Polycyclic Aromatic Hydrocarbons and Phenolic Antioxidants do not Significantly Induce Carbonyl Reductase in Human Cell Lines

Abstract

Carbonyl reductase (E.C. 1.1.1.184) is a cytosolic, monomelic oxidoreductase belonging to the short-chain alcohol dehydrogenase superfamily (Wermuth, 1992). It is widely distributed in human and animal tissues (Wirth and Wermuth, 1992). Characteristically, it occurs in three size heterogeneous forms with apparent molecular weights between 30′000 and 33′000. Evidence from sequence analysis suggests that the heterogeneity arises from posttranslational modification of lysine residues (Forrest et al., 1990). The nature of the modification and its physiological significance, however, are not yet known. Carbonyl reductase catalyzes the NADPH-dependent reduction of a variety of aldehydes, ketones and quinones among which quinones are most efficiently reduced. Based on the broad substrate specificity, including quinones derived from polycyclic aromatic hydrocarbons (PAH), we suggested that the enzyme may be involved in the detoxication of quinones and other reactive carbonyl compounds (Wermuth et al, 1986).