Voltage-dependent anion channel transports calcium ions through biomimetic membranes.
Fiche publication
Date publication
mars 2007
Journal
Langmuir : the ACS journal of surfaces and colloids
Auteurs
Membres identifiés du Cancéropôle Est :
Dr BERQUAND Alexandre
Tous les auteurs :
Deniaud A, Rossi C, Berquand A, Homand J, Campagna S, Knoll W, Brenner C, Chopineau J
Lien Pubmed
Résumé
The mitochondrial outer membrane channel (VDAC), a central player in mitochondria and cell death, was reconstituted in polymer-supported phospholipid bilayers. Highly purified VDAC was first reconstituted in vesicles; channel properties and NADH-ferricyanide reductase activity were ascertained before deposition onto solid substrates. 1-Palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine/1,2-distearoyl-sn-glycero-3-phosphoethanolamine-poly(ethylene glycol)-N-hydroxysuccinimide mixed vesicles containing VDAC were linked onto amine-grafted surfaces (glass and gold) and disrupted to form a VDAC-containing polymer-tethered planar bilayer. Surface plasmon spectroscopy, fluorescence microscopy, and atomic force microscopy measurements ascertained the membrane thickness, fluidity, and continuity. VDAC reconstituted in bilayers efficiently transported calcium ions and was modulable by two channel blockers, 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid and l-glutamate. The novel setup may allow the study of the assembly of a polyprotein complex centered on VDAC and its role in mitochondrial biology, calcium fluxes, and apoptosis.
Mots clés
Animals, Apoptosis, Calcium, chemistry, Calcium Channel Blockers, chemistry, Humans, Ion Transport, Membranes, Artificial, Multiprotein Complexes, chemistry, NADH, NADPH Oxidoreductases, chemistry, Surface Plasmon Resonance, Voltage-Dependent Anion Channels, antagonists & inhibitors
Référence
Langmuir. 2007 Mar 27;23(7):3898-905