Wiktorek M, Sabała P, Czarny M, Barańska J
Department of Cellular Biochemistry, Nencki Institute of Experimental Biology, Warsaw, Poland.
Biochem Biophys Res Commun. 1996 Jul 25;224(3):645-50. doi: 10.1006/bbrc.1996.1079.
The effects of 2,5-di-tert-butylhydroquinone (DBHQ) and thimerosal on phosphatidylserine synthesis by the base exchange reaction and on calcium mobilization in intact glioma C6 cells were compared with that of thapsigargin, a selective inhibitor of the endoplasmic reticulum Ca(2+)-ATPase. It has been found that all these agents inhibit phosphatidylserine synthesis by 70%, but their effectiveness are different. The data show that this inhibition is caused by Ca2+ depletion of the endoplasmic reticulum, indicating that phosphatidylserine synthesis requires high concentration of Ca2+ within this structure. On this basis and on literature data, a new model for the localization of the serine base exchange enzyme in the endoplasmic reticulum membrane is proposed.
将2,5 - 二叔丁基对苯二酚（DBHQ）和硫柳汞对完整神经胶质瘤C6细胞中通过碱基交换反应合成磷脂酰丝氨酸以及钙动员的影响，与内质网Ca(2 +)-ATP酶的选择性抑制剂毒胡萝卜素的影响进行了比较。已发现所有这些试剂均抑制磷脂酰丝氨酸合成达70%，但它们的有效性有所不同。数据表明这种抑制是由内质网的Ca2 +耗竭引起的，这表明磷脂酰丝氨酸合成需要该结构内的高浓度Ca2 +。基于此以及文献数据，提出了内质网膜中丝氨酸碱基交换酶定位的新模型。
