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Authordc.contributor.authorLlanos Vidal, Paola 
Authordc.contributor.authorHenríquez, Mauricio 
Authordc.contributor.authorMinic, Jasmina 
Authordc.contributor.authorElmorjani, Khalil 
Authordc.contributor.authorMarion, Didier 
Authordc.contributor.authorRiquelme, Gloria 
Authordc.contributor.authorMolgó, Jordi 
Authordc.contributor.authorBenoit, Evelyne 
Admission datedc.date.accessioned2019-03-11T12:51:08Z
Available datedc.date.available2019-03-11T12:51:08Z
Publication datedc.date.issued2006
Cita de ítemdc.identifier.citationFEBS Journal, Volumen 273, Issue 8, 2018, Pages 1710-1722
Identifierdc.identifier.issn1742464X
Identifierdc.identifier.issn17424658
Identifierdc.identifier.other10.1111/j.1742-4658.2006.05185.x
Identifierdc.identifier.urihttps://repositorio.uchile.cl/handle/2250/164153
Abstractdc.description.abstractPuroindoline-a (PIN-a) and α1-purothionin (α1-PTH), isolated from wheat endosperm of Triticum aestivum sp., have been suggested to play a role in plant defence mechanisms against phytopathogenic organisms. We investigated their ability to form pores when incorporated into giant liposomes using the patch-clamp technique. PIN-a formed cationic channels (≈ 15 pS) with the following selectivity K+ > Na+ ≫ Cl -. Also, α1-PTH formed channels of ≈ 46 pS and 125 pS at +100 mV, the selectivity of which was Ca2+ > Na+ ≈ K+ ≫ Cl- and Cl- ≫ Na+, respectively. In isolated mouse neuromuscular preparations, α1-PTH induced muscle membrane depolarization, leading to blockade of synaptic transmission and directly elicited muscle twitches. Also, α1-PTH caused swelling of differentiated neuroblastoma NG108-15 cells, membrane bleb formation, and disorganization of F-actin. In contrast, similar concentrations of PIN-a had no detectable effects. The cytotoxic actions of α1-PTH on mammalian cells may be expla
Lenguagedc.language.isoen
Type of licensedc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile
Link to Licensedc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/
Sourcedc.sourceFEBS Journal
Keywordsdc.subjectα1-purothionin
Keywordsdc.subjectGiant liposomes
Keywordsdc.subjectIon channels
Keywordsdc.subjectNeuromuscular transmission
Keywordsdc.subjectPuroindoline-a
Títulodc.titlePuroindoline-a and α1-purothionin form ion channels in giant liposomes but exert different toxic actions on murine cells
Document typedc.typeArtículo de revista
Catalogueruchile.catalogadorSCOPUS
Indexationuchile.indexArtículo de publicación SCOPUS
uchile.cosechauchile.cosechaSI


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Attribution-NonCommercial-NoDerivs 3.0 Chile
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 3.0 Chile