Fiche publication
Date publication
janvier 2022
Journal
Methods in molecular biology (Clifton, N.J.)
Auteurs
Membres identifiés du Cancéropôle Est :
Dr GRUTTER Thomas
Tous les auteurs :
Dunning K, Peverini L, Grutter T
Lien Pubmed
Résumé
P2X7 receptors are ATP-gated ion channels permeable to metal cations, such as Na, K, and Ca. They also exhibit permeability to various large molecular weight species, reaching up to 900 Da, in a process known as macropore formation, which is a unique functional hallmark across the P2X family. While well-documented in a range of different cell types, the molecular mechanism underlying this phenomenon is poorly understood, and has been clouded through the use of electrophysiological methodology prone to artifacts as a result of significant changes in ionic concentrations in asymmetric conditions. In this chapter, we discuss the permeation properties of P2X7, the related methodological challenges and the use of symmetrical organic cation solutions as a useful technique for probing P2X7 permeation.
Mots clés
ATP, Electrophysiology, Macropore, NMDG, P2X7 ion channel, Permeation, Spermidine
Référence
Methods Mol Biol. 2022 ;2510:239-252
