Single-channel recordings of chloride currents in primary culturedDrosophila neurons

1987 ◽  
Vol 6 (3) ◽  
pp. 151-158 ◽  
Author(s):  
Daisuke Yamamoto ◽  
Nobuyuki Suzuki
Keyword(s):  
Single Channel ◽  
Chloride Currents ◽  
Single Channel Recordings

Mechanically Stable Lipid Bilayers in Teflon-Coated Silicon Chips for Single-Channel Recordings

2012 ◽  
Vol 4 (1) ◽  
pp. 2-7 ◽  
Author(s):  
Azusa Oshima ◽  
Ayumi Hirano-Iwata ◽  
Tomohiro Nasu ◽  
Yasuo Kimura ◽  
Michio Niwano
Keyword(s):  
Lipid Bilayers ◽  
Single Channel ◽  
Single Channel Recordings ◽  
Silicon Chips

Ryanodine receptor dysfunction in porcine stunned myocardium

1997 ◽  
Vol 273 (2) ◽  
pp. H796-H804 ◽  
Author(s):  
C. Valdivia ◽  
J. O. Hegge ◽  
R. D. Lasley ◽  
H. H. Valdivia ◽  
R. Mentzer
Keyword(s):  
Coronary Artery ◽  
Lipid Bilayers ◽  
Ryanodine Receptor ◽  
Myocardial Stunning ◽  
Single Channel ◽  
Stunned Myocardium ◽  
Wall Thickening ◽  
Planar Lipid Bilayers ◽  
Open Probability ◽  
Single Channel Recordings

We investigated the effects of myocardial stunning on the function of the two main Ca2+ transport proteins of the sarcoplasmic reticulum (SR), the Ca(2+)-adenosinetriphosphatase and the Ca(2+)-release channel or ryanodine receptor. Regional myocardial stunning was induced in open-chest pigs (n = 6) by a 10-min occlusion of the left anterior descending coronary artery (LAD) and 2 h reperfusion. SR vesicles isolated from the LAD-perfused region (stunned) and the normal left circumflex coronary artery (LC)-perfused region were used to assess the oxalate-supported 45Ca2+ uptake, [3H]ryanodine binding, and single-channel recordings of ryanodine-sensitive Ca(2+)-release channels in planar lipid bilayers. Myocardial stunning decreased LAD systolic wall thickening to 20% of preischemic values. The rate of SR 45Ca2+ uptake in the stunned LAD bed was reduced by 37% compared with that of the normal LC bed (P < 0.05). Stunning was also associated with a 38% reduction in the maximal density of high-affinity [3H]ryanodine binding sites (P < 0.05 vs. normal LC) but had no effect on the dissociation constant. The open probability of ryanodine-sensitive Ca(2+)-release channels determined by single channel recordings in planar lipid bilayers was 26 +/- 2% for control SR (n = 33 channels from 3 animals) and 14 +/- 2% for stunned SR (n = 21 channels; P < 0.05). This depressed activity of SR function observed in postischemic myocardium could be one of the mechanisms underlying myocardial stunning.

Single-channel recordings from purified acetylcholine receptors reconstituted in bilayers formed at the tip of patch pipets

Biochemistry ◽  
1983 ◽  
Vol 22 (10) ◽  
pp. 2319-2323 ◽  
Author(s):  
Benjamin A. Suarez-Isla ◽  
Kee Wan ◽  
Jon Lindstrom ◽  
Mauricio Montal
Keyword(s):  
Acetylcholine Receptors ◽  
Single Channel ◽  
Single Channel Recordings

scholarly journals A central core disease mutation in the Ca2+-binding site of skeletal muscle ryanodine receptor impairs single-channel regulation

2019 ◽  
Vol 317 (2) ◽  
pp. C358-C365 ◽  
Author(s):  
Venkat R. Chirasani ◽  
Le Xu ◽  
Hannah G. Addis ◽  
Daniel A. Pasek ◽  
Nikolay V. Dokholyan ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Missense Mutation ◽  
Ryanodine Receptor ◽  
Single Channel ◽  
Central Core ◽  
Central Core Disease ◽  
Hek293 Cells ◽  
Amino Acid Residues ◽  
Single Channel Recordings

Cryoelectron microscopy and mutational analyses have shown that type 1 ryanodine receptor (RyR1) amino acid residues RyR1-E3893, -E3967, and -T5001 are critical for Ca2+-mediated activation of skeletal muscle Ca2+ release channel. De novo missense mutation RyR1-Q3970K in the secondary binding sphere of Ca2+ was reported in association with central core disease (CCD) in a 2-yr-old boy. Here, we characterized recombinant RyR1-Q3970K mutant by cellular Ca2+ release measurements, single-channel recordings, and computational methods. Caffeine-induced Ca2+ release studies indicated that RyR1-Q3970K formed caffeine-sensitive, Ca2+-conducting channel in HEK293 cells. However, in single-channel recordings, RyR1-Q3970K displayed low Ca2+-dependent channel activity and greatly reduced activation by caffeine or ATP. A RyR1-Q3970E mutant corresponds to missense mutation RyR2-Q3925E associated with arrhythmogenic syndrome in cardiac muscle. RyR1-Q3970E also formed caffeine-induced Ca2+ release in HEK293 cells and exhibited low activity in the presence of the activating ligand Ca2+ but, in contrast to RyR1-Q3970K, was activated by ATP and caffeine in single-channel recordings. Computational analyses suggested distinct structural rearrangements in the secondary binding sphere of Ca2+ of the two mutants, whereas the interaction of Ca2+ with directly interacting RyR1 amino acid residues Glu3893, Glu3967, and Thr5001 was only minimally affected. We conclude that RyR1-Q3970 has a critical role in Ca2+-dependent activation of RyR1 and that a missense RyR1-Q3970K mutant may give rise to myopathy in skeletal muscle.

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