By Kirk L. Hamilton, Daniel C Devor
This booklet sheds new mild at the body structure, molecular biology and pathophysiology of epithelial ion channels and transporters. It combines the elemental mobile versions and capabilities by way of a compelling medical point of view, addressing points from the laboratory bench to the bedside. the person chapters, written through major scientists and clinicians, discover particular ion channels and transporters positioned within the epithelial tissues of the kidney, gut, pancreas and respiration tract, all of which play a vital half in holding homeostasis. extra subject matters comprise the basics of epithelial delivery; mathematical modeling of ion delivery; phone quantity rules; membrane protein folding and trafficking; transepithelial delivery services; and finally, a dialogue of shipping proteins as strength pharmacological objectives with a spotlight at the pharmacology of potassium channels.
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This e-book sheds new mild at the body structure, molecular biology and pathophysiology of epithelial ion channels and transporters. It combines the fundamental mobile types and services via a compelling scientific standpoint, addressing elements from the laboratory bench to the bedside. the person chapters, written via top scientists and clinicians, discover particular ion channels and transporters situated within the epithelial tissues of the kidney, gut, pancreas and respiration tract, all of which play an important half in conserving homeostasis.
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Additional resources for Ion Channels and Transporters of Epithelia in Health and Disease
1996) characterized clotrimazole as a blocker of Ca2+mediated ClÀ secretion and that this effect was due to block of a basolateral K+ conductance. Devor et al. (1997) subsequently conﬁrmed that this was due to a direct inhibition of the charybdotoxin-sensitive basolateral K+ channel (see Chap. 20 for additional details). The use of these pharmacological tools unequivocally demonstrated that cAMP- and Ca2+-mediated agonists activate unique basolateral membrane K+ channels and played a pivotal role in conﬁrming their molecular identities.
However, given the intermediate conductance of the channel, based on historical precedence, Ishii et al. (1997) referred to this channel as IK1. Based on the standard nomenclature derived from the International Union of Pharmacology (IUPHAR; (Gutman et al. 1. These channels were posited to have 6 transmembrane domains (S1–S6), with the reentrant pore loop between S5 and S6 and cytosolic N- and C-termini. Joiner et al. (1997) and Ishii et al. 1 was activated by Ca2+ and was blocked by charybdotoxin and clotrimazole while being insensitive to blockers of Maxi-K and small conductance K+ channels, similar to what had been reported for the endogenously expressed basolateral membrane, Ca2+-activated K+ channel of epithelia.
J Biol Chem 288:36841–36854. 525931 Anderson MP, Welsh MJ (1992) Regulation by ATP and ADP of CFTR chloride channels that contain mutant nucleotide-binding domains. Science 257:1701–1704 Anderson MP, Berger HA, Rich DP, Gregory RJ, Smith AE, Welsh MJ (1991a) Nucleoside triphosphates are required to open the CFTR chloride channel. Cell 67:775–784 Anderson MP, Gregory RJ, Thompson S, Souza DW, Paul S, Mulligan RC, Smith AE, Welsh MJ (1991b) Demonstration that CFTR is a chloride channel by alteration of its anion selectivity.
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