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Research ArticleArticle

Powerful Activation of Skeletal Muscle Actomyosin ATPase by Goniodomin A Is Highly Sensitive to Troponin/Tropomyosin Complex

Kimihiro Matsunaga, Keigo Nakatani, Masahiro Murakami, Katsumi Yamaguchi and Yasushi Ohizumi
Journal of Pharmacology and Experimental Therapeutics December 1999, 291 (3) 1121-1126;
Kimihiro Matsunaga
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Keigo Nakatani
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Masahiro Murakami
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Katsumi Yamaguchi
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Yasushi Ohizumi
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Abstract

Goniodomin A has been shown to cause the conformational change of actin to modify actomyosin ATPase activity. Goniodomin A induced a potent stimulation of the actomyosin ATPase activities of the actin-myosin reconstituted system and natural actomyosin in the range of 10−8 to 10−7 M. When the concentration was increased above 10−7 M, actomyosin ATPase activity was decreased. Interestingly, the troponin/tropomyosin complex caused a concentration-dependent inhibition of the goniodomin A-induced stimulation of actomyosin ATPase activity. In the presence of a high concentration of the troponin/tropomyosin complex, goniodomin A decreased actomyosin ATPase activity in a concentration-dependent manner. The enhancement of the ATPase activity of troponin/tropomyosin-free natural actomyosin by goniodomin A was larger than that obtained with natural actomyosin. Goniodomin A at lower concentrations enhanced the superprecipitation of natural actomyosin but decreased it at higher concentrations. The ATPase activity of skeletal muscle myofibrils and the contractile response of skinned fibers to Ca2+ were never activated and were decreased by this compound, suggesting an inhibition by the troponin/tropomyosin complex. In the far ultraviolet circular dichroism, goniodomin A above 10−8 M increased the negative ellipticity at 220 nm, suggesting an increase in the α-helical content of actin. These results suggest that goniodomin A increases and decreases actomyosin ATPase activity, probably through the stimulatory and inhibitory sites on actin, respectively. It is also suggested that the troponin/tropomyosin complex binds to actin to inhibit the goniodomin A-induced enhancement of actomyosin ATPase activity, probably by affecting the stimulatory site on the molecule.

Footnotes

  • Send reprint requests to: Yasushi Ohizumi, Ph.D., Department of Pharmaceutical Molecular Biology, Graduate School 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 a grant-in-aid for Scientific Research from the Ministry of Education, Science, Sports and Culture of Japan. Financial support from The Sagawa Foundation for Promotion of Cancer Research and The Nakatomi Foundation is also acknowledged.

  • Abbreviation:
    CD
    circular dichroism
    • Received May 4, 1999.
    • Accepted August 23, 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

Powerful Activation of Skeletal Muscle Actomyosin ATPase by Goniodomin A Is Highly Sensitive to Troponin/Tropomyosin Complex

Kimihiro Matsunaga, Keigo Nakatani, Masahiro Murakami, Katsumi Yamaguchi and Yasushi Ohizumi
Journal of Pharmacology and Experimental Therapeutics December 1, 1999, 291 (3) 1121-1126;

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Research ArticleArticle

Powerful Activation of Skeletal Muscle Actomyosin ATPase by Goniodomin A Is Highly Sensitive to Troponin/Tropomyosin Complex

Kimihiro Matsunaga, Keigo Nakatani, Masahiro Murakami, Katsumi Yamaguchi and Yasushi Ohizumi
Journal of Pharmacology and Experimental Therapeutics December 1, 1999, 291 (3) 1121-1126;
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