Villalobos-Molina R, Devlin T M
Department of Biological Chemistry, Hahnemann University School of Medicine, Philadelphia, PA 19102-1192.
Biochem Biophys Res Commun. 1994 Jun 30;201(3):1457-63. doi: 10.1006/bbrc.1994.1867.
Phosphorylase activity of isolated rat liver cells was increased about 2-fold on addition of tri-Calciphor (trimer of 16, 16-dimethyl-15-dehydroprostaglandin B1), epinephrine or the Ca2+ ionophore A23187, in all cases presumably due to an increase in cytosolic Ca2+. Extracellular Ca2+ was required with A23187, but not with either tri-Calciphor or epinephrine. Tri-Calciphor, however, did not stimulate a sustained release of glucose from hepatocytes as compared to the other Ca2+ mobilizing agents, even at concentrations 10-fold higher than that required to stimulate the phosphorylase activity. Tri-Calciphor did not alter the glucose release by epinephrine. It is concluded that tri-Calciphor can alter cytosolic Ca2+, but that its mechanism of action is more complex than that of a simple Ca2+ ionophore.
添加三钙磷素（16,16 - 二甲基 - 15 - 脱氢前列腺素B1的三聚体）、肾上腺素或钙离子载体A23187后，分离的大鼠肝细胞的磷酸化酶活性增加了约2倍，在所有情况下，推测这是由于细胞溶质钙增加所致。使用A23187时需要细胞外钙，但使用三钙磷素或肾上腺素时则不需要。然而，与其他钙离子动员剂相比，即使三钙磷素的浓度比刺激磷酸化酶活性所需的浓度高10倍，它也不会刺激肝细胞持续释放葡萄糖。三钙磷素不会改变肾上腺素引起的葡萄糖释放。得出的结论是，三钙磷素可以改变细胞溶质钙，但其作用机制比简单的钙离子载体更为复杂。
