A major portion of synaptic basal lamina acetylcholinesterase is detached by high salt- and heparin-containing buffers from rat diaphragm muscle and <i>Torpedo</i> electric organ

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dc.contributor.authorCasanueva, OI
dc.contributor.authorGarcía-Huidobro, T
dc.contributor.authorCampos, EO
dc.contributor.authorAldunate, R
dc.contributor.authorGarrido, J
dc.contributor.authorInestrosa, NC
dc.date.accessioned2025-01-21T01:32:49Z
dc.date.available2025-01-21T01:32:49Z
dc.date.issued1998
dc.description.abstractCollagen-tailed asymmetric acetylcholinesterase (AChE) forms are believed to be anchored to the synaptic basal lamina via electrostatic: interactions involving proteoglycans. However, it was recently found that in avian and rat muscles, high ionic strength or polyanionic buffers could not detach AChE: from cell-surface clusters and that these buffers solubilized intracellular non-junctional asymmetric AChE rather than synaptic: forms of the enzyme. In the present study, asymmetric AChE forms were specifically solubilized by ionic buffers from sg synaptic basal! lamina-enriched fractions, largely devoid of intracellular material, obtained from the electric organ of Torpedo californica and the end plate regions of rat diaphragm muscle, Furthermore, foci of AChE activity were seen to diminish in size, number, and staining intensity when the rat synaptic basal lamina-enriched preparations were treated with the extraction buffers, Pn the case of Torpedo, almost all the AChE activity was removed from the pure basal lamina sheets. We therefore conclude that a major portion of extracellular collagen-tailed AChE is extractable from rat and Torpedo synaptic basal lamina by high ionic strength and heparin buffers,;although some non-extractable AChE activity remains associated with the junctional regions.
dc.fuente.origenWOS
dc.identifier.issn0021-9258
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/97327
dc.identifier.wosidWOS:000072048400066
dc.issue.numero7
dc.language.isoen
dc.pagina.final4265
dc.pagina.inicio4258
dc.revistaJournal of biological chemistry
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleA major portion of synaptic basal lamina acetylcholinesterase is detached by high salt- and heparin-containing buffers from rat diaphragm muscle and <i>Torpedo</i> electric organ
dc.typeartículo
dc.volumen273
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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