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J. Biol. Chem., Vol. 269, Issue 1, 192-198, 01, 1994
BR Fruen, JR Mickelson, NH Shomer, TJ Roghair and CF Louis
To better understand the mechanisms regulating myoplasmic Ca2+ during
muscle activity, we have examined the effect of inorganic phosphate (P(i))
on the ryanodine receptor (RyR) Ca2+ release channel of the sarcoplasmic
reticulum (SR). We report that P(i) at concentrations reached in exercising
skeletal muscle (3-30 mM) produced a dose- dependent stimulation of
ryanodine binding to skeletal muscle SR. Ryanodine binding was increased by
84% in the presence of 30 mM P(i) with half-maximal stimulation at 4 mM
P(i). In contrast to its effect on skeletal muscle SR, ryanodine binding to
cardiac muscle SR was not stimulated by P(i) (3-30 mM). Stimulation of
ryanodine binding to skeletal muscle SR was maximal in the presence of
micromolar Ca2+ and was associated with an increased affinity of the RyR
for ryanodine (Kd = 204 nM in the absence, versus 107 nM in the presence of
10 mM P(i)). P(i) (10 mM) also increased the rate of Ca2+ release from
45Ca(2+)- filled skeletal muscle SR vesicles by 50% in the presence of
micromolar Ca2+. Conversely, arsenate and sulfate (10 mM) had no effect on
either ryanodine binding or Ca(2+)-induced Ca2+ release, demonstrating the
specificity of the P(i) effect. Single-channel recordings of purified
skeletal muscle SR RyR incorporated into planar lipid bilayers showed that
addition of 10 mM P(i) to the cis chamber increased the open probability of
the channel by 91%. These results demonstrate that concentrations of P(i)
which occur in vivo during exercise significantly stimulate the in vitro
activity of the skeletal muscle RyR Ca2+ release channel.
Regulation of the sarcoplasmic reticulum ryanodine receptor by inorganic phosphate
Department of Veterinary PathoBiology, University of Minnesota, St. Paul 55108.
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