ArticleThe Journal of biological chemistry2008
Ectodomain lysines and suramin block of P2X1 receptors.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 34 citations in OpenAlex.
- Structural insights into the human P2X1 receptor and ligand interactions.Nature communications · 2024Article
- Hearing loss mutations alter the functional properties of human P2X2 receptor channels through distinct mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Purinergic P2X4 receptors and mitochondrial ATP production regulate T cell migration.The Journal of clinical investigation · 2018Article
- Insights into the channel gating of P2X receptors from structures, dynamics and small molecules.Acta pharmacologica Sinica · 2016Review
- Use of chimeras, point mutants, and molecular modeling to map the antagonist-binding site of 4,4',4″,4‴-(carbonylbis-(imino-5,1,3-benzenetriylbis(carbonylimino)))tetrakisbenzene-1,3-disulfonic acid (NF449) at P2X1 receptors for ATP.The Journal of biological chemistry · 2015Article
- Key sites for P2X receptor function and multimerization: overview of mutagenesis studies on a structural basis.Current medicinal chemistry · 2015Review
- Suppression of cell membrane permeability by suramin: involvement of its inhibitory actions on connexin 43 hemichannels.British journal of pharmacology · 2014Article
- P2X receptor chimeras highlight roles of the amino terminus to partial agonist efficacy, the carboxyl terminus to recovery from desensitization, and independent regulation of channel transitions.The Journal of biological chemistry · 2013Article
- Gintonin, a ginseng-derived lysophosphatidic acid receptor ligand, potentiates ATP-gated P2X₁ receptor channel currents.Molecules and cells · 2013Article
- Size matters in activation/inhibition of ligand-gated ion channels.Trends in pharmacological sciences · 2012Review
- Molecular and functional properties of P2X receptors--recent progress and persisting challenges.Purinergic signalling · 2012Review
- Molecular basis of selective antagonism of the P2X1 receptor for ATP by NF449 and suramin: contribution of basic amino acids in the cysteine-rich loop.British journal of pharmacology · 2012Article
- Cloning and characterization of a P2X receptor expressed in the central nervous system of Lymnaea stagnalis.PloS one · 2012Article
- Activation and regulation of purinergic P2X receptor channels.Pharmacological reviews · 2011Review
- Article
- Structural interpretation of P2X receptor mutagenesis studies on drug action.British journal of pharmacology · 2010Review
- New structure enlivens interest in P2X receptors.Trends in pharmacological sciences · 2010Review
- Amitriptyline does not block the action of ATP at human P2X4 receptor.British journal of pharmacology · 2010Article
- Sphingosine-1-phosphate elicits receptor-dependent calcium signaling in retinal amacrine cells.Journal of neurophysiology · 2009Article
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
P2X(1) receptors belong to a family of cation channels gated by extracellular ATP; they are found inter alia in smooth muscle, platelets, and immune cells. Suramin has been widely used as an antagonist at P2X receptors, and its analog 4,4',4'',4'''-[carbonylbis(imino-5,1,3-benzenetriylbis(carbonylimino))] tetrakis-benzene-1,3-disulfonic acid (NF449) is selective for the P2X(1) subtype. Human and mouse P2X(1) receptors were expressed in human embryonic kidney cells, and membrane currents evoked by ATP were recorded. ATP (10 nm to 100 microm) was applied only once to each cell, to avoid the profound desensitization exhibited by P2X(1) receptors. Suramin (10 microm) and NF449 (3-300 nM) effectively blocked the human receptor. Suramin had little effect on the mouse receptor. Suramin and NF449 are polysulfonates, with six and eight negative charges, respectively. We hypothesized that species differences might result from differences in positive residues presented by the large receptor ectodomain. Four lysines in the human sequence (Lys(111), Lys(127), Lys(138), and Lys(148)) were changed individually and together to their counterparts in the mouse sequence. The substitution K138E, either alone or together with K111Q, K127Q, and K148N, reduced the sensitivity to block by both suramin and NF449. Conversely, when lysine was introduced into the mouse receptor, the sensitivity to block by suramin and NF449 was much increased for E138K, but not for Q111K, Q127K, or N148K. The results explain the marked species difference in antagonist sensitivity and identify an ectodomain lysine residue that plays a key role in the binding of both suramin and NF449 to P2X(1) receptors.
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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.