| Author | Souza, Cristina Alves Magalhães de | |
| Author | Teixeira, Pedro Celso Nogueira | |
| Author | Faria, Robson Xavier | |
| Author | Krylova, Oxana | |
| Author | Pohl, Peter | |
| Author | Alves, Luiz Anastacio | |
| Access date | 2020-03-30T20:38:36Z | |
| Available date | 2020-03-30T20:38:36Z | |
| Document date | 2012 | |
| Citation | SOUZA, Cristina Alves Magalhães de et al. A consensus segment in the M2 domain of the hP2X7 receptor shows ion channel activity in planar lipid bilayers and in biological membranes. Biochimica et Biophysica Acta, v. 1818, p. 64-71, 2012. | pt_BR |
| ISSN | 0006-3002 | pt_BR |
| URI | https://www.arca.fiocruz.br/handle/icict/40569 | |
| Language | eng | pt_BR |
| Publisher | Elsevier | pt_BR |
| Rights | restricted access | |
| Subject in Portuguese | Receptor P2X7 | pt_BR |
| Subject in Portuguese | Atividade do canal iônico | pt_BR |
| Subject in Portuguese | Atividade de canal único peptídeo | pt_BR |
| Subject in Portuguese | Bicamada lipídica planar artificial | pt_BR |
| Subject in Portuguese | Grampo de remendo | pt_BR |
| Title | A consensus segment in the M2 domain of the hP2X(7) receptor shows ion channel activity in planar lipid bilayers and in biological membranes | pt_BR |
| Type | Article | |
| DOI | 10.1016/j.bbamem.2011.09.010 | |
| Abstract | The P2X(7) receptor (P2X(7)R) is an ATP-gated, cation-selective channel permeable to Na(+), K(+) and Ca(2+). This channel has also been associated with the opening of a non-selective pore that allows the flow of large organic ions. However, the biophysical properties of the P2X(7)R have yet to be characterized unequivocally. We investigated a region named ADSEG, which is conserved among all subtypes of P2X receptors (P2XRs). It is located in the M2 domain of hP2X(7)R, which aligns with the H5 signature sequence of potassium channels. We investigated the channel forming ability of ADSEG in artificial planar lipid bilayers and in biological membranes using the cell-attached patch-clamp techniques. ADSEG forms channels, which exhibit a preference for cations. They are voltage independent and show long-term stability in planar lipid bilayers as well as under patch-clamping conditions. The open probability of the ADSEG was similar to that of native P2X(7)R. The conserved part of the M2 domain of P2X(7)R forms ionic channels in planar lipid bilayers and in biological membranes. Its electrophysiological characteristics are similar to those of the whole receptor. Conserved and hydrophobic part of the M2 domain forms ion channels. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Comunicação Celular. Rio de Janeiro, RJ, Brasil / Leibniz Institute for Molecular Pharmacology. Berlin, Germany. | 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 | Leibniz Institute for Molecular Pharmacology. Berlin, Germany. | pt_BR |
| Affilliation | Johannes Kepler Universität. Institut für Biophysis. Linz, Austria. | pt_BR |
| Affilliation | undação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Comunicação Celular. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Subject | P2X7 receptor | pt_BR |
| Subject | Ionic channel activity | pt_BR |
| Subject | Peptide single channel activity | pt_BR |
| Subject | Artificial planar lipid bilayer | pt_BR |
| Subject | Patch-clamp | pt_BR |
| Embargo date | 2025-01-01 | |
