Article
The P2X7 receptor: Shifting from a low- to a high-conductance channel — An enigmatic phenomenon?
Registro en:
ALVES, Luiz Anastacio et al. The P2X7 receptor: Shifting from a low- to a high-conductance channel — An enigmatic phenomenon?. Biochimica et Biophysica Acta, v.1838,n.10, p.2578–2587, 2014.
10.1016/j.bbamem.2014.05.015
Autor
Alves, Luiz Anastácio
Reis, Ricardo Augusto de Melo
Souza, Cristina Alves Magalhães de
Freitas, Monica Santos de
Teixeira, Pedro Celso Nogueira
Ferreira, Dinarte Neto Moreira
Xavier, Robson Faria
Resumen
The general structure of the P2X7 receptor (P2X7R) is similar to the structure of other P2X receptor family
members, with the exception of its C terminus, which is the longest of this family. The P2X7R activates several
intracellular signaling cascades, such as the calmodulin, mitogen-activated protein kinase and phospholipase
D pathways. At low concentrations of ATP (micromolar range), P2X7R activation opens a cationic channel, similarly
to other P2X receptors. However, in the presence of high concentrations of ATP (millimolar range), it opens
a pathway that allows the passage of larger organic cations and anions. Here,we discuss both the structural characteristics
of P2X7R related to its remarkable functions and the proposed mechanisms, including the dilation of
the endogenous pore and the integration of another channel. In addition, we highlight the importance of
P2X7R as a therapeutic target.