Lin Y, Ishikawa R, Kohama K
Department of Pharmacology, Gunma University School of Medicine.
J Biochem. 1993 Aug;114(2):279-83. doi: 10.1093/oxfordjournals.jbchem.a124167.
We have previously shown that caldesmon at low concentrations stimulates the interaction between actin, myosin, and ATP, while at high concentrations it inhibits the interaction [Ishikawa, R., Okagaki, T., Higashi-Fujime, S., & Kohama, K. (1991) J. Biol. Chem. 266, 21784-21790]. When the effect of caldesmon at low concentrations was monitored by measuring myosin ATPase activity in the absence of actin, the effect was slightly but significantly stimulatory; and at higher concentrations no inhibitory effect was observed. Therefore, we related the stimulatory effect with the myosin-binding property of caldesmon. In the presence of actin, a low concentration of caldesmon was not enough to evince the stimulatory effect: myosin concentration must also be low. This is because the stimulatory effect was obscured when myosin concentration was elevated. Ca(2+)-calmodulin abolished the stimulatory effect of caldesmon. However, the concentration of calmodulin required to abolish the stimulation was higher than that required to abolish the inhibition.
我们之前已经表明,低浓度的钙调蛋白能刺激肌动蛋白、肌球蛋白和ATP之间的相互作用,而高浓度时则抑制这种相互作用[石川,R.,冈垣,T.,东藤美枝,S.,& 小滨,K.(1991)《生物化学杂志》266,21784 - 21790]。当在没有肌动蛋白的情况下通过测量肌球蛋白ATP酶活性来监测低浓度钙调蛋白的作用时,该作用具有轻微但显著的刺激作用;而在较高浓度下未观察到抑制作用。因此,我们将这种刺激作用与钙调蛋白的肌球蛋白结合特性联系起来。在有肌动蛋白存在的情况下,低浓度的钙调蛋白不足以显示出刺激作用:肌球蛋白浓度也必须较低。这是因为当肌球蛋白浓度升高时,刺激作用就会被掩盖。钙(2 +) - 钙调蛋白消除了钙调蛋白的刺激作用。然而,消除刺激作用所需的钙调蛋白浓度高于消除抑制作用所需的浓度。