Inhibition by ca2+ of the incorporation of myo-inositol into phosphatidylinositol
Inhibition by ca2+ of the incorporation of myo-inositol into phosphatidylinositol
复制标题
ca2 抑制肌醇掺入磷脂酰肌醇
DOI:
10.1016/0303-7207(81)90027-7
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发表时间:
1981
影响因子:
4.1
通讯作者:
B. Sacktor
中科院分区:
文献类型:
--
作者:
Egawa Kohji;Takenawa Tadaomi;B. Sacktor
The incorporation ofmyo-[2-3H]inositol into phosphatidylinositol of the aorta and the vas deferens was measured and the effects of Ca2+and other divalent cations were determined. When incubated in normal Krebs-Ringer buffer, only negligible radioactivity was incorporated into aorta slices. Mn2+increased the incorporation greatly. The enhanced incorporation was attributable to an increase in CDP-diglyceride:inositol transferase activity, rather than themyo-inositol exchange reaction. Transferase activity was increased 20-fold by 1 mM Mn2+, in the presence of 20 mM Mg2+. The Mn2+-stimulated activity was strongly inhibited by Ca2+. In the absence of Mn2+, but presence of 20 mM Mg2+, transferase activity was inhibited 80% by 0.01 mM Ca2+. Removal of endogenous Ca2+from the tissue by ionophore A23187 and EGTA increased the incorporation ofmyo-[2-3H]inositol into phosphatidylinositol. These findings indicate that Ca2+inhibited the synthesis of phosphatidylinositol. The proposed action of cholinergic and α-adrenergic agonists in enhancing the degradation and turnover of phosphatidylinositol and in provoking the influx of Ca2+should be unfavorable to the recovery of cellular phosphatidylinositol content.