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      Divalent metal modulation of Japanese flounder ( Paralichthys olivaceus) purinergic P2X7 receptor

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          Abstract

          Paralichthys olivaceus P2X7 receptor (poP2X7R) is a recently identified as a P2X7 purinergic receptor involved in innate immunity of the Japanese flounder Paralichthys olivaceus. Divalent metals are allosteric modulators of mammalian P2 XRs, but there is no information for fish P2 XRs. Here, we characterized the effects of divalent metals on poP2X7R channel activity by electrophysiology and molecular biology techniques. Copper, zinc and mercury inhibited poP2X7R‐mediated currents with different maximal inhibition potency, while cadmium had no effect on poP2X7R activity. Mercury‐induced inhibition was irreversible, but the inhibitory effects of copper and zinc were reversed after washout. Cooper and zinc also reduced poP2X7R‐mediated interleukin‐1 mRNA production. These findings suggest that divalent metals have potential effects on the Japanese flounder innate immune response through modulation of poP2X7R activity.

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          Activation and regulation of purinergic P2X receptor channels.

          Claudio Coddou, Zonghe Yan, Tomas Obsil … (2011)
          Mammalian ATP-gated nonselective cation channels (P2XRs) can be composed of seven possible subunits, denoted P2X1 to P2X7. Each subunit contains a large ectodomain, two transmembrane domains, and intracellular N and C termini. Functional P2XRs are organized as homomeric and heteromeric trimers. This review focuses on the binding sites involved in the activation (orthosteric) and regulation (allosteric) of P2XRs. The ectodomains contain three ATP binding sites, presumably located between neighboring subunits and formed by highly conserved residues. The detection and coordination of three ATP phosphate residues by positively charged amino acids are likely to play a dominant role in determining agonist potency, whereas an AsnPheArg motif may contribute to binding by coordinating the adenine ring. Nonconserved ectodomain histidines provide the binding sites for trace metals, divalent cations, and protons. The transmembrane domains account not only for the formation of the channel pore but also for the binding of ivermectin (a specific P2X4R allosteric regulator) and alcohols. The N- and C- domains provide the structures that determine the kinetics of receptor desensitization and/or pore dilation and are critical for the regulation of receptor functions by intracellular messengers, kinases, reactive oxygen species and mercury. The recent publication of the crystal structure of the zebrafish P2X4.1R in a closed state provides a major advance in the understanding of this family of receptor channels. We will discuss data obtained from numerous site-directed mutagenesis experiments accumulated during the last 15 years with reference to the crystal structure, allowing a structural interpretation of the molecular basis of orthosteric and allosteric ligand actions.
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            The P2X7 receptor: a key player in IL-1 processing and release.

            Marco Idzko, Roberto Lemoli, J F Virgilio … (2006)
            Human IL-1 family proteins are key mediators of the host response to infections, injury, and immunologic challenges. The mechanism by which IL-1 activates proinflammatory responses in target cells, and the plasma membrane receptors involved, is fairly well known. This has led to the development of innovative drugs that block IL-1 downstream to its synthesis and secretion. On the contrary, the mechanism of IL-1 and other IL-1 family members (e.g., IL-18) maturation and release is incompletely understood. Accruing evidence points to a plasma membrane receptor for extracellular ATP, the P2X(7) receptor, as a key player in both processes. A deeper understanding of the mechanism by which the P2X(7) receptor triggers IL-1 maturation and exteriorization may suggest novel avenues for the treatment of inflammatory diseases and provide a deeper insight in the fundamental mechanism of protease activation and cellular export of proteins lacking a leader sequence.
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              Effects of divalent cations, protons and calmidazolium at the rat P2X7 receptor.

              Caterina Virginio, Dennis J. Church, R.Alan North … (1997)
              The P2X7 receptor is a uniquely bifunctional molecule through which ATP can open a small cationic channel typical of ionotropic receptors and also induce a large pore permeable to high molecular weight molecules (> 600 Da). Activation of this large pore can lead to cell lysis within 1-2 min. We asked whether pharmacological differences existed between the cationic channel and the cell permeabilizing pore by measuring whole-cell currents and uptake of a propidium dye (YO-PRO; Mw 629) in HEK293 cells stably expressing the rat P2X7 receptor, and comparing the actions of divalent cations and protons in these two assays. Currents in response to 2'-3'-(O)-(4-benzoyl benzoyl) ATP (BzATP, 30 microM) were inhibited by extracellular calcium, magnesium, zinc, copper and protons with half-maximal inhibitory concentrations (IC50) of 2.9 mM, 0.5 mM, 11 microM, 0.5 microM and 0.4 microM, respectively. The inhibition was voltage independent in each case. YO-PRO uptake induced by BzATP was also inhibited with similar IC50 values. The rank order of potency of a range of divalents was Cu2+ > Cd2+ = Zn2+ > Ni2+ > Mg2+ = Co2+ > Mn2+ > Ca2+ = Ba2+ > Sr2+. These results suggest that these divalent cations and protons all act primarily as allosteric modulators to alter the affinity of ATP binding to the P2X7 receptor. In contrast, extracellular (but not intracellular) calmidazolium inhibited the BzATP-evoked current by up to 90% (IC50 = 15 nM) but had no effect on YO-PRO uptake. Thus, calmidazolium can block activation of the ionic channel but this does not prevent the formation of the large permeabilizing pore.
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                Author and article information

                Contributors
                Claudio Coddou: ccoddou@ucn.cl
                Journal
                Journal ID (nlm-ta): FEBS Open Bio
                Journal ID (iso-abbrev): FEBS Open Bio
                Journal ID (doi): 10.1002/(ISSN)2211-5463
                Journal ID (publisher-id): FEB4
                Title: FEBS Open Bio
                Publisher: John Wiley and Sons Inc. (Hoboken )
                ISSN (Electronic): 2211-5463
                Publication date (Electronic): 23 January 2018
                Publication date Collection: March 2018
                Volume: 8
                Issue: 3 ( doiID: 10.1002/feb4.2018.8.issue-3 )
                Pages: 383-389
                Affiliations
                [ 1 ] Department of Biomedical Sciences Faculty of Medicine Universidad Católica del Norte Coquimbo Chile
                [ 2 ] Tianjin Key Laboratory of Animal and Plant Resistance College of Life Sciences Tianjin Normal University China
                Author notes
                [*] [* ] Correspondence

                C. Coddou, Department of Biomedical Sciences, Faculty of Medicine, Universidad Católica del Norte, Larrondo 1281, Coquimbo 1781421, Chile

                E‐mail: ccoddou@ 123456ucn.cl

                Article
                Publisher ID: FEB412375
                DOI: 10.1002/2211-5463.12375
                PMC ID: 5832984
                SO-VID: fdd233d7-5ffb-4a73-9504-2376ef7f228d
                Copyright © © 2018 The Authors. Published by FEBS Press and John Wiley & Sons Ltd.
                License:

                This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 02 November 2017
                Date revision received : 19 December 2017
                Date accepted : 21 December 2017
                Page count
                Figures: 3, Tables: 1, Pages: 7, Words: 4297
                Funding
                Funded by: FONDECYT
                Award ID: 11121302
                Award ID: 1161490
                Funded by: Chilean Science and Technology Agency (CONICYT)
                Funded by: National Natural Science Fundation of China
                Award ID: 31572645
                Categories
                Subject: Research Article
                Subject: Research Articles
                Custom metadata
                source-schema-version-number 2.0
                component-id feb412375
                cover-date March 2018
                details-of-publishers-convertor Converter:WILEY_ML3GV2_TO_NLMPMC version:version=5.3.2.2 mode:remove_FC converted:02.03.2018

                Keywords: atp,divalent metals,japanese flounder,paralichthys olivaceus,purinergic receptor p2x7
                Data availability:
                Keywords: atp, divalent metals, japanese flounder, paralichthys olivaceus, purinergic receptor p2x7

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