Cartus T, Heurich R O, Drews G, Ammon H P
Institute of Pharmaceutical Sciences, Department of Pharmacology, University of Tübingen, Germany.
Regul Pept. 1998 Oct 16;77(1-3):77-81. doi: 10.1016/s0167-0115(98)00043-3.
In the insulin producing cell line RINm5F distribution of serine/threonine specific protein phosphatases type 1 (PP1) and 2A (PP2A) was studied. Using different agents which inhibit or stimulate PP1 and PP2A we found that in membrane and nuclear fractions phosphatase activity was inhibited by okadaic acid (OA), protamine, heparin, and inhibitor-2 in a concentration-dependent manner. C2-ceramide had no effect. In the cytosolic fraction the inhibitory effect of okadaic acid was tenfold higher. Protamine stimulated phosphatase activity at low concentrations and became inhibitory at higher concentrations. Inhibitor-2 and heparin caused a decrease in phosphatase activity whereas C2-ceramide led to a slight activation. The data suggest that in membrane and nuclear fractions of RINmSF cells predominantly PP1 is present, whereas in the cytosol PP1 as well as PP2A can be detected.
在胰岛素产生细胞系RINm5F中,研究了1型丝氨酸/苏氨酸特异性蛋白磷酸酶(PP1)和2A型丝氨酸/苏氨酸特异性蛋白磷酸酶(PP2A)的分布。使用不同的抑制或刺激PP1和PP2A的试剂,我们发现,在膜和核组分中,磷酸酶活性受到冈田酸(OA)、鱼精蛋白、肝素和抑制剂-2的浓度依赖性抑制。C2-神经酰胺没有作用。在胞质组分中,冈田酸的抑制作用高10倍。鱼精蛋白在低浓度时刺激磷酸酶活性,而在高浓度时则具有抑制作用。抑制剂-2和肝素导致磷酸酶活性降低,而C2-神经酰胺则导致轻微激活。数据表明,在RINmSF细胞的膜和核组分中主要存在PP1,而在胞质溶胶中可以检测到PP1以及PP2A。