[Goniodomin A induces modulation of actomyosin ATPase activity mediated through conformational change of actin].

نویسندگان

  • K Matsunaga
  • K Nakatani
  • M Murakami
  • N Nakahata
  • Y Ohizumi
چکیده

Goniodomin A induced a potent stimulation of the actomyosin ATPase activities of actin-myosin reconstituted system and natural actomyosin. Interestingly, these stimulatory effects of goniodomin A were significantly inhibited by troponin-tropomyosin complex. 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 inhibition by troponin-tropomyosin complex. In the analysis of the far-ultraviolet circular dichroism spectra, goniodomin A caused a concentration-dependent increase in alpha-helical content of actin. Goniodomin A inhibited the ATPase activities of atrial myofibrils, naural actimyosin and reconstituted actomyosin. Interestingly, these ATPase activities of ventricular muscle were enhanced by goniodomin A. The stimulatory effect of goniodomin A was significantly inhibited by troponin-tropomyosin complex. Goniodomin A increased the intracellular content of F-actin and caused the change in its distribution in 1321N1 cells. Goniodomin A-induced inositol phosphates accumulation in 1321N1 cells was reduced by C3 exoenzyme but was not affected by pertussis toxin. These results suggest that goniodomin A affects actin directly to modify the actin-myosin interaction and that goniodomin A-induced activation of the actomyosin ATPase activity may be physiologically significant because its activation is sensitive to the regulatory protein system, troponin-tropomyosin complex.

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Powerful activation of skeletal muscle actomyosin ATPase by goniodomin A is highly sensitive to troponin/tropomyosin complex.

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عنوان ژورنال:
  • Nihon yakurigaku zasshi. Folia pharmacologica Japonica

دوره 114 Suppl 1  شماره 

صفحات  -

تاریخ انتشار 1993