Wülfroth P, Petzelt C
Cell Calcium. 1985 Aug;6(4):295-310. doi: 10.1016/0143-4160(85)90001-6.
We present evidence that a Ca2+- transport system of the endoplasmic reticulum with the "mitotic" Ca2+- ATPase as an essential component is another target for the anticalmodulin drugs fluphenazine, calmidazolium, and compound 48/80. Furthermore we show by affinity chromatography that there is a direct interaction between the solubilized Ca2+- ATPase and fluphenazine. Since the Ca2+- uptake system as well as the solubilized Ca2+- ATPase are calmodulin- free, the effect of fluphenazine, calmidazolium and compound 48/80 may be understood as a result of the interaction between these drugs and the Ca2+- ATPase. We propose that there are calmodulin- like sequences in the molecule of the Ca2+- ATPase. The inhibitory effect of these three drugs can be then explained by their recognition of the calmodulin- like structures.
我们提供的证据表明，以内质网的Ca2+转运系统（以“有丝分裂”Ca2+ - ATP酶作为重要组成部分）是抗钙调蛋白药物氟奋乃静、氯米达唑和48/80化合物的另一个作用靶点。此外，我们通过亲和层析表明，溶解的Ca2+ - ATP酶与氟奋乃静之间存在直接相互作用。由于Ca2+摄取系统以及溶解的Ca2+ - ATP酶都不含钙调蛋白，氟奋乃静、氯米达唑和48/80化合物的作用可能被理解为这些药物与Ca2+ - ATP酶之间相互作用的结果。我们提出，Ca2+ - ATP酶分子中存在类似钙调蛋白的序列。这三种药物的抑制作用随后可通过它们对类似钙调蛋白结构的识别来解释。
