Phospholipase D activity of cytochrome P450 in human liver endoplasmic reticulum.
Phospholipase D activity of cytochrome P450 in human liver endoplasmic reticulum.
复制标题
DOI：
10.1006/abbi.1999.1254
复制
发表时间：
1999-07
影响因子：
3.9
通讯作者：
C. Yun;T. Ahn;F. Guengerich;H. Yamazaki;T. Shimada
中科院分区：
文献类型：
--
作者：
C. Yun;T. Ahn;F. Guengerich;H. Yamazaki;T. Shimada
磷脂酶D （PLD）在哺乳动物肝内质网（ER）中的活性尚未被表征。纯化的人肝微粒体细胞色素P450 (P450)-P450 1A2和P450 2e1 -显示出明显的PLD活性，水解磷脂酰胆碱，但不水解其他磷脂，产生PA和胆碱。利用重组和突变的人p450在细菌中表达证实了其活性。在人肝微粒体中，观察到抗p450 1A2、抗p450 2C、抗p450 2E1、抗p450 2E1对PLD活性的免疫抑制作用。因此，P450可能在人肝脏内质网中作为一种重要的PLD，并通过信号功能和膜性质的改变等多种机制发挥其生物学作用。
Phospholipase D (PLD) activity in mammalian liver endoplasmic reticulum (ER) has not been characterized. Purified human liver microsomal cytochromes P450 (P450)-P450 1A2 and P450 2E1-were shown to have appreciable PLD activity, hydrolyzing phosphatidylcholine but not other phospholipids, generating PA and choline. The activity was confirmed using recombinant and mutated human P450s expressed in bacteria. In human liver microsomes, immunoinhibition of PLD activity was observed with anti-P450 1A2 > anti-P450 2C > anti-P450 2E1. Thus, P450 may act as a significant PLD in human liver ER and exert its biological effects by several mechanisms, including signaling functions and change of membrane properties.