title: The activities of several detoxication enzymes are differentially induced by juices of garden cress, water cress and mustard in human HepG2 cells.
abstract: It has been previously demonstrated in a human-derived hepatoma cell line (HepG2) that juices from cruciferous vegetables protect against the genotoxicity caused by dietary carcinogens. HepG2 cells possess different enzymes involved in the biotransformation of xenobiotics. Therefore, we investigated the effect of cruciferous juices on the activities of CYP 1A and several phase II enzymes in this cell model. For each experiment, 1 x 10(6) cells were seeded on Petri dishes. After 2 days, the juices (0.5-8 microl/ml of culture medium) were added for 48 h prior to cell harvesting. The addition of juice from water cress (Nasturtium officinalis R. Br) significantly increased the activities of ethoxyresorufin-O-deethylase at high doses only and NAD(P)H-quinone reductase in a dose-dependent manner (1.8- and 5-fold, respectively). The addition of juice from garden cress (Lepidum sativum L.) significantly increased the activities of NAD(P)H-quinone reductase and UDP-glucuronosyl-transferase with a maximal effect around the dose of 2 microl/ml juice (1.4- and 1.2-fold, respectively) while the other enzymes were not altered. Mustard (Sinapis alba L.) juice increased the activities of NAD(P)H-quinone reductase (2.6-fold at the dose of 8 microl/ml), and N-acetyl-transferase (1.4-fold at the dose of 8 microl/ml) in a dose-dependent manner while a maximal induction of UDP-glucuronosyl-transferase was obtained with a dose of 2 microl/ml (1.8-fold). These observations show that the three juices have different induction profiles: only water cress acted as a bifunctional inducer by enhancing both phase I and phase II enzymes. As a consequence, each juice may preferentially inhibit the genotoxicity of specific compounds.
authors.affiliation: Unité d'Ecologie et de Physiologie du Système Digestif., INRA, Domaine de Vilvert, 78350 Jouy en Josas, France. lhoste@jouy.inra.fr
authors.forename: E F
authors.initials: EF
authors.lastname: Lhoste
authors.forename: K
authors.initials: K
authors.lastname: Gloux
authors.forename: I
authors.initials: I
authors.lastname: De Waziers
authors.forename: S
authors.initials: S
authors.lastname: Garrido
authors.forename: S
authors.initials: S
authors.lastname: Lory
authors.forename: C
authors.initials: C
authors.lastname: Philippe
authors.forename: S
authors.initials: S
authors.lastname: Rabot
authors.forename: S
authors.initials: S
authors.lastname: Knasmüller
mesh_terms: D000123:Acetyltransferases / Q000096:biosynthesis; D019607:Brassicaceae; D006528:Carcinoma, Hepatocellular; D045744:Cell Line, Tumor; D019363:Cytochrome P-450 CYP1A1 / Q000096:biosynthesis; D004790:Enzyme Induction; D014453:Glucuronosyltransferase / Q000096:biosynthesis; D005982:Glutathione Transferase / Q000096:biosynthesis; D006801:Humans; D008099:Liver / Q000166:cytology / Q000187:drug effects / Q000201:enzymology*; D016660:NAD(P)H Dehydrogenase (Quinone) / Q000096:biosynthesis; D010936:Plant Extracts / Q000494:pharmacology*; D015238:Sulfotransferases / Q000096:biosynthesis
chemical_list: D010936:Plant Extracts; D019363:Cytochrome P-450 CYP1A1; D016660:NAD(P)H Dehydrogenase (Quinone); D000123:Acetyltransferases; D014453:Glucuronosyltransferase; D005982:Glutathione Transferase; D015238:Sulfotransferases