Krutetskaia Z I, Lebedev O E, Krutetskaia N I
Physiological Research Institute, St. Petersburg University.
Tsitologiia. 1998;40(5):445-54.
The effect of protein kinase C activating phorbol ester, phorbol-12-myristate-13-acetate (PMA), on purinergic agonists- and thapsigargin-induced Ca2+ signals in Fura-2 loaded rat peritoneal macrophages was investigated. PMA (100 ng/ml) was shown to inhibit 200 muM ATP- or 200 microM UTP-evoked Ca2+ entry in macrophages. Protein kinase C activation by PMA also inhibits the store-dependent or "capacitative" Ca2+ influx stimulated by emptying the intracellular Ca2+ stores with endoplasmic Ca(2+)-ATPase inhibitor thapsigargin (0.5 microM). Inhibition of entry by PMA was fully prevented by protein kinase C inhibitor 50 microM H-7. These data are compatible with the important role played by protein kinase C in the control of Ca2+ entry in rat peritoneal macrophages.
研究了蛋白激酶C激活剂佛波酯（phorbol-12-肉豆蔻酸酯-13-乙酸酯，PMA）对用Fura-2负载的大鼠腹腔巨噬细胞中嘌呤能激动剂和毒胡萝卜素诱导的Ca2+信号的影响。结果显示，PMA（100 ng/ml）可抑制巨噬细胞中200 μM ATP或200 μM UTP诱发的Ca2+内流。PMA激活蛋白激酶C还可抑制通过用内质网Ca(2+)-ATP酶抑制剂毒胡萝卜素（0.5 μM）排空细胞内Ca2+储存而刺激的储存依赖性或“容量性”Ca2+内流。蛋白激酶C抑制剂50 μM H-7可完全阻止PMA对Ca2+内流的抑制作用。这些数据与蛋白激酶C在控制大鼠腹腔巨噬细胞Ca2+内流中所起的重要作用相符。
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