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J. Biochem, 1997, Vol. 122, No. 2 344-351
© 1997 Japanese Biochemical Society

research-article

Interaction of Chicken Gizzard Smooth Muscle Calponin with Brain Microtubules

Toshihiro Fujii*,1, Tsuneyoshi Hiromori*, Masateru Hamamoto* and Tatsuo Suzuki{dagger}

*Department of Imagination Science (Kansei Engineering), Faculty of Textile Science and Technology, Shinshu University Ueda, Nagano 386
{dagger}Department of Neuroplasticity, Research Center on Aging and Adaptation, Shinshu University School of Medicine Matsumoto, Nagano 390

1To whom correspondence should be addressed

Calponin, a major actin-, tropomyosin-, and calmodulin-binding protein in smooth muscle, interacted with tubulin, a main constituent of microtubules, in a concentration-dependent fashion in vitro. The apparent Kd value of calponin to tubulin was calculated to be 5.2 µM with 2 mol of calponin maximally bound per 1 mol of tubulin. At low ionic strength, tubulin bound to calponin immobilized on Sepharose 4B, and the bound protein was released at about 270 mM NaCl. Chemical cross-linking experiments showed that a 1:1 molar covalent complex of calponin and tubulin was produced. The amount of calponin bound to microtubules decreased with increasing ionic strength or ca2+ concentration. The addition of calmodulin or S100 to the mixture of calponin and microtubule proteins caused the removal of calponin from microtubules in the presence of ca2+, but not in the presence of EGTA. Calponin-related proteins including tropomyosin, SM22, and caldesmon had little effect on the calponin binding to microtubules, whereas MAP2 inhibited the binding. Interestingly, there was little, if any, effect of mycalolide B-treated actin on the binding of calponin to microtubules. Furthermore, only about 20% of calponin-F-actin interaction was inhibited in the presence of an excess amount of tubulin (4 mol per mol of calponin), indicating that tubulin binds to calponin at a different site from that of actin. Compared with MAP2, calponin had little effect on microtubule polymerization.


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