In today's article we will talk about KCNK3, a topic that has gained great relevance in recent times. From its origins to its impact on today's society, KCNK3 has been the object of study and interest for numerous experts in different fields. Throughout history, KCNK3 has experienced various changes and transformations that have marked its evolution and its influence on people's lives. Therefore, it is important to stop and analyze in detail what KCNK3 is, what its importance is and how it has affected different areas of daily life. Through this article, we will delve into the exciting world of KCNK3 to better understand its meaning and its impact on today's society.
Potassium channel subfamily K member 3 is a protein that in humans is encoded by the KCNK3gene.[5][6][7][8]
This gene encodes K2P3.1, one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. K2P3.1 is an outwardly rectifying channel that is sensitive to changes in extracellular pH and is inhibited by extracellular acidification. Also referred to as an acid-sensitive potassium channel, it is activated by the anesthetics halothane and isoflurane. Although three transcripts are detected in northern blots, there is currently no sequence available to confirm transcript variants for this gene.[8]
Interactive pathway map
Click on genes, proteins and metabolites below to link to respective articles.[§ 1]
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^Lesage F, Lazdunski M (Oct 1998). "Mapping of human potassium channel genes TREK-1 (KCNK2) and TASK (KCNK3) to chromosomes 1q41 and 2p23". Genomics. 51 (3): 478–9. doi:10.1006/geno.1998.5397. PMID9721223.
Buist SC, Cherrington NJ, Choudhuri S, et al. (2002). "Gender-specific and developmental influences on the expression of rat organic anion transporters". J. Pharmacol. Exp. Ther. 301 (1): 145–51. doi:10.1124/jpet.301.1.145. PMID11907168.
Barbuti A, Ishii S, Shimizu T, et al. (2002). "Block of the background K(+) channel TASK-1 contributes to arrhythmogenic effects of platelet-activating factor". Am. J. Physiol. Heart Circ. Physiol. 282 (6): H2024–30. doi:10.1152/ajpheart.00956.2001. PMID12003807.
Aslamkhan A, Han YH, Walden R, et al. (2003). "Stoichiometry of organic anion/dicarboxylate exchange in membrane vesicles from rat renal cortex and hOAT1-expressing cells". Am. J. Physiol. Renal Physiol. 285 (4): F775–83. doi:10.1152/ajprenal.00140.2003. PMID12837685.
Bai X, Greenwood SL, Glazier JD, et al. (2005). "Localization of TASK and TREK, two-pore domain K+ channels, in human cytotrophoblast cells". J. Soc. Gynecol. Investig. 12 (2): 77–83. doi:10.1016/j.jsgi.2004.08.004. PMID15695101. S2CID20173840.