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(Received for publication, May 26, 1995; and in revised form, August 17, 1995) Hydrogen peroxide (H
Volume 270,
Number 43,
Issue of October 27, 1995 pp. 25557-25563
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Release Channel from Skeletal
Muscle Sarcoplasmic Reticulum
O) at millimolar
concentrations induces Ca release from actively
loaded sarcoplasmic reticulum vesicles and induces biphasic
[
H]ryanodine binding behavior. High affinity
[H]ryanodine binding is enhanced at
concentrations from 100 µM to 10 mM (3-4-fold). At HO concentrations
greater than 10 mM, equilibrium binding is inhibited.
HO decreased the k for [
H]ryanodine binding by increasing
its association rate, while having no effect on the rate of
dissociation of [H]ryanodine from its receptor.
HO (1 mM) also reduced the EC for Ca
activation from 632 nM to 335
nM. These effects were completely abolished in the presence of
catalase, ruthenium red, and/or Mg
(mM).
H
O-stimulated
[H]ryanodine binding is not further enhanced by
either doxorubicin or caffeine. The direct interaction between
HO and the Ca release
mechanism was further demonstrated in single-channel reconstitution
experiments. Peroxide, at submillimolar concentrations, activated the
Ca
release channel following fusion of a sarcoplasmic
reticulum vesicle to a bilayer lipid membrane. At millimolar
concentrations of peroxide, Ca
channel activity was
inhibited. Peroxide stimulation of Ca
channel
activity was reversed by the thiol reducing agent dithiothreitol.
Paralleling peroxide induced activation of ryanodine binding,
Ca
transport, and single Ca
channel
activity, it was observed that the ryanodine receptor formed large
disulfidelinked protein complexes that dissociated upon addition of
dithiothreitol.
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B. Aghdasi, J.-Z. Zhang, Y. Wu, M. B. Reid, and S. L. Hamilton Multiple Classes of Sulfhydryls Modulate the Skeletal Muscle Ca2+ Release Channel J. Biol. Chem., February 7, 1997; 272(6): 3739 - 3748. [Abstract] [Full Text] [PDF]
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R. Xia, T. Stangler, and J. J. Abramson Skeletal Muscle Ryanodine Receptor Is a Redox Sensor with a Well Defined Redox Potential That Is Sensitive to Channel Modulators J. Biol. Chem., November 17, 2000; 275(47): 36556 - 36561. [Abstract] [Full Text] [PDF]
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