Hydrogen peroxide generation associated with the oxidations of the eumelanin precursors 5,6-dihydroxyindole and 5,6-dihydroxyindole-2-carboxylic acid

Melanoma Research

Volumn 6, Issue 5, 1996, Pages 341-349

  Nappi, A J ^a   Vass, E ^a  

^a LOYOLA UNIVERSITY CHICAGO   (United States)

Author keywords

5,6 dihydroxyindole; 5,6 dihydroxyindole 2 carboxylic acid; H2O2; melanogenesis; salicylate hydroxylation

Indexed keywords

CATALASE; DIHYDROXYINDOLE; DIHYDROXYINDOLE CARBOXYLIC ACID; HYDROGEN PEROXIDE; MELANIN; MONOPHENOL MONOOXYGENASE; PEROXIDASE; UNCLASSIFIED DRUG;

ARTICLE; CARCINOGENESIS; CONTROLLED STUDY; MELANOGENESIS; MELANOMA; NONHUMAN; PRIORITY JOURNAL;

CATALASE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; ENZYME INHIBITORS; HYDROGEN PEROXIDE; INDOLES; IRON; KINETICS; MELANINS; MONOPHENOL MONOOXYGENASE; OXIDATION-REDUCTION; PEROXIDASE; SALICYLATES;

EID: 0029923970     PISSN: 09608931     EISSN: None     Source Type: Journal    
DOI: 10.1097/00008390-199610000-00001     Document Type: Article

References (52)

1. Kameyama K, Jimenze J, Muller J, et al. Regulation of mammalian melanogenesis by tyrosinase inhibition. Differentiation 1989; 42: 28-36.
2. Kameyama K, Takemura T, Hamada Y, et al. Pigment product in murine melanoma cells is regulated by a tyrosinase-related protein 1 (TRP1), DOPAchrome tautomerase (TRP2), and a melanogenic inhibitor. J Invest Dermatol 1993; 100: 126-131.
3. Kameyama K, Sakai C, Nishiyama S, et al. The expression of tyrosinase, tyrosinase-related proteins 1 and 2 (TRP1 and TRP2), the silver protein, and a melanogenic inhibitor in human melanoma cells of differing melanogenic activities. Pigment Cell Res 1995; 8: 97-104.
4. Hearing VJ, Tsukamoto K. Enzymatic control of pigmentation in mammals. FASEB J 1991; 5: 2902-2909.
5. Winder AJ, Harris H. Induction of tyrosinase in human melanoma cells by 1-tyrosine phosphate and cytochalasin D. Exp Cell Res 1992; 199: 248-254.
6. Winder A, Kobayashi T, Tsukamoto K, et al. The tyrosinase gene family - interactions of melanogenic proteins to regulate melanogenesis. Cell Mol Biol Res 1994; 40: 613-626.
7. Sanchez-Ferrer A, Rodriguez-Lopez JN, Garcia-Canovas F, et al. Tyrosinase: a comprehensive review of its mechanism. Biochim Biophys Acta 1995; 1247: 1-11.
8. Pawelek JM. After dopachrome? Pigment Cell Res 1991; 4: 53-62.
9. Tsukamoto K, Palumbo A, d'Ischia M, et al. 5,6-Dihydroxyindole-2-carboxylic acid is incorporated in mammalian melanin. Biochem J 1992; 286: 491-495.
10. Halaban R, Moellmann G. Murine and human b locus pigmentation genes encode a glycoprotein (gp75) with catalase activity. Proc Natl Acad Sci USA 1990; 87: 4809-4813.
11. Jimenez-Cervantes C, Solano F, Kobayashi T, et al. A new enzymatic function in the melanogenic pathway. The 5,6-dihydroxyindole-2-carboxylic acid oxidase activity of tyrosinase-related protein-1 (TRP1). J Biol Chem 1994; 269: 17993-8000.
12. Jimenez M, Maloy WL, Hearing VJ. Specific identification of an authentic clone for mammalian tyrosinase. J Biol Chem 1989; 264: 3397-3403.
13. Jimenez M, Tsukamoto K, Hearing VJ. Tyrosinases from two different loci are expressed by normal and by transformed melanocytes. J Biol Chem 1991; 266: 1147-1156.
14. Zhao H, Zhao Y, Nordlund JJ, et al. Human TRP-1 has tyrosine hydroxylase but no dopa oxidase activity. Pigment Cell Res 1994; 7: 131-140.
15. Ito S, Wakamatsu K. Melanin chemistry and melanin precursors in melanoma. J Invest Dermatol 1989; 92: 261S-265S.
16. Orlow SJ, Osber MP, Pawelek JM. Synthesis and characterization of melanins from dihydroxyindole-2-carboxylic acid and dihydroxyindole. Pigment Cell Res 1992; 5: 113-121.
17. Aroca P, Solano F, Salinas C, et al. Regulation of the final phase of mammalian melanogenesis. The role of dopachrome tautomerase and the ratio between 5,6-dihydroxyindole-2-carboxylic acid and 5,6-dihydroxyindole. Eur J Biochem 1992; 208: 155-163.
18. Odh G, Hindemith A, Carstam R, et al. Melanins in IGR 1 melanoma cells Pigment Cell Res 1994; 7: 419-427.
19. Napolitano A, Palumbo A, Misuraca G, et al. Inhibitory effect of melanin precursors on arachidonic acid peroxidation. Biochim Biophys Acta 1993; 1168: 175-180.
20. Urabe K, Aroca P, Tsukamoto K, et al. The inherent cytotoxicity of melanin precursors: a revision. Biochim Biophys Acta 1994; 1221: 272-278.
21. d'Ischia M, Napolitano A, Prota G. Peroxidase as an alternative to tyrosinase in the oxidative polymerization of 5,6-dihydroxyindoles to melanin(s). Biochim Biophys Acta 1991; 1073: 423-430.
22. Radzik DM, Roston DA, Kissenger PT. Determination of hydroxylated aromatic compounds produced in a superoxide-dependent formation of hydroxyl radicals by liquid chromatography/electrochemistry. Anal Biochem 1983; 131: 458-464.
23. Floyd RA, Watson JJ, Wong PK. Sensitive assay of hydroxyl free radical formation utilizing high pressure liquid chromatography with electrochemical detection of phenol and salicylate hydroxylation products. J Biochem Biophys Methods 1984; 10: 221-235.
24. Maskos Z, Rush JD, Koppenol WH. The hydroxylation of phenylalanine and tyrosine: a comparison with salicylate and tryptophan. Arch Biochem Biophys 1992; 296: 521-529.
25. +. Free Rad Biol Med 1992; 13: 581-583.
26. .OH) formation reflected by salicylate hydroxylation and neuromelanin: in vivo markers for oxidant injury of nigral neurons. Ann NY Acad Sci 1993; 679: 370-375.
27. Nappi AJ, Vass E, Prota G, et al. The effects of hydroxyl radical attack on dopa, dopamine, 6-hydroxydopa, and 6-hydroxydopamine. Pigment Cell Res 1995; 8: 283-293.
28. Tsukamoto K, Jackson IL, Urabe K, et al. A second tyrosinase-related protein, TRP-2, is a melanogenic enzyme termed dopachrome tautomerase. EMBO J 1992; 11: 519-526.
29. Kwon BS. Pigmentation genes: the tyrosinase gene family and the pmel 17 gene family. J Invest Dermatol 1993; 101: 141-144.
30. Donatien PD, Orlow SJ. Interaction of melanosomal proteins with melanin. Eur J Biochem 1995; 232: 159-164.
31. Kobayashi T, Urabe K, Orlow SJ, et al. The Pmel 17/silver locus protein. Characterization and investigation of its melanogenic function. J Biol Chem 1994; 269: 29198-29205.
32. Orlow SJ, Zhou BK, Chakraborty AK, et al. High-molecular-weight forms of tyrosinase and the tyrosinase-related proteins: evidence for a melanogenic complex. J Invest Dermatol 1994; 103: 196-201.
33. Kobayashi T, Urabe K, Winder A, et al. DHICA oxidase activity of TRP1 and interactions with other melanogenic enzymes. Pigment Cell Res 1994; 7: 227-234.
34. Kobayashi T, Urabe K, Winder A, et al. Tyrosinase related protein 1 (TRP1) functions as a DHICA oxidase in melanin biosynthesis. EMBO J 1994; 13: 5818-5825.
35. Kroumpouzos G, Urabe K, Kobayashi T, et al. Functional analysis of the slaty gene product (TRP2) as dopachrome tautomerase and the effect of a point mutation on its catalytic function. Biochem Biophys Res Commun 1994; 202: 1060-1068.
36. Vijayasaradhi S, Doskoch PM, Wolchok J, et al. Melanocyte differentiation marker Gp75, the Brown locus protein, can be regulated independently of tyrosinase and pigmentation. J Invest Dermatol 1995; 105: 113-119.
37. Orlow SJ. Melanosomes are specialized members of the lysosomal lineage of organelles. J Invest Dermatol 1995; 105: 3-7.
38. Shibata T, Prota G, Mishima Y. Non-melanosomal regulatory factors in melanogenesis. J Invest Dermatol 1993; 100: 274S-280S.
39. Prota G. The role of peroxidase in melanogenesis revisited. Pigment Cell Res 1992; Suppl. 1: 25-31.
40. Prota G. Regulatory mechanisms of melanogenesis: beyond the tyrosinase concept. J Invest Dermatol 1993; 100: 156S-161S.
41. Karg E, Odh G, Wittbjer A, et al. Hydrogen peroxide as an inducer of elevated tyrosinase level in melanoma cells. J Invest Dermatol 1993; 100: 209S-213S.
42. Parsons PG. Modification of dopa toxicity in human tumour cells. Biochem Pharmacol 1985; 34: 1801-1807.
43. 2 oxidation of dopamine. J Med Chem 1995; 38: 917-922.
44. Ito S, Inoue S, Fujita K. The mechanism of toxicity of 5-S-cysteinyldopa to tumour cells. Hydrogen peroxide as a mediator of cytotoxicity. Biochem Pharmacol 1983; 32: 2079-2081.
45. Singh S, Dryhurst G. Further insights into the oxidation chemistry and biochemistry of the serotonergic neurotoxin 5,6-dihydroxytryptamine.J Med Chem 1990; 33: 3035-3044.
46. Salinas C, Garcia-Borron JC, Solano F, et al. Dopachrome tautomerase decreases the binding of indolic melanogenesis intermediates to proteins. Biochim Biophys Acta 1994; 1204: 53-60.
47. Misra HP, Fridovich I. The univalent reduction of oxygen by reduced flavins and quinones. J Biol Chem 1972; 247: 188-192.
48. Sullivan SG, Stern A. Effects of Superoxide dismutase and catalase on catalysis of 6-hydroxydopamine and 6-aminodopamine autoxidation by iron and ascorbate. Biochem Pharmacol 1981; 30: 2279-2285.
49. Fridovich I. Superoxide dismutases. Advances in Enzymology and Related Areas of Molecular Biology 1986; 58: 61-97.
50. Kalyanaraman B, Korytowski W, Pilas B, et al. Reaction between ortho-semiquinones and oxygen: pulse radiolysis, electron spin resonance, and oxygen uptake studies. Arch Biochem Biophys 1988; 266: 277-284.
51. Lambert C, Chacon JN, Chedekel MR, et al. A pulse radiolysis investigation of the oxidation of indolic melanin precursors: evidence for indolequinones and subsequent intermediates. Biochim Biophys Acta 1989; 993: 12-20.
52. Lambert C, Land EJ, Riley PA, et al. A pulse radiolysis investigation of the oxidation of methoxylated metabolites of indolic melanin precursors. Biochim Biophys Acta 1990; 1035: 319-324.