KCNH1
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Potassium voltage-gated channel subfamily H member 1 is a protein that in humans is encoded by the KCNH1 gene.[4][5][6]
Voltage-gated potassium (Kv) channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. This gene encodes a member of the potassium channel, voltage-gated, subfamily H. This member is a pore-forming (alpha) subunit of a voltage-gated non-inactivating delayed rectifier potassium channel. It is activated at the onset of myoblast differentiation. The gene is highly expressed in brain and in myoblasts. Overexpression of the gene may confer a growth advantage to cancer cells and favor tumor cell proliferation. Alternative splicing of this gene results in two transcript variants encoding distinct isoforms.[6]
Interactions
KCNH1 has been shown to interact with KCNB1.[7]
See also
References
- ↑ "Drugs that physically interact with Potassium voltage-gated channel subfamily H member 1 view/edit references on wikidata".
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- ↑ Occhiodoro T, Bernheim L, Liu JH, Bijlenga P, Sinnreich M, Bader CR, Fischer-Lougheed J (Sep 1998). "Cloning of a human ether-a-go-go potassium channel expressed in myoblasts at the onset of fusion". FEBS Lett. 434 (1–2): 177–82. doi:10.1016/S0014-5793(98)00973-9. PMID 9738473.
- ↑ Gutman GA, Chandy KG, Grissmer S, Lazdunski M, McKinnon D, Pardo LA, Robertson GA, Rudy B, Sanguinetti MC, Stuhmer W, Wang X (Dec 2005). "International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels". Pharmacol Rev. 57 (4): 473–508. doi:10.1124/pr.57.4.10. PMID 16382104.
- 1 2 "Entrez Gene: KCNH1 potassium voltage-gated channel, subfamily H (eag-related), member 1".
- ↑ Ottschytsch, N; Raes A; Van Hoorick D; Snyders D J (Jun 2002). "Obligatory heterotetramerization of three previously uncharacterized Kv channel α-subunits identified in the human genome". Proc. Natl. Acad. Sci. U.S.A. United States. 99 (12): 7986–91. doi:10.1073/pnas.122617999. ISSN 0027-8424. PMC 123007. PMID 12060745.
Further reading
- Warmke JW, Ganetzky B (1994). "A family of potassium channel genes related to eag in Drosophila and mammals". Proc. Natl. Acad. Sci. U.S.A. 91 (8): 3438–42. doi:10.1073/pnas.91.8.3438. PMC 43592. PMID 8159766.
- Hoshi N, Takahashi H, Shahidullah M, et al. (1998). "KCR1, a membrane protein that facilitates functional expression of non-inactivating K+ currents associates with rat EAG voltage-dependent K+ channels". J. Biol. Chem. 273 (36): 23080–5. doi:10.1074/jbc.273.36.23080. PMID 9722534.
- Pardo LA, del Camino D, Sánchez A, et al. (1999). "Oncogenic potential of EAG K(+) channels". EMBO J. 18 (20): 5540–7. doi:10.1093/emboj/18.20.5540. PMC 1171622. PMID 10523298.
- Schönherr R, Löber K, Heinemann SH (2000). "Inhibition of human ether à go-go potassium channels by Ca2+/calmodulin". EMBO J. 19 (13): 3263–71. doi:10.1093/emboj/19.13.3263. PMC 313935. PMID 10880439.
- Cayabyab FS, Schlichter LC (2002). "Regulation of an ERG K+ current by Src tyrosine kinase". J. Biol. Chem. 277 (16): 13673–81. doi:10.1074/jbc.M108211200. PMID 11834728.
- Schönherr R, Gessner G, Löber K, Heinemann SH (2002). "Functional distinction of human EAG1 and EAG2 potassium channels". FEBS Lett. 514 (2–3): 204–8. doi:10.1016/S0014-5793(02)02365-7. PMID 11943152.
- Ottschytsch N, Raes A, Van Hoorick D, Snyders DJ (2002). "Obligatory heterotetramerization of three previously uncharacterized Kv channel α-subunits identified in the human genome". Proc. Natl. Acad. Sci. U.S.A. 99 (12): 7986–91. doi:10.1073/pnas.122617999. PMC 123007. PMID 12060745.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Farias LM, Ocaña DB, Díaz L, et al. (2004). "Ether a go-go potassium channels as human cervical cancer markers". Cancer Res. 64 (19): 6996–7001. doi:10.1158/0008-5472.CAN-04-1204. PMID 15466192.
- Kang J, Chen XL, Wang H, et al. (2005). "Discovery of a small molecule activator of the human ether-a-go-go-related gene (HERG) cardiac K+ channel". Mol. Pharmacol. 67 (3): 827–36. doi:10.1124/mol.104.006577. PMID 15548764.
- Ziechner U, Schönherr R, Born AK, et al. (2006). "Inhibition of human ether à go-go potassium channels by Ca2+/calmodulin binding to the cytosolic N- and C-termini". FEBS J. 273 (5): 1074–86. doi:10.1111/j.1742-4658.2006.05134.x. PMID 16478480.
- Weber C, Mello de Queiroz F, Downie BR, et al. (2006). "Silencing the activity and proliferative properties of the human EagI Potassium Channel by RNA Interference". J. Biol. Chem. 281 (19): 13030–7. doi:10.1074/jbc.M600883200. PMID 16537547.
- Mello de Queiroz F, Suarez-Kurtz G, Stühmer W, Pardo LA (2006). "Ether à go-go potassium channel expression in soft tissue sarcoma patients". Mol. Cancer. 5: 42. doi:10.1186/1476-4598-5-42. PMC 1618397. PMID 17022811.
- Ocorr K, Reeves NL, Wessells RJ, et al. (2007). "KCNQ potassium channel mutations cause cardiac arrhythmias in Drosophila that mimic the effects of aging". Proc. Natl. Acad. Sci. U.S.A. 104 (10): 3943–8. doi:10.1073/pnas.0609278104. PMC 1820688. PMID 17360457.
- Ding XW, Yan JJ, An P, et al. (2007). "Aberrant expression of ether à go-go potassium channel in colorectal cancer patients and cell lines". World J. Gastroenterol. 13 (8): 1257–61. doi:10.3748/wjg.v13.i8.1257. PMID 17451210.
- Borowiec AS, Hague F, Harir N, et al. (2007). "IGF-1 activates hEAG K(+) channels through an Akt-dependent signaling pathway in breast cancer cells: role in cell proliferation". J. Cell. Physiol. 212 (3): 690–701. doi:10.1002/jcp.21065. PMID 17520698.
External links
- KCNH1 protein, human at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.