Tennes K A, Roberts M L
Biochim Biophys Acta. 1982 Nov 24;719(2):238-43. doi: 10.1016/0304-4165(82)90094-0.
The effects of Ca2+ on agonist-stimulated hydrolysis of myo-[2-3H]inositol-labelled phosphatidylinositol in mouse pancreas in vitro, were studied. The increase in cytosol Ca2+ concentration produced by the ionophore A23187 did not stimulate the breakdown of phosphatidylinositol. Cholecystokinin-octapeptide (CCK-8) stimulated the hydrolysis of phosphatidylinositol under conditions in which intracellular calcium stores were depleted. The breakdown of phosphatidylinositol was stimulated by bethanechol and CCK-8 in Ca2+ -free Krebs solution, and the addition of Ca2+ to the medium potentiated the effects of these agonists. Lanthanum significantly reduced bethanechol and CCK-8-stimulated hydrolysis of phosphatidylinositol in Krebs solution, but was without effect in Ca2+ -free Krebs solution. The results of this study support the proposal that hydrolysis does not occur as a result of Ca2+ mobilization and may be involved in Ca2+ gating in the pancreas.
研究了钙离子(Ca2+)对体外培养的小鼠胰腺中激动剂刺激的肌醇-[2-3H]标记磷脂酰肌醇水解的影响。离子载体A23187引起的胞质Ca2+浓度升高并未刺激磷脂酰肌醇的分解。在细胞内钙库耗尽的条件下,胆囊收缩素八肽(CCK-8)刺激了磷脂酰肌醇的水解。在无Ca2+的Krebs溶液中,氨甲酰甲胆碱和CCK-8刺激了磷脂酰肌醇的分解,向培养基中添加Ca2+增强了这些激动剂的作用。镧显著降低了Krebs溶液中氨甲酰甲胆碱和CCK-8刺激的磷脂酰肌醇水解,但在无Ca2+的Krebs溶液中无作用。本研究结果支持以下观点:水解并非由Ca2+动员引起,可能参与胰腺中的Ca2+门控。