Illiano G, Cuatrecasas P
Science. 1972 Feb 25;175(4024):906-8. doi: 10.1126/science.175.4024.906.
Insulin depresses both the activity of adenylate cyclase stimulated by glucagon, epinephrine, and sodium fluoride in liver cell membranes and the activity of adenylate cyclase stimulated by epinephrine and adrenocorticotropin in particulate preparations from homogenates of isolated fat cells. Significant inhibition is detected with very low concentrations (10(-11) molar) of insulin but not with unphysiologically high (10(-9)molar) concentrations of the hormone. These direct effects of insulin on an enzymatic system in broken-cell -preparations suggest a fundamental role of adenylate cyclase activity and of cyclic adenosine monophosphate in the mechanism of action of insulin.
胰岛素可抑制肝细胞膜中由胰高血糖素、肾上腺素和氟化钠刺激的腺苷酸环化酶的活性，以及分离脂肪细胞匀浆的微粒体制剂中由肾上腺素和促肾上腺皮质激素刺激的腺苷酸环化酶的活性。在极低浓度（10^(-11)摩尔）的胰岛素下即可检测到显著抑制作用，但在非生理高浓度（10^(-9)摩尔）的该激素下则未检测到。胰岛素对破碎细胞制剂中酶系统的这些直接作用表明，腺苷酸环化酶活性和环磷酸腺苷在胰岛素作用机制中具有重要作用。
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