Lin Y, Ye L H, Ishikawa R, Fujita K, Kohama K
Department of Pharmacology, Gunma University School of Medicine.
J Biochem. 1993 Jun;113(6):643-5. doi: 10.1093/oxfordjournals.jbchem.a124096.
Calponin, a calmodulin-binding protein of smooth muscle that inhibits the actin-myosin interaction by binding to actin, was shown to bind to myosin and to stimulate the ATPase activity of myosin to some extent. Actin abolished this myosin-linked, stimulatory effect of calponin. Ca(2+)-calmodulin affected neither the myosin-binding activity nor the stimulatory effect of calponin. We further presented a few data which suggest that calponin may exert regulatory activity toward myosin in quite a different way from caldesmon, another smooth muscle protein that binds to myosin, actin, and calmodulin.
钙调蛋白是一种平滑肌的钙调素结合蛋白，它通过与肌动蛋白结合来抑制肌动蛋白-肌球蛋白的相互作用，研究表明它也能与肌球蛋白结合，并在一定程度上刺激肌球蛋白的ATP酶活性。肌动蛋白消除了钙调蛋白这种与肌球蛋白相关的刺激作用。钙离子-钙调素既不影响钙调蛋白与肌球蛋白的结合活性，也不影响其刺激作用。我们还提供了一些数据，表明钙调蛋白可能以一种与钙调蛋白截然不同的方式对肌球蛋白发挥调节活性，钙调蛋白是另一种与肌球蛋白、肌动蛋白和钙调素结合的平滑肌蛋白。
