Puroindoline-a and alpha 1-purothionin form ion channels in giant liposomes but exert different toxic actions on murine cells

Llanos P.; Henríquez M; Minic, J; Elmorjani, K; Marion, D; RIQUELME, G; Molgó J.; Benoit, E

Abstract

Puroindoline-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 explained by its ability to induce cationic-selective channels. © 2006 The Authors.

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Título según WOS: Puroindoline-a and alpha 1-purothionin form ion channels in giant liposomes but exert different toxic actions on murine cells
Título según SCOPUS: Puroindoline-a and a1-purothionin form ion channels in giant liposomes but exert different toxic actions on murine cells
Título de la Revista: FEBS JOURNAL
Volumen: 273
Número: 8
Editorial: WILEY-BLACKWELL
Fecha de publicación: 2006
Página de inicio: 1710
Página final: 1722
Idioma: English
URL: http://doi.wiley.com/10.1111/j.1742-4658.2006.05185.x
DOI:

10.1111/j.1742-4658.2006.05185.x

Notas: ISI, SCOPUS