Rhododendrol, a depigmentation-inducing phenolic compound, exerts melanocyte cytotoxicity via a tyrosinase-dependent mechanism

Pigment Cell and Melanoma Research

Volumn 27, Issue 5, 2014, Pages 754-763

  Sasaki, Minoru ^a   Kondo, Masatoshi ^a   Sato, Kohji ^a   Umeda, Mai ^a   Kawabata, Keigo ^a   Takahashi, Yoshito ^a   Suzuki, Tamio ^b   Matsunaga, Kayoko ^c   Inoue, Shintaro ^a  

^a Kanebo Cosmetics Inc   (Japan)

^b YAMAGATA UNIVERSITY   (Japan)

^c FUJITA HEALTH UNIVERSITY SCHOOL OF MEDICINE   (Japan)

Author keywords

Chemical leukoderma; Cytotoxicity; Depigmentation; ER stress; Rhododendrol; Tyrosinase; Vitiligo

Indexed keywords

BUTANOL; CASPASE 3; CHELATING AGENT; COPPER; DEPIGMENTING AGENT; INTERLEUKIN 8; MONOPHENOL MONOOXYGENASE; PHENYLTHIOUREA; REACTIVE OXYGEN METABOLITE; RHODODENDROL; SMALL INTERFERING RNA;

AGARICALES; ANTAGONISTS AND INHIBITORS; APOPTOSIS; CELL CULTURE; CELL SURVIVAL; CHEMICALLY INDUCED; CHEMISTRY; CYTOLOGY; DRUG EFFECTS; ENDOPLASMIC RETICULUM STRESS; ENHANCER REGION; ENZYME ACTIVE SITE; ENZYME LINKED IMMUNOSORBENT ASSAY; ENZYMOLOGY; GENE EXPRESSION PROFILING; GENE EXPRESSION REGULATION; HUMAN; HYPOPIGMENTATION; IC50; MELANOCYTE; METABOLISM; PIGMENTATION; UPREGULATION; VITILIGO;

AGARICALES; APOPTOSIS; BUTANOLS; CASPASE 3; CATALYTIC DOMAIN; CELL SURVIVAL; CELLS, CULTURED; CHELATING AGENTS; COPPER; ENDOPLASMIC RETICULUM STRESS; ENHANCER ELEMENTS, GENETIC; ENZYME-LINKED IMMUNOSORBENT ASSAY; GENE EXPRESSION PROFILING; GENE EXPRESSION REGULATION; HUMANS; HYPOPIGMENTATION; INHIBITORY CONCENTRATION 50; INTERLEUKIN-8; MELANOCYTES; MONOPHENOL MONOOXYGENASE; PHENYLTHIOUREA; PIGMENTATION; REACTIVE OXYGEN SPECIES; RNA, SMALL INTERFERING; SKIN LIGHTENING PREPARATIONS; UP-REGULATION; VITILIGO;

EID: 84907980722     PISSN: 17551471     EISSN: 1755148X     Source Type: Journal    
DOI: 10.1111/pcmr.12269     Document Type: Article

References (28)

1. Basma, A.N., Morris, E.J., Nicklas, W.J., and Geller, H.M. (1995). L-dopa cytotoxicity to PC12 cells in culture is via its autoxidation. J. Neurochem. 64, 825-832.
2. Boissy, R.E., and Manga, P. (2004). On the etiology of contact/occupational vitiligo. Pigment Cell Res. 17, 208-214.
3. Bolognia, J.L., Lapia, K., and Somma, S. (2001). Depigmentation therapy. Dermatol. Ther. 14, 29-34.
4. Carruthers, W. (1978). Modern Methods of Organic Synthesis. (Cambridge, UK: Cambridge University Press), pp. 407-432.
5. Clement, M.V., Long, L.H., Ramalingam, J., and Halliwell, B. (2002). The cytotoxicity of dopamine may be an artefact of cell culture. J. Neurochem. 81, 414-421.
6. Cooksey, C.J., Garratt, P.J., Land, E.J., Pavel, S., Ramsden, C.A., Riley, P.A., and Smit, N.P. (1997). Evidence of the indirect formation of the catecholic intermediate substrate responsible for the autoactivation kinetics of tyrosinase. J. Biol. Chem. 272, 26226-26235.
7. Cummings, M.P., and Nordlund, J.J. (1995). Chemical leukoderma: fact or fancy. Am. J. Contact Dermat. 6, 122-126.
8. Fuchino, H., Konishi, S., Satoh, T., Yagi, A., Saitsu, K., Tatsumi, T., and Tanaka, N. (1996). Chemical evaluation of Betula species in Japan. II. Constituents of Betula platyphylla var. japonica. Chem. Pharm. Bull. (Tokyo) 44, 1033-1038.
9. Fukuda, Y., Nagano, M., and Futatsuka, M. (1998a). Occupational leukoderma in workers engaged in 4-(p-hydroxyphenyl)-2-butanone manufacturing. J. Occup. Health 40, 118-122.
10. Fukuda, Y., Nagano, M., Tsukamoto, K., and Futatsuka, M. (1998b). In vitro studies on the depigmenting activity of 4-(p-hydroxyphenyl)-2-butanone. J. Occup. Health 40, 137-142.
11. Gettler, J.D., and Hammett, L.P. (1943). Rates and temperature coefficients of the hydroxyl ion catalyzed aldol condensation of benzaldehyde with methyl ethyl ketone and acetone. J. Am. Chem. Soc. 65, 1824-1829.
12. Ghosh, S. (2010). Chemical leukoderma: what's new on etiopathological and clinical aspects? Indian J. Dermatol. 55, 255.
13. Hall, A.M., and Orlow, S.J. (2005). Degradation of tyrosinase induced by phenylthiourea occurs following Golgi maturation. Pigment Cell Res. 18, 122-129.
14. Hariharan, V., Klarquist, J., Reust, M.J., Koshoffer, A., Mckee, M.D., Boissy, R.E., and Le Poole, I.C. (2010). Monobenzyl ether of hydroquinone and 4-tertiary butyl phenol activate markedly different physiological responses in melanocytes: relevance to skin depigmentation. J. Invest. Dermatol. 130, 211-220.
15. Inoue, T., Ishidate, Y., Fujita, M., Kubo, M., Fukushima, M., and Nagai, M. (1978). Studies on the constituents of Aceraceae plants. I. Constituents in the leaves and the stem bark of Acer nikoense Maxim. Yakugaku Zasshi 98, 41-46.
16. James, O., Mayes, R., and Stevenson, C. (1977). Occupational vitiligo induced by p-tert-butylphenol, a systemic disease? Lancet 310, 1217-1219.
17. Klabunde, T., Eicken, C., Sacchettini, J.C., and Krebs, B. (1998). Crystal structure of a plant catechol oxidase containing a dicopper center. Nat. Struct. Biol. 5, 1084-1090.
18. Manga, P., Sheyn, D., Yang, F., Sarangarajan, R., and Boissy, R.E. (2006). A role for tyrosinase-related protein 1 in 4-tert-butylphenol-induced toxicity in melanocytes: implications for vitiligo. Am. J. Pathol. 169, 1652-1662.
19. Oakley, A.M. (1996). Rapid repigmentation after depigmentation therapy: vitiligo treated with monobenzyl ether of hydroquinone. Australas. J. Dermatol. 37, 96-98.
20. Oikawa, A., Nakayasu, M., Nohara, M., and Tchen, T.T. (1972). Fate of L-(3, 5-3H) tyrosine in cell-free extracts and tissue cultures of melanoma cells: a new assay method for tyrosinase in living cells. Arch. Biochem. Biophys. 148, 548-557.
21. Olivares, C., Garcia-Borron, J.C., and Solano, F. (2002). Identification of active site residues involved in metal cofactor binding and stereospecific substrate recognition in Mammalian tyrosinase. Implications to the catalytic cycle. Biochemistry 41, 679-686.
22. Pomerantz, S.H. (1966). The tyrosine hydroxylase activity of mammalian tyrosinase. J. Biol. Chem. 241, 161-168.
23. Ryazanova, A.D., Alekseev, A.A., and Slepneva, I.A. (2012). The phenylthiourea is a competitive inhibitor of the enzymatic oxidation of DOPA by phenoloxidase. J. Enzyme Inhib. Med. Chem. 27, 78-83.
24. Toosi, S., Orlow, S.J., and Manga, P. (2012). Vitiligo-inducing phenols activate the unfolded protein response in melanocytes resulting in upregulation of IL6 and IL8. J. Invest. Dermatol. 132, 2601-2609.
25. Toyofuku, K., Wada, I., Valencia, J.C., Kushimoto, T., Ferrans, V.J., and Hearing, V.J. (2001). Oculocutaneous albinism types 1 and 3 are ER retention diseases: mutation of tyrosinase or Tyrp1 can affect the processing of both mutant and wild-type proteins. FASEB J. 15, 2149-2161.
26. Van Den Boorn, J.G., Picavet, D.I., Van Swieten, P.F. et al. (2011). Skin-depigmenting agent monobenzone induces potent T-cell autoimmunity toward pigmented cells by tyrosinase haptenation and melanosome autophagy. J. Invest. Dermatol. 131, 1240-1251.
27. Yang, F., and Boissy, R.E. (1999). Effects of 4-tertiary butylphenol on the tyrosinase activity in human melanocytes. Pigment Cell Res. 12, 237-245.
28. Yang, F., Sarangarajan, R., Le Poole, I.C., Medrano, E.E., and Boissy, R.E. (2000). The cytotoxicity and apoptosis induced by 4-tertiary butylphenol in human melanocytes are independent of tyrosinase activity. J. Invest. Dermatol. 114, 157-164.