Lipopolysaccharide inhibits the channel activity of the P2X7 receptor
Author
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Leiva Salcedo, Elías
Author
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Coddou, Claudio
Author
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Rodríguez, Felipe
Author
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Penna, Antonello
Author
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López, Ximena
Author
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Neira, Tanya
Author
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Fernández, Ricardo
Author
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Imarai, Mónica
Author
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Rios, Miguel
Author
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Escobar, Jorge
Author
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Montoya, Margarita
Author
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Huidobro Toro, Juan
Author
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Escobar, Alejandro
Author
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Acuña Castillo, Claudio
Admission date
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2018-12-20T15:24:43Z
Available date
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2018-12-20T15:24:43Z
Publication date
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2011
Cita de ítem
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Mediators of Inflammation, Volumen 2011, 2011, Pages 1-12.
Identifier
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09629351
Identifier
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14661861
Identifier
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10.1155/2011/152625
Identifier
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https://repositorio.uchile.cl/handle/2250/159074
Abstract
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The purinergic P2X7 receptor (P2X7R) plays an important role during the immune response, participating in several events such
as cytokine release, apoptosis, and necrosis. The bacterial endotoxin lipopolysaccharide (LPS) is one of the strongest stimuli of the
immune response, and it has been shown that P2X7R activation can modulate LPS-induced responses. Moreover, a C-terminal
binding site for LPS has been proposed. In order to evaluate if LPS can directly modulate the activity of the P2X7R, we tested several
signaling pathways associated with P2X7R activation in HEK293 cells that do not express the TLR-4 receptor. We found that LPS
alone was unable to induce any P2X7R-related activity, suggesting that the P2X7R is not directly activated by the endotoxin. On the
other hand, preapplication of LPS inhibited ATP-induced currents, intracellular calcium increase, and ethidium bromide uptake
and had no effect on ERK activation in HEK293 cells. In splenocytes-derived T-regulatory cells, in which ATP-induced apoptosis is
driven by the P2X7R, LPS inhibited ATP-induced apoptosis. Altogether, these results demonstrate that LPS modulates the activity
of the P2X7R and suggest that this effect could be of physiological relevance.