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Bioscience, Biotechnology, and Biochemistry Volume 72, 2008 - Issue 6
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Original Articles

Ingested β-Carotene Enhances Glutathione Level and up-Regulates the Activity of Cysteine Cathepsin in Murine Splenocytes

Saki TAKEDADepartment of Food Science, Graduate School of Nutrition and Biosciences, The University of Tokushima
,
Noriko BANDODepartment of Food Science, Graduate School of Nutrition and Biosciences, The University of Tokushima
&
Rintaro YAMANISHIDepartment of Food Science, Graduate School of Nutrition and Biosciences, The University of Tokushima
Pages 1595-1600 | Received 15 Feb 2008, Accepted 25 Mar 2008, Published online: 22 May 2014

  • 1) Stahl, W., and Sies, H., Bioactivity and protective effects of natural carotenoids. Biochim. Biophys. Acta, 1740, 101–107 (2005).
  • 2) Pryor, W. A., Stahl, W., and Rock, C. L., Beta carotene: from biochemistry to clinical trials. Nutr. Rev., 58, 39–53 (2000).
  • 3) Peto, R., Doll, R., Buckley, J. D., and Sporn, M. B., Can dietary β-carotene materially reduce human cancer rates? Nature, 290, 201–208 (1981).
  • 4) Toma, S., Losardo, P. L., Vincent, M., and Palumbo, R., Effectiveness of β-carotene in cancer chemoprevention. Eur. J. Cancer Prev., 4, 213–224 (1995).
  • 5) van Poppel, G., and Goldbohm, R. A., Epidemiologic evidence for β-carotene and cancer prevention. Am. J. Clin. Nutr., 62, 1393S–1402S (1995).
  • 6) Verhoeven, D. T., Assen, N., Goldbohm, R. A., Dorant, E., van ’t Veer, P., Sturmans, F., Hermus, R. J., and van den Brandt, P. A., Vitamins C and E, retinol, β-carotene and dietary fibre in relation to breast cancer risk: a prospective cohort study. Br. J. Cancer, 75, 149–155 (1997).
  • 7) Halliwell, B., Effect of diet on cancer development: is oxidative DNA damage a biomarker? Free Radic. Biol. Med., 32, 968–974 (2002).
  • 8) Higdon, J., and Frei, B., Vitamin C, vitamin E, and β-carotene in cancer chemoprevention. In “Phytopharmaceuticals in Cancer Chemoprevention,” eds. Bagchi, D., and Preuss, H. G., CRC Press, Boca Raton, pp. 271–309 (2005).
  • 9) Imamura, T., Bando, N., and Yamanishi, R., β-Carotene modulates the immunological function of RAW264, a murine macrophage cell line, by enhancing the level of intracellular glutathione. Biosci. Biotechnol. Biochem., 70, 2112–2120 (2006).
  • 10) Victor, V. M., and De la Fuente, M., Immune cells redox state from mice with endotoxin-induced oxidative stress. Involvement of NF-κB. Free Radic. Res., 37, 19–27 (2003).
  • 11) Lockwood, T. D., Cathepsin B responsiveness to glutathione and lipoic acid redox. Antioxid. Redox Signal., 4, 681–691 (2002).
  • 12) Koizumi, T., Bando, N., Terao, J., and Yamanishi, R., Feeding with both β-carotene and supplemental alpha-tocopherol enhances type 1 helper T cell activity among splenocytes isolated from DO11.10 mice. Biosci. Biotechnol. Biochem., 70, 3042–3045 (2006).
  • 13) Bando, N., Hayashi, H., Wakamatsu, S., Inakuma, T., Miyoshi, M., Nagao, A., Yamauchi, R., and Terao, J., Participation of singlet oxygen in ultraviolet-a-induced lipid peroxidation in mouse skin and its inhibition by dietary β-carotene: an ex vivo study. Free Radic. Biol. Med., 37, 1854–1863 (2004).
  • 14) Fariss, M. W., and Reed, D. J., High-performance liquid chromatography of thiols and disulfides: dinitrophenol derivatives. Methods Enzymol., 143, 101–109 (1987).
  • 15) Barrett, A. J., Fluorimetric assays for cathepsin B and cathepsin H with methylcoumarylamide substrates. Biochem. J., 187, 909–912 (1980).
  • 16) Yasuda, Y., Kageyama, T., Akamine, A., Shibata, M., Kominami, E., Uchiyama, Y., and Yamamoto, K., Characterization of new fluorogenic substrates for the rapid and sensitive assay of cathepsin E and cathepsin D. J. Biochem. (Tokyo), 125, 1137–1143 (1999).
  • 17) Buus, S., and Werdelin, O., A group-specific inhibitor of lysosomal cysteine proteinases selectively inhibits both proteolytic degradation and presentation of the antigen dinitrophenyl-poly-L-lysine by guinea pig accessory cells to T cells. J. Immunol., 136, 452–458 (1986).
  • 18) Takahashi, H., Cease, K. B., and Berzofsky, J. A., Identification of proteases that process distinct epitopes on the same protein. J. Immunol., 142, 2221–2229 (1989).
  • 19) Diment, S., Different roles for thiol and aspartyl proteases in antigen presentation of ovalbumin. J. Immunol., 145, 417–422 (1990).
  • 20) Mizuochi, T., Yee, S. T., Kasai, M., Kakiuchi, T., Muno, D., and Kominami, E., Both cathepsin B and cathepsin D are necessary for processing of ovalbumin as well as for degradation of class II MHC invariant chain. Immunol. Lett., 43, 189–193 (1994).
  • 21) Droge, W., Schulze-Osthoff, K., Mihm, S., Galter, D., Schenk, H., Eck, H.-P., Roth, S., and Gmunder, H., Functions of glutathione and glutathione disulfide in immunology and immunopathology. FASEB J., 8, 1131–1138 (1994).
  • 22) Ben-Dor, A., Steiner, M., Gheber, L., Danilenko, M., Dubi, N., Linnewiel, K., Zick, A., Sharoni, Y., and Levy, J., Carotenoids activate the antioxidant response element transcription system. Mol. Cancer Ther., 4, 177–186 (2005).
  • 23) Peterson, J. D., Herzenberg, L. A., Vasquez, K., and Waltenbaugh, C., Glutathione levels in antigen-presenting cells modulate Th1 versus Th2 response patterns. Proc. Natl. Acad. Sci. USA, 95, 3071–3076 (1998).
  • 24) Murata, Y., Ohteki, T., Koyasu, S., and Hamuro, J., IFN-γ and pro-inflammatory cytokine production by antigen-presenting cells is dictated by intracellular thiol redox status regulated by oxygen tension. Eur. J. Immunol., 32, 2866–2873 (2002).
  • 25) Koike, Y., Hisada, T., Utsugi, M., Ishizuka, T., Shimizu, Y., Ono, A., Murata, Y., Hamuro, J., Mori, M., and Dobashi, K., Glutathione redox regulates airway hyperresponsiveness and airway inflammation in mice. Am. J. Respir. Cell Mol. Biol., 37, 322–329 (2007).
  • 26) Bando, N., Yamanishi, R., and Terao, J., Inhibition of immunoglobulin E production in allergic model mice by supplementation with vitamin E and β-carotene. Biosci. Biotechnol. Biochem., 67, 2176–2182 (2003).
  • 27) Constant, S., Pfeiffer, C., Woodard, A., Pasqualini, T., and Bottomly, K., Extent of T cell receptor ligation can determine the functional differentiation of naive CD4+ T cells. J. Exp. Med., 182, 1591–1596 (1995).
  • 28) Schountz, T., Kasselman, J. P., Martinson, F. A., Brown, L., and Murray, J. S., MHC genotype controls the capacity of ligand density to switch T helper (Th)-1/Th-2 priming in vivo. J. Immunol., 157, 3893–3901 (1996).

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