Anionic phospholipid-induced regulation of reactive oxygen species production by human cytochrome P450 2E1.
We suggest that the cytochrome P450 2E1 (CYP2E1)-induced formation of reactive oxygen species (ROS) can be regulated by anionic phospholipids and the presence of the N-terminal region of the enzyme. When the content of cardiolipin (CL) in membranes at the expense of phosphatidylcholine matrix was increased, the ROS produced by recombinant human CYP2E1 was decreased as a function of CL concentration. On the contrary, the N-terminally truncated CYP2E1 had a decreased effect on the lipid-induced reduction of ROS formation. These results suggest that specific phospholipids can regulate the function of CYP2E1 by interaction with the enzyme including the N-terminal region(s).
Cho
Eun Yi
EY
School of Biological Sciences and Technology and Hormone Research Center, Chonnam National University, Gwangju 500-757, Republic of Korea.
Yun
Chul-Ho
CH
Chae
Ho-Zoon
HZ
Chae
Han-Jung
HJ
Ahn
Taeho
T
D000838:Anions / Q000378:metabolism; D002308:Cardiolipins / Q000378:metabolism*; D019392:Cytochrome P-450 CYP2E1 / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D009249:NADP / Q000378:metabolism; D010084:Oxidation-Reduction; D017433:Protein Structure, Secondary; D017382:Reactive Oxygen Species / Q000378:metabolism*; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D000838:Anions; D002308:Cardiolipins; D017382:Reactive Oxygen Species; D011994:Recombinant Proteins; D009249:NADP; D019392:Cytochrome P-450 CYP2E1