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Vol. 53, Issue 3, 497-503, March 1998
Department of Pharmacology and ESR Laboratory, Kanagawa Dental
College, Yokosuka, Kanagawa 238, Japan
The ryanodine receptor Ca2+ channel (RyRC) constitutes the
Ca2+-release pathway in sarcoplasmic reticulum (SR) of
cardiac muscle. A direct mechanical and a Ca2+-triggered
mechanism (Ca2+-induced Ca2+ release) have been
proposed to explain the in situ activation of
Ca2+ release in cardiac muscle. A variety of chemical
oxidants have been shown to activate RyRC; however, the role of
modification induced by oxygen-derived free radicals in pathological
states of the muscle remains to be elucidated. It has been hypothesized that oxygen-derived free radicals initiate Ca2+-mediated
functional changes in or damage to cardiac muscle by acting on the SR
and promoting an increase in Ca2+ release. We confirmed
that superoxide anion radical (O2
) generated from
hypoxanthine-xanthine oxidase reaction decreases calmodulin content and
increases 45Ca2+ efflux from the heavy fraction
of canine cardiac SR vesicles; hypoxanthine-xanthine oxidase also
decreases Ca2+ free within the intravesicular space of the
SR with no effect on Ca2+-ATPase activity. Current
fluctuations through single Ca2+-release channels have been
monitored after incorporation into planar phospholipid bilayers. We
demonstrate that activation of the channel by O2 is
dependent of the presence of calmodulin and identified calmodulin as a
functional mediator of O2-triggered Ca2+ release through the RyRC. For the first time, we show
that O2 stimulates Ca2+ release from
heavy SR vesicles and suggest the importance of accessory proteins such
as calmodulin in modulating the effect of O2. The
decreased calmodulin content induced by oxygen-derived free radicals,
especially O2, is a likely mechanism of
accumulation of cytosolic Ca2+ (due to increased
Ca2+ release from SR) after reperfusion of the ischemic
heart.
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