期刊论文详细信息
FEBS Letters
A soluble NH2‐terminally truncated catalytically active form of rat cytochrome P450 2E1 targeted to liver mitochondria
Ingelman-Sundberg, Magnus1  Neve, Etienne P.A.1 
[1] Division of Molecular Toxicology, National Institute of Environmental Medicine, Karolinska Institute, Box 210, S-171 77 Stockholm, Sweden
关键词: Mitochondrial import;    Chlorzoxazone;    cDNA transfection;    Adrenodoxin;    Ethanol;    Oxidative stress;    Cytochrome P450 2E1;    P450;    cytochrome P450;    ER;    endoplasmic reticulum;    Adx;    adrenodoxin;    AdR;    adrenodoxin reductase;    NaDOC;    sodium deoxycholate;    PBS;    phosphate buffered saline;   
DOI  :  10.1016/S0014-5793(99)01361-7
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
PDF
【 摘 要 】

The role of the NH2-terminus of cytochrome P450 2E1 (CYP2E1) in intracellular targeting was investigated. Two NH2-terminal CYP2E1 mutants, Δ(2–29)2E1, lacking the transmembrane domain, and N++2E1, having Ala2Lys and Val3Arg substitutions, were generated and expressed in the H2.35 mouse hepatoma cell line. In cells transfected with both constructs, a 40 kDa fragment of CYP2E1 (Δ2E1) was found to be localized to mitochondria as evidenced from immunofluorescence microscopy and subcellular fractionation studies. Δ2E1 was shown to be a soluble protein localized inside the mitochondria, displayed catalytic activity when reconstituted with adrenodoxin and adrenodoxin reductase, and was also present in mitochondria isolated from rat liver. It is concluded that in the absence of the hydrophobic NH2-terminal sequence, a putative mitochondrial import signal is exposed which targets CYP2E1 to this organelle where it is further processed.

【 授权许可】

Unknown   

【 预 览 】
附件列表
Files Size Format View
RO201912020308496ZK.pdf 108KB PDF download
  文献评价指标  
  下载次数:7次 浏览次数:7次