn1097-4547
dc.identifier.issn0360-4012
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/99241
dc.identifier.wosidWOS:A1989AW74800006
dc.issue.numero2
dc.language.isoen
dc.pagina.final173
dc.pagina.inicio169
dc.revistaJournal of neuroscience research
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titlePHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE-C SOLUBILIZED G2 ACETYLCHOLINESTERASE FROM PLASMA-MEMBRANES OF CHROMAFFIN CELLS
dc.typeartículo
dc.volumen24
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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