Kawabe J i, Ebina T, Toya Y, Oka N, Schwencke C, Duzic E, Ishikawa Y
Brigham and Women's Hospital, Harvard Medical School, Boston, MA 02115, USA.
FEBS Lett. 1996 Apr 22;384(3):273-6. doi: 10.1016/0014-5793(96)00331-6.
Abstract Type V adenylyl cyclase (AC) was stably over-expressed in HEK293 cells (293AC-V). Forskolin-stimulated cAMP accumulation in 293AC-V was 5 times as great as that in control cells. PMA, a protein kinase C (PKC) activator, enhanced cAMP accumulation in 293AC-V cells dose-and time-dependently and this enhancement was abolished by staurosporine. Insulin also enhanced cAMP accumulation in 293AC-V cells. Co-transfection of PKC-zeta, but not PKC-alpha, potentiated the effects of insulin. These data suggest that type V AC activity is regulated in cells by PKC isoenzymes through different extracellular stimuli.
摘要 Ⅴ型腺苷酸环化酶（AC）在人胚肾293细胞（293AC-V）中稳定过表达。福斯高林刺激后，293AC-V细胞中cAMP的积累量是对照细胞的5倍。蛋白激酶C（PKC）激活剂佛波酯（PMA）能剂量和时间依赖性地增强293AC-V细胞中cAMP的积累，而这种增强作用被星形孢菌素消除。胰岛素也能增强293AC-V细胞中cAMP的积累。共转染PKC-ζ而非PKC-α可增强胰岛素的作用。这些数据表明，在细胞中，Ⅴ型AC活性受PKC同工酶通过不同细胞外刺激的调节。
