Regular ArticleEnzyme-Specific Transport of Rat Liver Cytochrome P450 to the Golgi Apparatus☆
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Cited by (48)
Plasma membrane localization of CYP4Z1 and CYP19A1 and the detection of anti-CYP19A1 autoantibodies in humans
2019, International ImmunopharmacologyPathophysiological implications of neurovascular P450 in brain disorders
2016, Drug Discovery TodayCYP2E1 autoantibodies in liver diseases
2014, Redox BiologyCitation Excerpt :Beside DC, antigen presentation might also involve hepatic stellate cells [59] and possibly hepatocytes themselves, as pro-inflammatory cytokines have been shown to induce the hepatocyte expression of class II major histocompatibility complex (MHC) and co-stimulatory CD80 (B7.1) molecules [60]. Although during chronic liver injury CYP released from damaged hepatocytes might be a trigger for the breaking of self-tolerance, it should be noted that anti-CYP self-reactivity associated to CHC, alcohol abuse or adverse drug reactions is highly specific to individual CYPs [7–10] and there is no cross-reactivity between anti-CYP2E1 and anti-CYP2D6 antibodies [54,55] in HCV-infected patients. This indicates that additional and more specific mechanisms are likely involved.
Mitochondria-targeted cytochrome P450 2E1 induces oxidative damage and augments alcohol-mediated oxidative stress
2010, Journal of Biological ChemistryCitation Excerpt :Additionally, a large number of studies implicate a role for CYP2E1 in reactive oxygen species (ROS) production and oxidative stress (7–11). A large fraction of hepatocellular CYP2E1 is located in the endoplasmic reticulum (ER), although significant levels are detected in other cell compartments including lysosomes (12), plasma membrane (13, 14), Golgi apparatus (15), peroxisomes (16), and mitochondria (17–20). Studies have shown increased mitochondrial CYP2E1 content in streptozotocin-treated and alcohol-treated rats and mice (21, 22).
Proteasome inhibition compromises direct retention of cytochrome P450 2C2 in the endoplasmic reticulum
2008, Experimental Cell ResearchCYP2E1 and oxidative liver injury by alcohol
2008, Free Radical Biology and Medicine
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This research was supported by grants from the Swedish Alcohol Research Fund and from the Swedish Medical Research Council.
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To whom correspondence should be addressed at Department of Medical Biochemistry and Biophysics, Berzelius Laboratory, Karolinska institutet, S-171 77 Stockholm, Sweden. Fax: 46-833-8453. E-mail: [email protected].