Effect of sulforaphane on glutathione-adduct formation and on glutathione_S_transferase-dependent detoxification of acrylamide in Caco-2 cells

Molecular Nutrition and Food Research

Volumn 53, Issue 12, 2009, Pages 1540-1550

  Pernice, Rita ^a   Hauder, Johanna ^b   Koehler, Peter ^b   Vitaglione, Paola ^a   Fogliano, Vincenzo ^a   Somoza, Veronika ^a  

^a UNIVERSITY OF NAPLES FEDERICO II   (Italy)

^b DEUTSCHE FORSCHUNGSANSTALT FÜR LEBENSMITTELCHEMIE   (Germany)

Author keywords

Acrylamide; Caco 2 cells; Glutathione S transferase; GSH adducts; Sulforaphane

Indexed keywords

ACRYLAMIDE; ANTINEOPLASTIC AGENT; CARCINOGEN; DRUG DERIVATIVE; EPOXIDE; GLUTATHIONE; GLUTATHIONE TRANSFERASE; GLYCIDAMIDE; SULFORAFAN; THIOCYANIC ACID DERIVATIVE;

ARTICLE; CELL STRAIN CACO 2; CHEMICAL STRUCTURE; CHEMISTRY; DRUG DETOXIFICATION; ELECTROSPRAY MASS SPECTROMETRY; FOOD CONTAMINATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; METABOLISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; TANDEM MASS SPECTROMETRY; TIME;

ACRYLAMIDE; ANTICARCINOGENIC AGENTS; CACO-2 CELLS; CARCINOGENS; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; EPOXY COMPOUNDS; FOOD CONTAMINATION; GLUTATHIONE; GLUTATHIONE TRANSFERASE; HUMANS; HYDROGEN-ION CONCENTRATION; MAGNETIC RESONANCE SPECTROSCOPY; METABOLIC DETOXICATION, PHASE II; MOLECULAR STRUCTURE; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; TANDEM MASS SPECTROMETRY; THIOCYANATES; TIME FACTORS;

EID: 71149113401     PISSN: 16134125     EISSN: 16134133     Source Type: Journal    
DOI: 10.1002/mnfr.200900447     Document Type: Article

References (42)

1. Tareke, E., Rydberg, P., Karlsson, P., Eriksson, M., Törnqvist, M., Analysis of acrylamide, a carcinogen formed in heated food-stuffs. J. Agric. Food Chem. 2002, 50, 4998-5006.
2. Calleman, C. J., Wu, Y., He, F., Tian, G. et al., Relationships between biomarkers of exposure and neurological effects in a group of workers exposed to acrylamide. Toxicol. Appl. Pharmacol. 1994, 126, 361-371.
3. He, F., Zhang, S., Wang, H. L., Li, G. et al., Neurological and electroneuromyographic assessment of the adverse effects of acrylamide on occupationally exposed workers. Scand. J. Work Environ. Health 1989, 15, 125-129.
4. Bull, R. J., Robinson, M., Laurie, R. D., Stoner, G. D. et al., Carcinogenic effects of acrylamide in Sencar and A/J Mice. Cancer Res. 1984, 44, 107-111.
5. 0-deoxynucleosides and DNA following in vitro reaction with acrylamide. Cancer Res. 1985, 45, 3465-3470.
6. Solomon, J. J., Cyclic adducts and intermediates induced by simple epoxides. IARC Sci. Publ. 1999, 150, 123-135.
7. Dearfield, K. L., Douglas, G. R., Ehling, U. H., Moore, M. M. et al., Acrylamide: a review of its genotoxicity and an assessment of heritable genetic risk. Mutat. Res. 1995, 330, 71-99.
8. Fuhr, U., Boettcher, M. I., Kinzig-Schippers, M., Weyer, A. et al., Toxicokinetics of acrylamide in humans after ingestion of a definded dose in a test meal to improve risk assessment for acrylamide carcinogenity. Cancer Epidemiol. Biomarkers Prev. 2006, 15, 266-271.
9. Cui, S., Kim, S.-J., Jo, S.-C., Lee, Y.-M., Lee, Y.-I., A study of in vitro scavenging reactions of acrylamide with glutathione using electrospray ionization tandem mass spectrometry. Bull. Korean Chem. Soc. 2005, 26, 1235-1240.
10. Dixit, R., Das, M., Seth, P. K., Mukhtar, H. P., Interaction of acrylamide with bovine serum albumin. Environ. Res. 1986, 40,365-371.
11. Wattenberg, L. W., Prevention, therapy and basic science and the resolution of the cancer problem. Cancer Res. 1993, 53,5890-5896.
12. Kohlmeier, L., Su, L., Cruciferous vegetable consumption and colorectal cancer risk: meta-analysis of the epidemiological evidence. FASEB J. 1997, 11, A369.
13. Talalay, P., Fahey, J. W., Phytochemicals from cruciferous plants protect against cancer by modulating carcinogen metabolism. J. Nutr. 2001, 131, 3027-3033.
14. Zhang, Y., Talalay, P., Cho, C. G., Posner, G. H., A major inducer of anticarcinogenic protective enzymes from broccoli: isolation and elucidation of structure. Proc. Natl. Acad. Sci. USA 1992, 89, 2399-2408.
15. Lee, K. Y., Shibutani, M., Kuroiwa, K., Takagi, H. et al., Chemoprevention of acrylamide toxicity by antioxidative agents in rats-effective suppression of testicular toxicity by phenylethyl isothiocyanate. Arch. Toxicol. 2005, 79, 531-541.
16. Odland, I., Romert, L., Clemedson, C., Walum, E., Glutathione content, glutathione transferase activity and lipid peroxidation in acrylamide-treated neuroblastoma NIE 115 cells. Toxicol in Vitro 1994, 8, 263-267.
17. Habig, W. H., Pabst, M. J., Jakoby, W. B., Glutathione Stransferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 1974, 25, 7130-7139.
18. Lowry, O. H., Rosebrough, N. L., Farr, A. L., Randall, R. J., Protein measurement with the folin phenol reagent. J. Biol. Chem. 1951, 193, 265-275.
19. Richie, J. P., Jr., Skowronski, L., Abraham, P., Leutzinger, Y., Blood glutathione concentrations in a large-scale human study. Clin. Chem. 1996, 42, 64-70.
20. Hayes, J. D., Pulford, D. J., The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit. Rev. Biochem. Mol. Biol. 1995, 30, 445-600.
21. Faist, V., Lindenmeier, M., Geisler, C., Erbersdobler et al, Influence of molecular weight fractions isolated from roasted malt on the enzyme activities of NADPH-cytochrome c-reductase and glutathion-S-transferase in caco-2 cells. J. Agric. Food Chem. 2002, 50, 602-606.
22. Lindenmeier, M., Faist, V., Hofmann, T., Structural and functional characerization of pronyl-lysine, a novel protein modification in bread crust melanoidins showing in vitro antioxidative and Phase I/II-enzyme modulating activity. J. Agric. Food Chem. 2002, 50, 6997-7006.
23. Somoza, V., Lindenmeier, M., Wenzel, E., Frank, O. et al., Activity-guided identification of a chemopreventive compound in coffee beverage using in vitro and in vivo techniques. J. Agric. Food Chem. 2003, 51, 6861-6869.
24. Puppel, N., Tjaden, Z., Fueller, F., Marko, D., DNA strand breaking capacity of acrylamide and glycidamide in mammalian cells. Mutat. Res. 2005, 580, 71-80.
25. Srivastava, S. P., Sabri, M. I., Agrawal, A. K., Seth, P. K., Effect of single and repeated doses of acrylamide and bisacrylamide on glutathione S-transferase and dopamine receptors in rat brain. Brain Res. 1986, 371, 319-323.
26. Zhang, Y., Molecular mechanism of rapid cellular accumulation of anticarcinogenic isothiocyanates. Carcinogenesis 2001,22,425-431
27. Svehlikova, V., Wang, S., Jakubikova, J., Williamson, G. et al., Interactions between sulforaphane and apigenin in the induction of UGT1A1 and GSTA1 in Caco-2 cells. Carcinogenesis 2004, 25, 1629-1637.
28. Zhang, Y., Talalay, P., Mechanism of differential potencies of isothiocyanates as inducers of anticarcinogenic phase 2 enzymes. Cancer Res.1998, 58, 4632-4639
29. Basten, G. B., Bao, Y. P., Williamson, G., Sulforaphane and its glutathione conjugate but not sulforaphane nitrile induce UDP-glucuronosyl transferase (GSTA1) in cultured cells. Carcinogenesis 2002, 23, 1399-1404
30. Ye, L., Zhang, Y., Total intracellular accumulation levels of dietary isothiocyanates determine their activity in elevation of cellular glutathione and induction of Phase 2 detoxification enzymes. Carcinogenesis 2001, 22, 1987-1992.
31. Gerhäuser, C., You, M., Liu, J., Moriarty, R. M. et al., Cancer chemopreventive potential of sulforamate, a novel analoue of sulforaphane that induces phase 2 drug-metabolizing enzymes. Cancer Res.1997, 57, 272-278
32. Posner, G. H., Cho, C. G., Green, J. V., Zhang, Y. et al., Design and synthesis of bifunctional isothiocyanate analogs of sulforaphane: correlation between structure and potency as inducers of anticarcinogenic detoxication enzmyes. J. Med. Chem.1994, 37, 170-176
33. Keck, A. S., Staack, R., Jeffery, E. H., The cruciferous nitrile crambene has bioactivity similar to sulforaphane when administered to Fischer 344 rats but is far less potent in cell culture. Nutr. Cancer 2002, 42, 233-240
34. Matusheski, N. V., Jeffery, E. H., Comparison of the bioactivity of two glucoraphanin hydrolysis products found in broccoli, sulforaphane and sulforaphane nitrile. J. Agric. Food Chem. 2001, 49, 5743-5749
35. Zhu, C. Y., Loft, S., Effect of chemopreventive compounds from Brassica vegetables on NAD(P)H:quinone reductase and induction of DNA strand breaks in murine hepa1c1c7 cells. Food Chem. Toxicol. 2003, 41, 455-462
36. Zoedl, B., Schmid, D., Wassler, G., Gundacker, C. et al., Intestinal transport and metabolism of acrylamide. Toxicology 2007, 232, 99-108.
37. Jakubíková, J., Sedlák, J., Bod'o, J., Bao, Y., Effect of isothiocyanates on nuclear accumulation of NF-kappaB, Nrf2, and thioredoxin in Caco-2 cells. J. Agric. Food. Chem. 2006,54,1656-1662.
38. Zhang, Y., Role of glutathione in the accumulation of anticarcinogenic isothiocyanates and their glutathione conjugates by murine hepatoma cells. Carcinogenesis 2000, 21,1175-1182.
39. Kim, B. R., Hu, R., Keum, Y. S., Hebbar, V. et al., Effects of glutathione on antioxidant response element-mediated gene expression and apoptosis elicited by sulforaphane. Cancer Res. 2003, 63, 7520-7525.
40. Schabacker, J., Schwend, T., Wink, M., Reduction of acrylamide uptake by dietary proteins in a Caco-2 gut model. J. Agric. Food Chem. 2004, 52, 4021-4025.
41. Cooper, D. A., Webb, D. R., Peters, J. C., Evalutation of the potential for olestra to affect the availability of dietary phytochemicals. J. Nutr. 1997, 127, 1699-1709.
42. Singh, S. V., Srivastava, S. K., Choi, S., Lew, K. L. et al., Sulforaphane-induced cell death in human prostate cancer cells is initiated by reactive oxygen species. J. Biol. Chem. 2005,280,19911-19924.