| Author | Alberto, Anael Viana Pinto | |
| Author | Faria, R. X. | |
| Author | Couto, C. G. C. | |
| Author | Ferreira, L. G. B. | |
| Author | Souza, C. A. M. | |
| Author | Teixeira, P. C. N. | |
| Author | Fróes, M. M. | |
| Author | Alves, L. A. | |
| Access date | 2015-09-21T17:25:29Z | |
| Available date | 2015-09-21T17:25:29Z | |
| Document date | 2013 | |
| Citation | ALBERTO, A. V. P.; et al. Is pannexin the pore associated with the P2X7 receptor?. Naunyn-Schmiedeberg's Arch Pharmacol, v.386, p..775–787, 2013. | pt_BR |
| URI | https://www.arca.fiocruz.br/handle/icict/11721 | |
| Language | eng | pt_BR |
| Publisher | Springer-Verlag Berlin Heidelberg | pt_BR |
| Rights | open access | |
| Title | Is pannexin the pore associated with the P2X7 receptor? | pt_BR |
| Type | Article | |
| DOI | 10.1007/s00210-013-0868-x | pt_BR |
| Abstract | The P2X7 receptor (P2X7R), an ATP-gated cation
channel, is expressed predominantly in leukocytes.
Activation of P2X7R has been implicated in the formation
of a cytolytic pore (i.e., a large conductance channel) that
allows the passage of molecules up to 900 Da in macrophages.
At least two hypotheses have been presented to
explain the conversion of a nonselective cation channel to
a cytolytic pore. One hypothesis suggests that the pore is a
separate molecular structure activated by P2X7R, and the
second asserts that this is an intrinsic property of P2X7R (pore
dilation). Based on connexin knockout and hemichannel antagonist
studies, some groups have concluded that connexins
and pannexins, the hemichannel-forming proteins in vertebrates,
are fundamental components of the large conductance
channel associated with P2X7R. Dye uptake and electrophysiology
experiments were used to evaluate the efficacy and
specificity of some hemichannel antagonists under conditions
known to open the large conductance channel associated with
P2X7R. Hemichannel antagonists and interference RNA
(RNAi) targeting pannexin-1 did not affect P2X7R macroscopic
currents [ATP, 1,570±189 pA; ATP+100 μMcarbenoxolone
(CBX), 1,498±100 pA; ATP+1 mM probenecid (Prob), 1,522
±9 pA] or dye uptake in a FACS assay (ATP, 63±5 %; ATP+
100 μM CBX, 51.51±8.4 %; ATP+1 mM Prob, 57.7±4.3 %)
in mousemacrophages. These findings strongly suggest that the
high-permeability pore evident after prolonged P2X7R activation
does not occur through connexin or pannexin
hemichannels in murine macrophages. Another membrane protein
may be involved in P2X7R pore formation. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Comunicação Celular. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Comunicação Celular. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Comunicação Celular. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Comunicação Celular. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Comunicação Celular. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Comunicação Celular. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Universidade Federal do Rio de Janeiro (UFRJ). Instituto de Ciências Biomédicas. Laboratório de Neuroanatomia Celular. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Comunicação Celular. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Subject | Connexin | pt_BR |
| Subject | Pannexin | pt_BR |
| Subject | Hemichannels | pt_BR |
| Subject | Gap junctions | pt_BR |
| Subject | P2X7 receptor | pt_BR |
| Subject | Gap junction antagonists | pt_BR |
| Subject | Electrophysiology | pt_BR |
| Subject | Pore | pt_BR |
| DeCS | Porinas | pt_BR |
| DeCS | Connexina 43 | pt_BR |
| DeCS | Junções gap | pt_BR |
| DeCS | Eletrofisiologia | pt_BR |
