Abstract
This chapter summarizes our recent studies on the regulation of melanin synthesis, a chemical pathway which bears a striking resemblance to that proposed to be involved in neuromelanin production from Dopamine (DN).1 Two key enzymes, DOPAchrome tautomerase (DCT) and macrophage migration inhibitory factor (MIF), have analogous catalytic actions in those biosynthetic pathways which may be linked to their roles as survival enzymes in melanocytes and in catecholaminergic neurons, respectively.
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References
W.S. Enochs, M.J. Nilges, and H.M. Swartz. Purified human neuromelanin, synthetic dopamine melanin as a potential model pigment, and the normal human substantia nigra: characterization by electron paramagnetic resonance spectroscopy, J. Neurochem. 61, 68–79 (1993).
J.M. Pawelek, A.M. Körner, A. Bergstrom, and J. Bolognia. New regulators of melanin biosynthesis and the autodestruction of melanoma cells, Nature 286, 617–619 (1980).
K. Urabe, P. Aroca, K. Tsukamoto, D. Mascagna, A. Palumbo, G. Prota, and V.J. Hearing. The inherent cytotoxicity of melanogenic intermediates: a revision, Biochim. Biophys. Acta 1221, 272–278 (1994).
K.P. Steel, D.R. Davidson, and I.J. Jackson. TRP2/DT, a new early melanoblast marker, shows that steel growth factor (c-kit ligand) is a survival factor, Development 115, 1111–1119 (1992).
E. Rosengren, R. Bucala, P. Aman, L. Jacobsson, G. Odh, C.N. Metz, and H. Rorsman. The immunoregulatory mediator macrophage migration inhibitory factor (MIF) catalyzes a tautomerization reaction, Mol. Med. 2, 143–149 (1996).
J.R. David. Delayed hypersensitivity in vitro: its mediation by cell-free substances formed by lymphoic cell-antigen interaction, Proc. Natl. Acad. Sci. USA 56, 72–77 (1966).
W.Y. Weiser, P.A. Temple, J.S. Witek-Giannotti, H.G. Remold, S.C. Clark, and J.R. David. Molecular cloning of a cDNA encoding a human macrophage migration inhibitory factor, Proc. Natl. Acad. Sci. USA 86, 7522–7526(1989).
N. Esumi, M. Budarf, L. Ciccarelli, B. Sellinger, C.A. Kozak, and G.J. Wistow. Conserved gene structure and genomic linkage for D-dopachrome tautomerase (DDT) and MIF, Mamm. Genome 9, 753–757 (1998).
J. Matsunaga, D. Sinha, L. Pannell, C. Santis, F. Solano, G.J. Wistow, and V.J. Hearing. Enzyme activity of macrophage migration inhibitory factor (MIF) towards oxidized catecholamines, J. Biol. Chem. 274, 3268–3271 (1999).
J. Matsunaga, D. Sinha, F. Solano, C. Santis, G.J. Wistow, and V.J. Hearing. Macrophage migration inhibitory factor (MIF) — Its role in catecholamine metabolism, Cell Mol. Biol. 45, 1035–1041 (1999).
U.S. Ito, K. Wakamatsu, and L. Zecca. Structure and function of neuromelanin, in: Catecholamine Research: From Molecular Insights to Clinical Medicine, edited by T. Nagatsu, R. Nabeshima, R. McCarthy, and D. Goldstein (Kluwer Academic/Plenum Pulbishers (New York, 2001) pp. (in this volume).
K.L. Double, L. Zecca, P. Costi, M. Mauer, C. Griesinger, S. Ito, D. Ben-Shacher, G. Bringmann, R.G. Fariello, P. Riederer, and M. Gerlach. Structural characteristics of human substantia nigra neuromelanin and synthetic dopamine melanins, J. Neurochem. 75, 2583–2589 (2000).
D.G. Graham. Oxidative pathways for catecholamines in the genesis of neuromelanin and cytotoxic quinones, Mol. Pharmacol. 14, 633–643 (1978).
F. Solano, V.J. Hearing, and J.C. García-Borrín. Neurotoxicity due to o-quinones: neuromelanin formation and possible mechanisms for o-quinone detoxification, Neurotoxicity Res. 1, 153–169 (2000).
J. Matsunaga, P.A. Riley, N. Kobayashi, N. Matsunaga, I. Takeuchi, H. Tagami, and V.J. Hearing. Cytotoxicity of intermediates in the melanin and neuromelanin biosynthetic pathways on B16F10 and Neuro2A cells, (submitted), (2001).
D. Offen, I. Ziv, A. Barzilai, S. Gorodin, E. Glater, A. Hochman, and E. Melamed. Dopamine-melanin induces apoptosis in PC12 cells; possible implications for the etiology of Parkinson’s disease, Neurochem. Int. 31, 207–216(1997).
N.G. Lindquist, B.S. Larsson, and A. Lyden-Sokolowski. Neuromelanin and its possible protective and destructive properties, Pigment Cell Res. 1, 133–136 (1987).
G. Prota, and M. d’Ischia. Neuromelanin: a key to Parkinson’s disease, Pigment Cell Res. 6, 333–335 (1993).
M. d’Ischia, and G. Prota. Biosynthesis, structure and function of neuromelanin and its relation to Parkinson’s disease: a critical update, Pigment Cell Res. 10, 370–376 (1997).
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Matsunaga, J., Riley, P.A., Solano, F., Hearing, V.J. (2002). Biosynthesis of Neuromelanin and Melanin: The Potential Involvement of Macrophage Inhibitory Factor and Dopachrome Tautomerase as Rescue Enzymes. In: Nagatsu, T., Nabeshima, T., McCarty, R., Goldstein, D.S. (eds) Catecholamine Research. Advances in Behavioral Biology, vol 53. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-3538-3_64
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DOI: https://doi.org/10.1007/978-1-4757-3538-3_64
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