Potassium channel opener

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A potassium channel opener is a type of drug which facilitates ion transmission through potassium channels.

Contents

Examples

Some examples include:

ClassSubclassesActivators
Calcium-activated

6T & 1P

[ citation needed ]
Inwardly rectifying

2T & 1P

[ citation needed ]
  • none
[ citation needed ]
[ citation needed ]
Tandem pore domain

4T & 2P

[ citation needed ]
Voltage-gated

6T & 1P

See also

Related Research Articles

<span class="mw-page-title-main">Potassium channel</span> Ion channel that selectively passes K+

Potassium channels are the most widely distributed type of ion channel found in virtually all organisms. They form potassium-selective pores that span cell membranes. Potassium channels are found in most cell types and control a wide variety of cell functions.

<span class="mw-page-title-main">Nicorandil</span> Chemical compound

Nicorandil is a vasodilator drug used to treat angina.

<span class="mw-page-title-main">Two-pore-domain potassium channel</span> Class of transport proteins

The two-pore-domain or tandem pore domain potassium channels are a family of 15 members that form what is known as leak channels which possess Goldman-Hodgkin-Katz (open) rectification. These channels are regulated by several mechanisms including signaling lipids, oxygen tension, pH, mechanical stretch, and G-proteins. Two-pore-domain potassium channels correspond structurally to a inward-rectifier potassium channel α-subunits. Each inward-rectifier potassium channel α-subunit is composed of two transmembrane α-helices, a pore helix and a potassium ion selectivity filter sequence and assembles into a tetramer forming the complete channel. The two-pore domain potassium channels instead are dimers where each subunit is essentially two α-subunits joined together.

<span class="mw-page-title-main">KvLQT2</span> Protein-coding gene in the species Homo sapiens

Kv7.2 (KvLQT2) is a voltage- and lipid-gated potassium channel protein coded for by the gene KCNQ2.

<span class="mw-page-title-main">KvLQT3</span> Protein-coding gene in the species Homo sapiens

Kv7.3 (KvLQT3) is a potassium channel protein coded for by the gene KCNQ3.

<span class="mw-page-title-main">KCNK3</span> Protein-coding gene in the species Homo sapiens

Potassium channel subfamily K member 3 is a protein that in humans is encoded by the KCNK3 gene.

<span class="mw-page-title-main">KCNQ4</span> Mammalian protein found in Homo sapiens

Potassium voltage-gated channel subfamily KQT member 4, also known as voltage-gated potassium channel subunit Kv7.4, is a protein that in humans is encoded by the KCNQ4 gene.

<span class="mw-page-title-main">KCNK1</span> Protein-coding gene in the species Homo sapiens

Potassium channel subfamily K member 1 is a protein that in humans is encoded by the KCNK1 gene.

<span class="mw-page-title-main">KCNK4</span> Protein-coding gene in the species Homo sapiens

Potassium channel subfamily K member 4 is a protein that in humans is encoded by the KCNK4 gene. KCNK4 protein channels are also called TRAAK channels.

<span class="mw-page-title-main">KCNK5</span> Protein-coding gene in the species Homo sapiens

Potassium channel subfamily K member 5 is a protein that in humans is encoded by the KCNK5 gene.

<span class="mw-page-title-main">KCNJ9</span> Protein-coding gene in the species Homo sapiens

G protein-activated inward rectifier potassium channel 3 is a protein that in humans is encoded by the KCNJ9 gene.

<span class="mw-page-title-main">KCNK17</span> Protein-coding gene in the species Homo sapiens

Potassium channel subfamily K member 17 is a protein that in humans is encoded by the KCNK17 gene.

<span class="mw-page-title-main">KCNK7</span> Protein-coding gene in the species Homo sapiens

Potassium channel, subfamily K, member 7, also known as KCNK7 or K2P7.1 is a protein which is encoded in humans by the KCNK7 gene. K2P7.1 is a potassium channel containing two pore-forming P domains. Multiple transcript variants encoding different isoforms have been found for this gene.

<span class="mw-page-title-main">KCNK10</span> Protein-coding gene in the species Homo sapiens

Potassium channel, subfamily K, member 10, also known as KCNK10 is a human gene. The protein encoded by this gene, K2P10.1, is a potassium channel containing two pore-forming P domains.

<span class="mw-page-title-main">KCNK16</span> Protein-coding gene in the species Homo sapiens

Potassium channel subfamily K member 16 is a protein that in humans is encoded by the KCNK16 gene. The protein encoded by this gene, K2P16.1, is a potassium channel containing two pore-forming P domains.

<span class="mw-page-title-main">KCNK18</span> Protein-coding gene in the species Homo sapiens

Potassium channel subfamily K member 18 (KCNK18), also known as TWIK-related spinal cord potassium channel (TRESK) or K2P18.1 is a protein that in humans is encoded by the KCNK18 gene. K2P18.1 is a potassium channel containing two pore-forming P domains.

<span class="mw-page-title-main">Potassium channel blocker</span> Several medications that disrupt movement of K+ ions

Potassium channel blockers are agents which interfere with conduction through potassium channels.

<span class="mw-page-title-main">Retigabine</span> Anticonvulsant, which works as a potassium-channel opener

Retigabine (INN) or ezogabine (USAN) is an anticonvulsant used as an adjunctive treatment for partial epilepsies in treatment-experienced adult patients. The drug was developed by Valeant Pharmaceuticals and GlaxoSmithKline. It was approved by the European Medicines Agency under the trade name Trobalt on March 28, 2011, and by the United States Food and Drug Administration (FDA), under the trade name Potiga, on June 10, 2011. Production was discontinued in June 2017.

Michel Lazdunski is a French biologist specializing in biochemistry, physiology, pathophysiology, molecular pharmacology and neuroscience.

<span class="mw-page-title-main">XEN1101</span> Cholesterol 24-hydroxylase inhibitor

XEN1101 (encukalner) is an experimental small molecule anticonvulsant and selective Kv7.2/Kv7.3 potassium channel opener being investigated as a treatment for refractory focal onset seizures and major depressive disorder.

References

  1. ↑ Mizutani S, Prasad SM, Sellitto AD, Schuessler RB, Damiano RJ, Lawton JS (August 2005). "Myocyte volume and function in response to osmotic stress: observations in the presence of an adenosine triphosphate-sensitive potassium channel opener". Circulation. 112 (9 Suppl): I219–23. doi: 10.1161/CIRCULATIONAHA.104.523746 . PMID   16159820.
  2. ↑ Wang T (February 2003). "The effects of the potassium channel opener minoxidil on renal electrolytes transport in the loop of henle". J. Pharmacol. Exp. Ther. 304 (2): 833–40. doi:10.1124/jpet.102.043380. PMID   12538840. S2CID   6948410.
  3. ↑ Sudo H, Yogo K, Ishizuka N, Otsuka H, Horie S, Saito K (November 2008). "Nicorandil, a potassium channel opener and nitric oxide donor, improves the frequent urination without changing the blood pressure in rats with partial bladder outlet obstruction". Biol. Pharm. Bull. 31 (11): 2079–82. doi: 10.1248/bpb.31.2079 . PMID   18981577.
  4. ↑ Stojnic N, Gojkovic-Bukarica L, Peric M, et al. (June 2007). "Potassium channel opener pinacidil induces relaxation of the isolated human radial artery". J. Pharmacol. Sci. 104 (2): 122–9. doi: 10.1254/jphs.FP0061434 . PMID   17538231.[ dead link ]
  5. ↑ Rundfeldt C (October 1997). "The new anticonvulsant retigabine (D-23129) acts as an opener of K+ channels in neuronal cells". European Journal of Pharmacology. 336 (2–3): 243–9. doi:10.1016/S0014-2999(97)01249-1. PMID   9384239.
  6. ↑ Main MJ, Cryan JE, Dupere JR, Cox B, Clare JJ, Burbidge SA (August 2000). "Modulation of KCNQ2/3 potassium channels by the novel anticonvulsant retigabine". Molecular Pharmacology. 58 (2): 253–62. doi:10.1124/mol.58.2.253. PMID   10908292. S2CID   11112809.
  7. 1 2 3 4 5 6 Enyedi P, Czirják G (Apr 2010). "Molecular background of leak K+ currents: two-pore domain potassium channels" (PDF). Physiological Reviews. 90 (2): 559–605. doi:10.1152/physrev.00029.2009. PMID   20393194. S2CID   9358238.
  8. 1 2 3 4 5 6 Lotshaw DP (2007). "Biophysical, pharmacological, and functional characteristics of cloned and native mammalian two-pore domain K+ channels". Cell Biochemistry and Biophysics . 47 (2): 209–56. doi:10.1007/s12013-007-0007-8. PMID   17652773. S2CID   12759521.
  9. 1 2 Fink M, Lesage F, Duprat F, Heurteaux C, Reyes R, Fosset M, Lazdunski M (Jun 1998). "A neuronal two P domain K+ channel stimulated by arachidonic acid and polyunsaturated fatty acids". The EMBO Journal. 17 (12): 3297–308. doi:10.1093/emboj/17.12.3297. PMC   1170668 . PMID   9628867.
  10. ↑ Goldstein SA, Bockenhauer D, O'Kelly I, Zilberberg N (Mar 2001). "Potassium leak channels and the KCNK family of two-P-domain subunits". Nature Reviews. Neuroscience. 2 (3): 175–84. doi:10.1038/35058574. PMID   11256078. S2CID   9682396.
  11. ↑ Sano Y, Inamura K, Miyake A, Mochizuki S, Kitada C, Yokoi H, Nozawa K, Okada H, Matsushime H, Furuichi K (Jul 2003). "A novel two-pore domain K+ channel, TRESK, is localized in the spinal cord". The Journal of Biological Chemistry. 278 (30): 27406–12. doi:10.1074/jbc.M206810200. PMID   12754259. S2CID   22656809.
  12. ↑ Czirják G, Tóth ZE, Enyedi P (Apr 2004). "The two-pore domain K+ channel, TRESK, is activated by the cytoplasmic calcium signal through calcineurin" (PDF). The Journal of Biological Chemistry. 279 (18): 18550–8. doi: 10.1074/jbc.M312229200 . PMID   14981085. S2CID   21219622.
  13. ↑ Meadows HJ, Randall AD (Mar 2001). "Functional characterisation of human TASK-3, an acid-sensitive two-pore domain potassium channel". Neuropharmacology. 40 (4): 551–9. doi:10.1016/S0028-3908(00)00189-1. PMID   11249964. S2CID   20181576.
  14. ↑ Patel AJ, Honoré E, Lesage F, Fink M, Romey G, Lazdunski M (May 1999). "Inhalational anesthetics activate two-pore-domain background K+ channels". Nature Neuroscience. 2 (5): 422–6. doi:10.1038/8084. PMID   10321245. S2CID   23092576.
  15. ↑ Gray AT, Zhao BB, Kindler CH, Winegar BD, Mazurek MJ, Xu J, Chavez RA, Forsayeth JR, Yost CS (Jun 2000). "Volatile anesthetics activate the human tandem pore domain baseline K+ channel KCNK5". Anesthesiology. 92 (6): 1722–30. doi:10.1097/00000542-200006000-00032. PMID   10839924. S2CID   45487917.
  16. ↑ Rogawski MA, Bazil CW (Jul 2008). "New molecular targets for antiepileptic drugs: alpha(2)delta, SV2A, and K(v)7/KCNQ/M potassium channels". Current Neurology and Neuroscience Reports. 8 (4): 345–52. doi:10.1007/s11910-008-0053-7. PMC   2587091 . PMID   18590620.
  17. ↑ Premoli I, Rossini PG, Goldberg PY, Posadas K, Green L, Yogo N, Pimstone S, Abela E, Beatch GN, Richardson MP (November 2019). "TMS as a pharmacodynamic indicator of cortical activity of a novel anti-epileptic drug, XEN1101". Annals of Clinical and Translational Neurology. 6 (11): 2164–2174. doi:10.1002/acn3.50896. PMC   6856596 . PMID   31568714. XEN1101 is a novel positive allosteric modulator ("opener") of the potassium channel KCNQ2/3 (Kv7.2/7.3) currently being developed by Xenon Pharmaceuticals Inc. for the treatment of focal epilepsy.


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