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J Biol Chem, Vol. 274, Issue 24, 17297-17308, June 11, 1999

Further Characterization of the Type 3 Ryanodine Receptor (RyR3) Purified from Rabbit Diaphragm

Takashi Murayama, Toshiharu Oba^¶, Eisaku Katayama, Hideto Oyamada^**, Katsuji Oguchi^**, Masakazu Kobayashi, Kazuyuki Otsuka, and Yasuo Ogawa

From the  Department of Pharmacology, Juntendo University School of Medicine, Tokyo 113-8421, the ^¶ Department of Physiology, Nagoya City University Medical School, Nagoya 467-8601, the  Department of Fine Morphology, Institute of Medical Science, The University of Tokyo, Tokyo 108-8639, ^** Department of Pharmacology, School of Medicine, Showa University, Tokyo 142-8555, and  Fujisawa Pharmaceutical Co. Ltd., Osaka 541-8541, Japan

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 (P_o), RyR3 displayed a homogeneous and steeply Ca²⁺-dependent activity with P_o ~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.

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