2007
DOI: 10.1111/j.1471-4159.2006.04343.x
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Differential role of extracellular histidines in copper, zinc, magnesium and proton modulation of the P2X7 purinergic receptor

Abstract: The P2X 7 receptor is a non-selective cationic channel activated by extracellular ATP, belonging to the P2X receptor family. To assess the role of extracellular histidines on the allosteric modulation of the rat P2X 7 receptor by divalent metals (copper, zinc and magnesium) and protons, these amino acid residues were singly substituted for corresponding alanines. Wild-type and mutated receptors were injected to Xenopus laevis oocytes; metal-related effects were evaluated by the two-electrode voltage-clamp tech… Show more

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Cited by 75 publications
(77 citation statements)
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“…This suggests that millimolar (or perhaps micromolar) concentrations of extracellular Ca 2+ and Mg 2+ may act as allosteric inhibitors of murine P2X7 as originally observed for rat P2X7 [46] and established by more recent studies of rat P2X7 [28,29]. The current study also demonstrates that an increase in intracellular Ca 2+ is not essential for P2X7-induced ROS formation (and pore formation) in MEL cells.…”
Section: +supporting
confidence: 62%
“…This suggests that millimolar (or perhaps micromolar) concentrations of extracellular Ca 2+ and Mg 2+ may act as allosteric inhibitors of murine P2X7 as originally observed for rat P2X7 [46] and established by more recent studies of rat P2X7 [28,29]. The current study also demonstrates that an increase in intracellular Ca 2+ is not essential for P2X7-induced ROS formation (and pore formation) in MEL cells.…”
Section: +supporting
confidence: 62%
“…It has long been considered that Mg 2+ chelates ATP 4− , the active form of the agonist, thereby inhibiting P2X 7 [39]. More recent data, however, demonstrates that Mg 2+ binds to the positively charged residues, histidine 130 and histidine 201 of rat P2X 7 to impair receptor function [40]. In this regard, histidine 201 is present in canine P2X 7 , as well as human P2X 7 , while an uncharged serine exists at position 130 in P2X 7 from these species [23,34].…”
Section: Discussionmentioning
confidence: 99%
“…5G), but the Zn 2ϩ effect on P2X7R remains controversial and depends on the preparation used. Indeed, Zn 2ϩ has a low potency on rat P2X7R expressed in oocytes (Coddou et al, 2002;Acuña-Castillo et al, 2007), when compared with rat P2X7R expressed in transfected HEK cells (Liu et al, 2008).…”
Section: Functional P2xrs Expressed By Embryonic Microglia In Situmentioning
confidence: 99%