| Author | Faria, Robson X. | |
| Author | Reis, Ricardo A. M. | |
| Author | Ferreira, Leonardo G.B. | |
| Author | Mello, Paula F. T. Cesar de | |
| Author | Moraes, Milton Ozório | |
| Access date | 2016-12-27T10:40:28Z | |
| Available date | 2016-12-27T10:40:28Z | |
| Document date | 2016 | |
| Citation | FARIA, Robson X. et al. P2X7R large pore is partially blocked by pore forming proteins antagonists in astrocytes. J Bioenerg Biomembr, v.48, p.309–324, 2016. | pt_BR |
| ISSN | 0145-479X | pt_BR |
| URI | https://www.arca.fiocruz.br/handle/icict/16568 | |
| Language | eng | pt_BR |
| Publisher | Springer Verlag | pt_BR |
| Rights | restricted access | |
| Subject in Portuguese | Eletrofisiologia | pt_BR |
| Subject in Portuguese | Antagonistas de Hemichannel | pt_BR |
| Subject in Portuguese | Formação de poros | pt_BR |
| Subject in Portuguese | Hemichannels | pt_BR |
| Title | P2X7R large pore is partially blocked by pore forming proteins antagonists in astrocytes | pt_BR |
| Type | Article | |
| DOI | 10.1007/s10863-016-9649-9 | |
| Abstract | The ATP-gated P2X7R (P2X7R) is a channel, which is involved in events, such as inflammation, cell death, and pain. The most intriguing event concerning P2X7R functions is the phenomenon of pore dilation. Once P2X7R is activated, the permeability of the plasma membrane becomes higher, leading to the permeation of 1000 Da-weight solutes. The mechanisms involved in this process remain unclear. Nevertheless, this event is not exclusively through P2X7R, as other proteins may form large pores in the plasma membrane. Recent evidence concerning pore formation reveals putative P2X7R and other pores-associated protein complexes, revealing cross-interactive pharmacological and biophysical issues. In this work, we showed results that corroborated with cross-interactive aspects with P2X7R and pores in astrocytes. These cells expressed most of the pores, including P2X7R. We discovered that different pore types open with peculiar characteristics, as both anionic and cationic charged solutes permeate the plasma membrane, following P2X7R activation. Moreover, we showed that both synergic and additive relationships are found within P2X7, cationic, and anionic large pores. Therefore, our data suggest that other protein-related pores are assembled following the formation of P2X7R pore. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Toxoplasmose. Rio de Janeiro, RJ. Brasil. | pt_BR |
| Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Biofísica Carlos Chagas Filho. Laboratório de Neuroquímica. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Inflamação. Rio de Janeiro, RJ. Brasil. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Hanseníase. Rio de Janeiro, RJ. Brasil. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Hanseníase. Rio de Janeiro, RJ. Brasil. | pt_BR |
| Subject | P2X7R | pt_BR |
| Subject | Pore formation | pt_BR |
| Subject | Hemichannels | pt_BR |
| Subject | Hemichannel antagonists | pt_BR |
| Subject | Electrophysiology | pt_BR |
| e-ISSN | 1573-6881 | |
| Embargo date | 2030-01-01 | |
