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Research ArticleArticle

Xestoquinone, Isolated from Sea Sponge, Causes Ca2+Release through Sulfhydryl Modification from Skeletal Muscle Sarcoplasmic Reticulum

Masaaki Ito, Yutaka Hirata, Hideshi Nakamura and Yasushi Ohizumi
Journal of Pharmacology and Experimental Therapeutics December 1999, 291 (3) 976-981;
Masaaki Ito
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Yutaka Hirata
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Hideshi Nakamura
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Yasushi Ohizumi
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Abstract

Xestoquinone (XQN) (3 × 10−7 to 3 × 10−3 M), isolated from the sea sponge Xestospongia sapra, induced a concentration-dependent Ca2+release from the heavy fraction of fragmented sarcoplasmic reticulum (HSR) of rabbit skeletal muscle with an EC50 value of ∼30 μM. On the basis of the EC50, XQN is 10 times more potent than caffeine. Dithiothreitol completely blocked XQN-induced Ca2+ release from HSR without affecting that induced by caffeine. Caffeine-induced Ca2+ release was reduced markedly by Mg2+, procaine, and ruthenium red, agents that are known to block release of Ca2+ from sarcoplasmic reticulum, whereas that induced by XQN was not inhibited. The bell-shaped profile of Ca2+ dependence for XQN was significantly shifted upward in a wider range of pCa (between 7 and 3), whereas that for caffeine was shifted to the left in a narrower range of pCa (between 8 and 7). The maximum response to caffeine in45Ca2+ release was not affected by 9-methyl-7-bromoeudistomin D, whereas the response was further increased by XQN. XQN caused a concentration-dependent decrease in [3H]ryanodine binding to HSR. This effect of XQN also was abolished in the presence of dithiothreitol. Scatchard analysis revealed that the mode of inhibition by XQN was noncompetitive in [3H]ryanodine binding to HSR. These results indicate that sulfhydryl groups are involved in both the XQN effect on ryanodine binding and on Ca2+ release.

Footnotes

  • Send reprint requests to: Yasushi Ohizumi, Ph.D, Department of Pharmaceutical Molecular Biology, Faculty of Pharmaceutical Sciences, Tohoku University, Aoba, Aramaki, Aoba-ku, Sendai 980-8578, Japan. E-mail: ohizumi{at}mail.pharm.tohoku.ac.jp

  • ↵1 This work was partially supported by research fellowships of the Japan Society for the Promotion of Science for Young Scientists and a grant-in-aid for scientific research from the Ministry of Education, Sciences, and Culture of Japan.

  • Abbreviations:
    RyR
    ryanodine receptor
    EC
    excitation-contraction
    SR
    sarcoplasmic reticulum
    XQN
    xestoquinone
    HSR
    heavy fraction of sarcoplasmic reticulum
    LSR
    light fraction of fragmented sarcoplasmic reticulum
    MOPS
    3-(N-morpholino)propanesulfonic acid
    EGTA
    ethylene glycol bis(β-aminoethyl ether)-N,N,N′N′,-tetraacetic acid
    DTT
    dithiothreitol
    MBED
    9-methyl-7-bromoeudistomin D
    • Received March 8, 1999.
    • Accepted August 13, 1999.
  • The American Society for Pharmacology and Experimental Therapeutics
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Journal of Pharmacology and Experimental Therapeutics: 291 (3)
Journal of Pharmacology and Experimental Therapeutics
Vol. 291, Issue 3
1 Dec 1999
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Research ArticleArticle

Xestoquinone, Isolated from Sea Sponge, Causes Ca2+Release through Sulfhydryl Modification from Skeletal Muscle Sarcoplasmic Reticulum

Masaaki Ito, Yutaka Hirata, Hideshi Nakamura and Yasushi Ohizumi
Journal of Pharmacology and Experimental Therapeutics December 1, 1999, 291 (3) 976-981;

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Research ArticleArticle

Xestoquinone, Isolated from Sea Sponge, Causes Ca2+Release through Sulfhydryl Modification from Skeletal Muscle Sarcoplasmic Reticulum

Masaaki Ito, Yutaka Hirata, Hideshi Nakamura and Yasushi Ohizumi
Journal of Pharmacology and Experimental Therapeutics December 1, 1999, 291 (3) 976-981;
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