Similar Ca2+ dependences of [3H]ryanodine binding to α‐ and β‐ryanodine receptors purified from bullfrog skeletal muscle in an isotonic medium

FEBS Letters

Ogawa, Yasuo¹  Murayama, Takashi¹ 

[1] Department of Pharmacology, Juntendo University School of Medicine, 2-1-1 Hongo, Bunkyo-ku, Tokyo 113, Japan

关键词: Calcium ion dependence;    Calcium ion release;    Excitation-contraction coupling;    Ryanodine receptor;    Sarcoplasmic reticulum;    Skeletal muscle (bullfrog);    AMPOPCP;    β;    γ-methylene adenosine triphosphate;    CHAPS;    3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate;    CICR;    Ca2+-induced Ca2+ release;    DICR;    depolarization-induced Ca2+ release;    EGTA;    ethylene glycol bis (β-aminoethyl ether)-N;    N;    N′;    N′-tetraacetic acid;    MOPSO;    3-(N-morpholino)-2-hydroxypropanesulfonic acid;    RyR;    ryanodine receptor;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;    SR;    sarcoplasmic reticulum;   

DOI  :  10.1016/0014-5793(96)00053-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

To understand the functions of the two ryanodine receptor isoforms (α- and β-RyRs) in nonmammalian skeletal muscles, we determined [³H]ryanodine binding to these isoforms purified from bullfrog skeletal muscle. In 0.17 M-NaCl medium, both isoforms demonstrated similar Ca²⁺ dependent ryanodine binding activities, while the Ca²⁺ sensitivity for activation of β-RyR was increased in 1 M-NaCl medium. This enhancement in Ca²⁺ sensitivity depended on the kind of salts used. These results imply that α- and β-RyRs may have similar properties as Ca²⁺-induced Ca²⁺ release channels in bullfrog skeletal muscle.

【 授权许可】

Unknown