Holler T, Klein J, Löffelholz K
Institute of Pharmacology, University of Mainz, Germany.
Biochem Pharmacol. 1994 Jan 20;47(2):411-4. doi: 10.1016/0006-2952(94)90033-7.
In order to investigate a possible G-protein-mediated activation of phospholipase D (PLD) and its relationship to the activation of phosphoinositide-specific phospholipase C (PI-PLC), we measured the effects of aluminium fluoride and carbachol on choline release, the PLD-specific transphosphatidylation reaction (generation of phosphatidylpropanol) and the formation of inositol phosphates in rat hippocampal slices. Aluminium fluoride markedly enhanced the formation of choline and phosphatidylpropanol but failed to increase the formation of inositol phosphates. In contrast, the muscarinic agonist carbachol strongly stimulated PI-PLC but failed to activate PLD. We conclude that PLD in hippocampal slices is activated by a G-protein independently of phosphoinositide hydrolysis.
为了研究G蛋白介导的磷脂酶D（PLD）激活的可能性及其与磷酸肌醇特异性磷脂酶C（PI-PLC）激活的关系，我们测定了氟化铝和卡巴胆碱对大鼠海马切片中胆碱释放、PLD特异性转磷脂酰基反应（磷脂酰丙醇的生成）以及肌醇磷酸形成的影响。氟化铝显著增强了胆碱和磷脂酰丙醇的形成，但未能增加肌醇磷酸的形成。相反，毒蕈碱激动剂卡巴胆碱强烈刺激PI-PLC，但未能激活PLD。我们得出结论，海马切片中的PLD由G蛋白激活，且不依赖于磷酸肌醇水解。
