K channels are involved in many critical functions in lung physiology. Recently, the family of Ca-activated K channels (K) has received more attention, and a massive amount of effort has been devoted to developing selective medications targeting these channels. Within the family of K channels, three small-conductance Ca-activated K (K2) channel subtypes, together with the intermediate-conductance K3.1 channel, are voltage-independent K channels, and they mediate Ca-induced membrane hyperpolarization. Many K2 channel members are involved in crucial roles in physiological and pathological systems throughout the body. In this article, different subtypes of K2 and K3.1 channels and their functions in respiratory diseases are discussed. Additionally, the pharmacology of the K2 and K3.1 channels and the link between these channels and respiratory ciliary regulations will be explained in more detail. In the future, specific modulators for small or intermediate Ca-activated K channels may offer a unique therapeutic opportunity to treat muco-obstructive lung diseases.
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http://dx.doi.org/10.3390/biomedicines11071780 | DOI Listing |
J Phys Chem A
November 2011
Radiation & Photochemistry Division, Bhabha Atomic Research Centre, Trombay, Mumbai, India.
The formation of cadmium selenide, CdSe, nanoparticles in aqueous solutions containing equimolar ammoniated cadmium sulfate, [Cd(NH(3))](4)SO(4) and sodium selenosulfate, Na(2)SeSO(3) as the starting materials, has been investigated by electron pulse radiolysis coupled with kinetic spectrometry. The formation of CdSe nanoparticles was found to proceed through the generation of short-lived transient intermediate species having an absorption peak at 520 nm, which is formed only upon the reaction of hydrated electrons, e(aq) with the precursor ions under deaerated conditions. The transient intermediate species decays with a weighted average rate constant, 1.
View Article and Find Full Text PDFJ Phys Chem A
November 2009
Departments of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
J Biol Chem
December 2005
Department of Pharmacology, University of Washington, Seattle, Washington 98195, USA.
Tyrosine phosphorylation is an important means of regulating ion channel function. Our previous gene expression studies using the Xenopus laevis oocyte system suggested that tyrosine phosphorylation of G-protein-gated inwardly rectifying potassium channels (K(ir)3 or GIRK) suppressed basal channel conductance and accelerated channel deactivation. To assess whether similar mechanisms regulate K(ir)3 function in mammalian cells, we developed and characterized a phosphoselective antibody recognizing K(ir)3.
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March 1999
CEA, Département d'Ingénierie et d'Etudes des Protéines, Gif-sur-Yvette, France.
Calcicludine, a 60-amino acid protein isolated from the green mamba venom, has been recently identified as blocking a large set (i.e., L-, N- and P-type) of Ca2+ channels.
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March 1999
Architecture et Fonction des Macromolécules Biologiques, Centre National de la Recherche Scientifique, UPR 9039, Marseille, France.
Lq2 is a unique scorpion toxin. Acting from the extracellular side, Lq2 blocks the ion conduction pore in not only the voltage- and Ca2+ -activated channels, but also the inward-rectifier K+ channels. This finding argues that the three-dimensional structures of the pores in these K+ channels are similar.
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