ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2008
Opposite effects of zinc on human and rat P2X2 receptors.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 30 citations in OpenAlex.
- Mechanisms of ligand recognition and channel opening for P2X2 receptors in lipid nanodiscs.Science advances · 2026Article
- Mechanisms of ligand recognition and channel opening for P2X2 receptors in lipid nanodiscs.bioRxiv : the preprint server for biology · 2025Article
- Copper Increases the Cooperative Gating of Rat P2X2a Receptor Channels.Pharmaceuticals (Basel, Switzerland) · 2024Article
- Subtype-Specific Ligand Binding and Activation Gating in Homomeric and Heteromeric P2X Receptors.Biomolecules · 2024Article
- Physiological Concentrations of Zinc Have Dual Effects on P2X Myenteric Receptors of Guinea Pig.Cellular and molecular neurobiology · 2018Article
- Key sites for P2X receptor function and multimerization: overview of mutagenesis studies on a structural basis.Current medicinal chemistry · 2015Review
- Regulation of ATP-gated P2X channels: from redox signaling to interactions with other proteins.Antioxidants & redox signaling · 2014Review
- Non-synonymous single nucleotide polymorphisms in the P2X receptor genes: association with diseases, impact on receptor functions and potential use as diagnosis biomarkers.International journal of molecular sciences · 2014Review
- Potent and long-lasting inhibition of human P2X2 receptors by copper.Neuropharmacology · 2014Article
- Heteromeric assembly of P2X subunits.Frontiers in cellular neuroscience · 2013Review
- Human stem cell-derived astrocytes and their application to studying Nrf2-mediated neuroprotective pathways and therapeutics in neurodegeneration.British journal of clinical pharmacology · 2013Review
- High potency zinc modulation of human P2X2 receptors and low potency zinc modulation of rat P2X2 receptors share a common molecular mechanism.The Journal of biological chemistry · 2012Article
- Neurons respond directly to mechanical deformation with pannexin-mediated ATP release and autostimulation of P2X7 receptors.The Journal of physiology · 2012Article
- Tightening of the ATP-binding sites induces the opening of P2X receptor channels.The EMBO journal · 2012Article
- Activation and regulation of purinergic P2X receptor channels.Pharmacological reviews · 2011Review
- Zinc inactivates melastatin transient receptor potential 2 channels via the outer pore.The Journal of biological chemistry · 2011Article
- Identification of P2X₃ and P2X₇ purinergic receptors activated by ATP in rat lacrimal gland.Investigative ophthalmology & visual science · 2011Article
- Allosteric modulation of ATP-gated P2X receptor channels.Reviews in the neurosciences · 2011Review
- Human embryonic stem cell-derived neurons as a tool for studying neuroprotection and neurodegeneration.Molecular neurobiology · 2010Article
- Gated access to the pore of a P2X receptor: structural implications for closed-open transitions.The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
P2X(2) receptors from rats show potentiation when a submaximal concentration of ATP is combined with zinc in the range of 10-100 microM. Alignment of the amino acid sequences of human P2X(2) (hP2X(2)) and rat P2X(2) (rP2X(2)) indicated that only one of two histidines essential for zinc potentiation in rP2X(2) is present at the homologous position in hP2X(2) (H132), with the position homologous to rat H213 instead having an arginine (R225). When expressed in Xenopus oocytes, mouse P2X(2a) and P2X(2b) receptors showed zinc potentiation indistinguishable from rat P2X(2a), but hP2X(2b) receptors were inhibited by zinc. The extent of zinc inhibition of hP2X(2b) varied with the ATP concentration, with an IC(50) of 8.4 microM zinc when ATP was applied at 10% of maximal and 87 microM zinc when ATP was applied at 99% of maximal. Site-directed mutagenesis showed that none of the nine histidines in the extracellular domain of hP2X(2b) were required for zinc inhibition, although inhibition was attenuated in the H204A and H209A mutations. Mutating R225 to a cysteine was sufficient to confer zinc potentiation onto hP2X(2b), and zinc potentiation was absent in the hP2X(2b)H132A/R225C double mutant. This suggests that zinc potentiation in the mutant hP2X(2b) uses the same mechanism as zinc potentiation in wild-type rP2X(2a). Because of the species-specific modulation by zinc, evidence for an in vivo role of P2X(2) receptors based on studies conducted on genetically modified mice needs to be viewed with caution when extrapolations are made to the function of the human nervous system.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.