Ausiello D A, Hall D
J Biol Chem. 1981 Oct 10;256(19):9796-8.
It has recently been demonstrated that an established cell line from pig kidney, LLC-PK1, is a useful model for the study of vasopressin-sensitive adenylate cyclase (Roy, C., and Ausiello, D. A. (1981) J. Biol. Chem. 256, 3415-3422; Roy, C., Hall, D., Karish, M., and Ausiello, D. A. (1981) J. Biol. Chem. 256, 3423-3427). The present study on the regulation of this enzyme has led to the demonstration of the modulation of vasopressin-stimulated adenylate cyclase by Ca2+-calmodulin. The characteristics of calmodulin regulation were similar to those described for other enzymes: (a) activation required micromolar quantities of free Ca2+; (b) maximal enzyme rates were altered but not the Km for hormone activation; (c) activity was inhibitable by trifluoperazine; and (d) activation was dependent on the Mg2+ concentration. These findings should help to define the mechanisms of action of several agents known to alter vasopressin-sensitive adenylate cyclase and cell Ca2+ content.
最近已证明，源自猪肾的已建立细胞系LLC-PK1是研究血管升压素敏感腺苷酸环化酶的有用模型（罗伊，C.，和奥西埃洛，D. A.（1981年）《生物化学杂志》256，3415 - 3422；罗伊，C.，霍尔，D.，卡里什，M.，和奥西埃洛，D. A.（1981年）《生物化学杂志》256，3423 - 3427）。目前对该酶调节的研究导致了Ca²⁺ - 钙调蛋白对血管升压素刺激的腺苷酸环化酶调节作用的证明。钙调蛋白调节的特征与其他酶所描述的特征相似：（a）激活需要微摩尔量的游离Ca²⁺；（b）最大酶促反应速率改变，但激素激活的米氏常数不变；（c）活性可被三氟拉嗪抑制；（d）激活取决于Mg²⁺浓度。这些发现应有助于确定几种已知可改变血管升压素敏感腺苷酸环化酶和细胞Ca²⁺含量的药物的作用机制。
