1. Unidirectional K+ (86Rb) influx in lamprey red blood cells was studied under different conditions. 2. The influx of 86Rb was markedly inhibited by 1 mM Ba2+ when cells were incubated in saline containing 4 mM K+. In K(+)-free media, the influx rate constant of 86Rb was lower, and 1 mM Ba2+ had no blocking effect. 3. Treatment of the red cells with 0.1 mM ouabain in the absence of external K+ resulted in the appearance of the component of 86Rb influx inhibited by 1 mM Ba2+, quinine, TEA or amiloride. 4. Similar results were obtained in red cells incubated in Na(+)-free media MgCl2-sucrose. 5. The results obtained provide evidence for the existence of K+ channels in the red cell membrane of the lamprey. Under physiological conditions (in the presence of 4 mM K+) the total rate constant for the 86Rb influx in erythrocytes was about 1.9/hr, including ouabain-sensitive (0.6/hr), Ba(2+)-sensitive (1.1/hr) and residual (0.2/hr) components.
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http://dx.doi.org/10.1016/0300-9629(92)90510-w | DOI Listing |
Channels (Austin)
December 2019
From the Département de pharmacologie et physiologie, Faculté de médecine, Université de Montréal, Montréal , Canada.
Atomic resolution structures have provided significant insight into the gating and permeation mechanisms of various ion channels, including potassium channels. However, ion channels may also be regulated by numerous factors, including the physiochemical properties of the membrane in which they are embedded. For example, the matching of the bilayer's hydrophobic region to the hydrophobic external surface of the ion channel is thought to minimize the energetic penalty needed to solvate hydrophobic residues or exposed lipid tails.
View Article and Find Full Text PDFBiochem Biophys Rep
December 2017
Faculty of Biology MV Lomonosov Moscow State University, Leninskiye gory 1/12, Moscow 119991, Russia.
Objectives: This study examined the dose-dependent actions of hydrogen sulfide donor sodium hydrosulphide (NaHS) on isometric contractions and ion transport in rat aorta smooth muscle cells (SMC).
Methods: Isometric contraction was measured in ring aortas segments from male Wistar rats. Activity of Na/K-pump and Na,K,2Clcotransport was measured in cultured endothelial and smooth muscle cells from the rat aorta as ouabain-sensitive and ouabain-resistant, bumetanide-sensitive components of the Rb influx, respectively.
Methods Mol Biol
June 2018
Red Blood Cell Research Group, Institute of Veterinary Physiology, Vetsuisse Faculty, University of Zurich, Winterthurerstrasse 260, CH-8057, Zurich, Switzerland.
Abundance and activity of N-methyl-D-aspartate (NMDA) in circulating red blood cells contributes to the maintenance of intracellular Ca in these cells and, by doing that, controls red cell volume, membrane stability, and O carrying capacity. Detection of the NMDA receptor activity in red blood cells is challenging as the number of its copies is low and shows substantial cell-to-cell heterogeneity. Receptor abundance is reliably assessed using the radiolabeled antagonist ([H]MK-801) binding technique.
View Article and Find Full Text PDFBiochemistry (Mosc)
August 2016
Lomonosov Moscow State University, Faculty of Biology, Moscow, 119991, Russia.
Side-by-side with inhibition of the Na+,K+-ATPase ouabain and other cardiotonic steroids (CTS) can affect cell functions by mechanisms other than regulation of the intracellular Na+ and K+ ratio ([Na+]i/[K+]i). Thus, we compared the dose- and time-dependences of the effect of ouabain on intracellular [Na+]i/[K+]i ratio, Na+,K+-ATPase activity, and proliferation of human umbilical vein endothelial cells (HUVEC). Treatment of the cells with 1-3 nM ouabain for 24-72 h decreased the [Na+]i/[K+]i ratio and increased cell proliferation by 20-50%.
View Article and Find Full Text PDFBiochem J
March 2014
*MRC Protein Phosphorylation and Ubiquitylation Unit, College of Life Sciences, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, U.K.
Precise homoeostasis of the intracellular concentration of Cl- is achieved via the co-ordinated activities of the Cl- influx and efflux. We demonstrate that the WNK (WNK lysine-deficient protein kinase)-activated SPAK (SPS1-related proline/alanine-rich kinase)/OSR1 (oxidative stress-responsive kinase 1) known to directly phosphorylate and stimulate the N[K]CCs (Na+-K+ ion co-transporters), also promote inhibition of the KCCs (K+-Cl- co-transporters) by directly phosphorylating a recently described C-terminal threonine residue conserved in all KCC isoforms [Site-2 (Thr1048)]. First, we demonstrate that SPAK and OSR1, in the presence of the MO25 regulatory subunit, robustly phosphorylates all KCC isoforms at Site-2 in vitro.
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