Short- and Long-Term Functional Alterations of the Skeletal Muscle Calcium Release Channel (Ryanodine Receptor) by Suramin: Apparent Dissociation of Single Channel Current Recording and [3H]Ryanodine Binding

2001 ◽  
Vol 59 (3) ◽  
pp. 543-556 ◽  
Author(s):  
Josef Suko ◽  
Gertrude Hellmann ◽  
Helmut Drobny
Keyword(s):  
Skeletal Muscle ◽  
Calcium Release ◽  
Single Channel ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Channel Current ◽  
Single Channel Current ◽  
Short And Long Term ◽  
Muscle Calcium

Electron cryomicroscopy and angular reconstitution used to visualize the skeletal muscle calcium release channel

1995 ◽  
Vol 2 (1) ◽  
pp. 18-24 ◽  
Author(s):  
Irina I. Serysheva ◽  
Elena V. Orlova ◽  
Wah Chiu ◽  
Michael B. Sherman ◽  
Susan L. Hamilton ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Calcium Release ◽  
Electron Cryomicroscopy ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Muscle Calcium

scholarly journals Chloroform extract of hog barn dust modulates skeletal muscle ryanodine receptor calcium-release channel (RyR1)

2010 ◽  
Vol 109 (3) ◽  
pp. 830-839 ◽  
Author(s):  
Chengju Tian ◽  
Chun Hong Shao ◽  
Danielle S. Fenster ◽  
Mark Mixan ◽  
Debra J. Romberger ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Ryanodine Receptor ◽  
Muscle Weakness ◽  
Calcium Release ◽  
Single Channel ◽  
Calcium Release Channel ◽  
Open Probability ◽  
Skeletal Muscle Function ◽  
Release Channel ◽  
Skeletal Muscle Weakness

Skeletal muscle weakness is a reported ailment in individuals working in commercial hog confinement facilities. To date, specific mechanisms responsible for this symptom remain undefined. The purpose of this study was to assess whether hog barn dust (HBD) contains components that are capable of binding to and modulating the activity of type 1 ryanodine receptor Ca2+-release channel (RyR1), a key regulator of skeletal muscle function. HBD collected from confinement facilities in Nebraska were extracted with chloroform, filtered, and rotary evaporated to dryness. Residues were resuspended in hexane-chloroform (20:1) and precipitates, referred to as HBDorg, were air-dried and studied further. In competition assays, HBDorg dose-dependently displaced [3H]ryanodine from binding sites on RyR1 with an IC50 of 1.5 ± 0.1 μg/ml ( Ki = 0.4 ± 0.0 μg/ml). In single-channel assays using RyR1 reconstituted into a lipid bilayer, HBDorg exhibited three distinct dose-dependent effects: first it increased the open probability of RyR1 by increasing its gating frequency and dwell time in the open state, then it induced a state of reduced conductance (55% of maximum) that was more likely to occur and persist at positive holding potentials, and finally it irreversibly closed RyR1. In differentiated C2C12 myotubes, addition of HBD triggered a rise in intracellular Ca2+ that was blocked by pretreatment with ryanodine. Since persistent activation and/or closure of RyR1 results in skeletal muscle weakness, these new data suggest that HBD is responsible, at least in part, for the muscle ailment reported by hog confinement workers.

scholarly journals Single channel measurements of the calcium release channel from skeletal muscle sarcoplasmic reticulum. Activation by Ca2+ and ATP and modulation by Mg2+.

1986 ◽  
Vol 88 (5) ◽  
pp. 573-588 ◽  
Author(s):  
J S Smith ◽  
R Coronado ◽  
G Meissner
Keyword(s):  
Skeletal Muscle ◽  
Sarcoplasmic Reticulum ◽  
Lipid Bilayers ◽  
Calcium Release ◽  
Single Channel ◽  
Ca Channel ◽  
Channel Measurements ◽  
Calcium Release Channel ◽  
Open Probability ◽  
Release Channel

A high-conductance (100 pS in 53 mM trans Ca2+) Ca2+ channel was incorporated from heavy-density skeletal muscle sarcoplasmic reticulum (SR) fractions into planar lipid bilayers of the Mueller-Rudin type. cis Ca2+ in the range of 2-950 microM increased open probability (Po) in single channel records without affecting open event lifetimes. Millimolar ATP was found to be as good as or better than Ca2+ in activation; however, both Ca2+ and ATP were required to fully activate the channel, i.e., to bring Po = 1. Exponential fits to open and closed single channel lifetimes suggested that the channel may exist in many distinct states. Two open and two closed states were identified when the channel was activated by either Ca2+ or ATP alone or by Ca2+ plus nucleotide. Mg2+ was found to permeate the SR Ca channel in a trans-to-cis direction such that iMg2+/iCa2+ = 0.40. cis Mg2+ was inhibitory and in single channel recordings produced an unresolvable flickering of Ca- and nucleotide-activated channels. At nanomolar cis Ca2+, 4 microM Mg2+ completely inhibited nucleotide-activated channels. In the presence of 2 microM cis Ca2+, the nucleotide-activated macroscopic Ba conductance was inhibited by cis Mg2+ with an IC50 equal to 1.5 mM.

scholarly journals The Skeletal Muscle Calcium Release Channel

Cell ◽  
2000 ◽  
Vol 102 (4) ◽  
pp. 499-509 ◽  
Author(s):  
Jerry P Eu ◽  
Junhui Sun ◽  
Le Xu ◽  
Jonathan S Stamler ◽  
Gerhard Meissner
Keyword(s):  
Skeletal Muscle ◽  
Calcium Release ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Muscle Calcium

Two structural configurations of the skeletal muscle calcium release channel

1996 ◽  
Vol 3 (6) ◽  
pp. 547-552 ◽  
Author(s):  
Elena V. Orlova ◽  
Irina I. Serysheva ◽  
Marin van Heel ◽  
Susan L. Hamilton ◽  
Wah Chiu
Keyword(s):  
Skeletal Muscle ◽  
Calcium Release ◽  
Calcium Release Channel ◽  
Release Channel ◽  
Structural Configurations ◽  
Muscle Calcium
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