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FEBS Lett
2007 Feb 06;5813:483-8. doi: 10.1016/j.febslet.2006.12.056.
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Pannexin1 is part of the pore forming unit of the P2X(7) receptor death complex.
Locovei S, Scemes E, Qiu F, Spray DC, Dahl G.
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The purinergic receptor P2X(7) is part of a complex signaling mechanism participating in a variety of physiological and pathological processes. Depending on the activation scheme, P2X(7) receptors in vivo are non-selective cation channels or form large pores that can mediate apoptotic cell death. Expression of P2X(7)R in Xenopus oocytes results exclusively in formation of a non-selective cation channel. However, here we show that co-expression of P2X(7)R with pannexin1 in oocytes leads to the complex response seen in many mammalian cells, including cell death with prolonged ATP application. While the cation channel activity is resistant to carbenoxolone treatment, this gap junction and hemichannel blocking drug suppressed the currents induced by ATP in pannexin1/P2X(7)R co-expressing cells. Thus, pannexin1 appears to be the molecular substrate for the permeabilization pore (or death receptor channel) recruited into the P2X(7)R signaling complex.
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17240370 ???displayArticle.pmcLink???PMC1868681 ???displayArticle.link???FEBS Lett ???displayArticle.grants???[+]
Bao,
Pannexin membrane channels are mechanosensitive conduits for ATP.
2004, Pubmed,
Xenbase
Bao,
Pannexin membrane channels are mechanosensitive conduits for ATP.
2004,
Pubmed
,
Xenbase Boldt,
Glu496Ala polymorphism of human P2X7 receptor does not affect its electrophysiological phenotype.
2003,
Pubmed
,
Xenbase Bruzzone,
Pharmacological properties of homomeric and heteromeric pannexin hemichannels expressed in Xenopus oocytes.
2005,
Pubmed
,
Xenbase Bruzzone,
Pannexins, a family of gap junction proteins expressed in brain.
2003,
Pubmed
,
Xenbase Burnstock,
Current state of purinoceptor research.
1995,
Pubmed Burnstock,
Overview. Purinergic mechanisms.
1990,
Pubmed Cheewatrakoolpong,
Identification and characterization of splice variants of the human P2X7 ATP channel.
2005,
Pubmed Coutinho-Silva,
P2Z purinoceptor-associated pores induced by extracellular ATP in macrophages and J774 cells.
1997,
Pubmed Dahl,
Mutagenesis to study channel structure.
2001,
Pubmed
,
Xenbase Dahl,
Pannexin: to gap or not to gap, is that a question?
2006,
Pubmed Di Virgilio,
The P2Z purinoceptor: an intriguing role in immunity, inflammation and cell death.
1995,
Pubmed Ellsworth,
The erythrocyte as a regulator of vascular tone.
1995,
Pubmed Faria,
Are second messengers crucial for opening the pore associated with P2X7 receptor?
2005,
Pubmed Hickman,
P2Z purinoceptors.
1996,
Pubmed
,
Xenbase Kim,
Proteomic and functional evidence for a P2X7 receptor signalling complex.
2001,
Pubmed Klapperstück,
Characteristics of P2X7 receptors from human B lymphocytes expressed in Xenopus oocytes.
2000,
Pubmed
,
Xenbase Locovei,
Pannexin 1 in erythrocytes: function without a gap.
2006,
Pubmed
,
Xenbase Locovei,
Activation of pannexin 1 channels by ATP through P2Y receptors and by cytoplasmic calcium.
2006,
Pubmed
,
Xenbase Newman,
Propagation of intercellular calcium waves in retinal astrocytes and Müller cells.
2001,
Pubmed North,
Molecular physiology of P2X receptors.
2002,
Pubmed Nuttle,
Expression of the pore-forming P2Z purinoreceptor in Xenopus oocytes injected with poly(A)+ RNA from murine macrophages.
1993,
Pubmed
,
Xenbase Panchin,
A ubiquitous family of putative gap junction molecules.
2000,
Pubmed Panchin,
Evolution of gap junction proteins--the pannexin alternative.
2005,
Pubmed Persechini,
Extracellular ATP in the lymphohematopoietic system: P2Z purinoceptors off membrane permeabilization.
1998,
Pubmed Petrou,
P2X7 purinoceptor expression in Xenopus oocytes is not sufficient to produce a pore-forming P2Z-like phenotype.
1997,
Pubmed
,
Xenbase Rassendren,
The permeabilizing ATP receptor, P2X7. Cloning and expression of a human cDNA.
1997,
Pubmed Schilling,
Maitotoxin and P2Z/P2X(7) purinergic receptor stimulation activate a common cytolytic pore.
1999,
Pubmed Seyffert,
Dissecting individual current components of co-expressed human P2X1 and P2X7 receptors.
2004,
Pubmed
,
Xenbase Smart,
Pore formation is not associated with macroscopic redistribution of P2X7 receptors.
2002,
Pubmed
,
Xenbase Steinberg,
ATP4- permeabilizes the plasma membrane of mouse macrophages to fluorescent dyes.
1987,
Pubmed Suadicani,
P2X7 receptors mediate ATP release and amplification of astrocytic intercellular Ca2+ signaling.
2006,
Pubmed Surprenant,
The cytolytic P2Z receptor for extracellular ATP identified as a P2X receptor (P2X7).
1996,
Pubmed Virginio,
Effects of divalent cations, protons and calmidazolium at the rat P2X7 receptor.
1997,
Pubmed Virginio,
Kinetics of cell lysis, dye uptake and permeability changes in cells expressing the rat P2X7 receptor.
1999,
Pubmed Wiley,
Partial agonists and antagonists reveal a second permeability state of human lymphocyte P2Z/P2X7 channel.
1998,
Pubmed
