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J Biol Chem, Vol. 274, Issue 24, 17297-17308, June 11, 1999
From the We characterized type 3 ryanodine receptor (RyR3)
purified from rabbit diaphragm by immunoaffinity chromatography using a specific antibody. The purified receptor was free from 12-kDa FK506-binding protein, although it retained the ability to bind 12-kDa
FK506-binding protein. Negatively stained images of RyR3 show a
characteristic rectangular structure that was indistinguishable from
RyR1. The location of the D2 segment, which exists uniquely in the RyR1
isoform, was determined as the region around domain 9 close to the
corner of the square-shaped assembly, with use of D2-directed antibody
as a probe. The RyR3 homotetramer had a single class of high affinity
[3H]ryanodine-binding sites with a stoichiometry of
1 mol/mol. In planar lipid bilayers, RyR3 displayed cation channel
activity that was modulated by several ligands including
Ca2+, Mg2+, caffeine, and ATP, which is
consistent with [3H]ryanodine binding activity. RyR3
showed a slightly larger unit conductance and a longer mean open time
than RyR1. Whereas RyR1 showed two classes of channel activity with
distinct open probabilities (Po), RyR3
displayed a homogeneous and steeply
Ca2+-dependent activity with
Po ~1. RyR3 was more steeply affected in the
channel activity by sulfhydryl-oxidizing and -reducing reagents than
RyR1, suggesting that the channel activity of RyR3 may be transformed
more precipitously by the redox state. This is also a likely
explanation for the difference in the Ca2+ dependence of
RyR3 between [3H]ryanodine binding and channel activity.
Further Characterization of the Type 3 Ryanodine Receptor (RyR3)
Purified from Rabbit Diaphragm
,
,
,
, and
Department of Pharmacology,
Department of Fine Morphology,
Fujisawa Pharmaceutical Co. Ltd.,
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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