Abstract
Tyrosine is generally considered to be the physiological precursor of melanins and tyrosinase the enzyme responsible. However, recent studies have shown that also peroxidases are involved in the biosynthesis of melanins. These enzymes use hydrogen peroxide to oxidise various phenol substrates. In this paper, we used a substrate other than tyrosine, i.e. 5-hydroxytryptophan, to verify if its peroxidase/H2O2-mediated oxidation gave rise to the formation of melanin. We also subjected 5-hydroxytryptophan to the action of tyrosinase, for comparison purposes. We observed that both enzymes converted this substrate to melanin and that peroxidase, in the presence of hydrogen peroxide, was much more effective than tyrosinase in catalysing the oxidative polymerization of 5-hydroxytryptophan, with the formation of insoluble black melanin-like pigments. Samples deriving from the reaction-substrate enzyme were ultrafiltered at different times through an Amicon ultrafiltration cell equipped with an Amicon Diaflo XM-50 membrane, in order to remove the enzyme, and immediately lyophilised. The resulting samples were analysed by matrix assisted laser desorption/ionisation (MALDI) mass spectrometry, which clearly identified several oligomer species in the reaction mixture.This work was undertaken to investigate the possible precursors of neuromelanin and the enzyme responsible for melanogenesis in brain. since although the central nervous system does not contain tyrosinase, it is rich in peroxidase and hydrogen peroxide.
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
I H. Mason, The chemistry of melanin III. Mechanisms of the oxidation of dihydroxyphenylalanine by tyrosinaseJ.Biol.Chem.172, 83–92 (1948).
G. Prota, The role of peroxidase in melanogenesis revisitedPigment Cell Res. Suppl. 2, 25–31 (1992).
M. d’Ischia, A. Napolitano and G. Prota, Peroxidase as an alternative to tyrosinase in the oxidative polymerization of 5,6-dihydroxyindoles tomelanin(s) Biochem. Biophys. Acta 1073, 423–430 (1991).
M.R. Okun, Peroxidase activity in normal and neoplastic melanocytesJ. Invest. Dermatol.48, 461–465, 1967
G. Prota, in Melanins and Melanogenesis, (Acad. Press, New York, 1992), pp 1–290.
M.R. Okun L.Edelstein, N.Or, G. Hamada and B. Donnellan, Histochemical studies of conversion of tyrosine and Dopa to melanin mediated by mammalian peroxidaseLife Sei.part II, 9, 491–505 (1970).
M.R. Okun, L. Eldestein, N.Or,G. Hamada and B. Donnellan, The role of peroxidase versus the role of tyrosinase in enzimatic conversion of tyrosine to melanin in melanocytes, mast cells, and eosinophils.An autoradiographic-histochemical study.J.Invest. Dermatol. 55, I-12 (1970).
M.R. Okun, R.P. Patel, B. Donnellan and L. Eldestein, Subcellular localization of peroxidase-mediated oxidation of tyrosine to melaninPigment Cell1, 98–110 (1973).
M. Okun, B. Donnellan, R. Patel and L. Edelstein, Subcellular demonstration of peroxidatic oxidation of tyrosine to melanin using dihydroxyfumarate as cofactor in mouse melanoma cellsJ.Invest. Dermatol.61, 60–66 (1973).
M.R. Okun, L.Edelstein, R.P. Patel and B. Donnellan, A revised concept of mammalian melanogenesis: The possible synergistic functions of aerobic dopa oxidase and peroxidaseYale J. Biol. Med.46, 535540 (1973).
R.P. Patel, M.R. Okun, L.M.Edelstein and D.Epstein, Biochemical studies on the peroxidase-mediated oxidation of tyrosine to melanin: Demonstration of the hydroxylation of tyrosine by plant and human peroxidasesBiochem. J. 124439–441 (1971).
R.P. Patel, M.R. Okun, L.M. Edelstein and N. Cariglia, Peroxidatic conversion of tyrosine to dopachromeJ.lnvest. Derrnntol.63, 374–377 (1974).
R.P. Patel, M.R. Okun, A. Wendell, G.F. Wilgram and L. Edelstein, Inability of murine melanoma “tyrosinase” (Dopa oxidase) to oxidize tyrosine in the presence or absence of Dopa or dihydroxyfumarate cofactorJ./nvest.Dermatol.61, 55–59 (1973).
M. d’Ischia, A. Napolitano, K. Tsiakas and G. Prota, New intermediates in the oxidative polymerisation of 5,6dihydroxyindole to melanin promoted by the peroxidase/H202 systemTetrahedron46, 5789–5796 (1990).
A. Bertazzo, C.V.L. Costa, G. Allegri, M. Schiavolin, D. Favretto and P. Traldi, Enzymatic oligomerization of tyrosine by tyrosinase and peroxidase studied by MALDI-MSRapid Catunun. Mass Speetrom.13, 542–547 (1999).
D. Favretto, A. Bertazzo, C.V.L. Costa, G. Allegri, P. Traldi, A study on the enzymatic oligomerization or 5hydroxytryptamine using Matrix-assisted Laser Desorption/lonization Mass SpectrometryRapid Commun. MassSpectrom. 111038–1042 (1997).
D. Favretto, A. Bertazzo, C.V.L. Costa, G. Allegri, P. Traldi, The role of peroxidase in the oligomerization of 5-hydroxytryptamine investigated by Matrix-assisted Laser Desorption/lonization Mass SpectrometryRapid Comrnun.Mass Specn’om.12, 193–197 (1998).
M.Z. Wrona and G. Dryhurst, Oxidation chemistry of 5-hydroxytryptamine. Part II. Mechanism and products formed at millimolar concentrations in acidic aqueous solutionJ.Electroanal. Chem.Inteifacial Electrochern.278, 249–267 (1990).
L. Musajo, C.A. Benassi, G. Allegri, E. Levorato and A. De Antoni, Azione della tirosinasi sul triptotanoesu suoi derivati metabolici,Chin. Ind. 48,1221 (1966).
C.A. Benassi, F.M. Veronese, A. De Antoni and P. Paietta, Prodotti dell’ossidazione del triptofano con acido performicoGaz_.Chim.11nl. 97.3–17 (1967).
L. Musajo, A. De Antoni, G. Allegri, E. Levorato and C.A. Benassi, Azione della tirosinasi sul triptofano c su suoi derivati metabolici, Convegno CNR Chimica del Farmaco e dei Prodotti Biologicamente Attivi. Roma 30–3I genn. -I febbr. 1967Atti CNR Roma 283,3–5 (1969).
A. De Antoni, G. Allegri and C. Costa, Azione di sistemi enzimatici ad attività politenolossidasica sul triptofano e suoi derivati metabolici, Gn-_.Chim.ltal. 1001039–1049 (1970).
G. Allegri, A. De Antoni, F. Baccichetti and C. Costa, Incorporation of D,L-tryptophan-benzene ring-“C (U) and D,L-tryptophan-methylene-’’C into the melanin of mouse Harding--Passey melanoma.Gazz.Chitn.lial. 102,426–430 (1972).
A. De Antoni, G. Allegri, C. Costa and F. Bordin, Melanogenesis from tryptophan. Biogenetic experiments with Harding-Passey mouse melanomaExperienlia 30,600–601 (1974).
C. Costa, G. Allegri and A. De Antoni, Studies on melanogenesis of tryptophan on Harding-Passey mouse melanomaActa Vitamin. Enz ‘mol. 29, 223–226 (1975).
G. Allegri, M. Biasiolo, G. Frison, B. Pelli and P. Traldi, Collisional spectroscopy in structural characterization of melanins 2-Laser Desorption experiments on bio-and synthetic tryptophan melaninsBiomed.Environ.Mass Spectrom.15353–355 (1988).
G. Allegri, Role of tryptophan in melanogenesis, in Adv.Tryptophan Research, edited by I. Ishiguro, R. Kido, T, Nagatsu, Y. Nagamura, Y. Ohta, (Fuijta Health University Press, Toyoake, 1992), pp 185–189.
A. Bertazzo, M. Biasiolo, C. Costa, G. Allegri, G. Elli, R. Seraglia and P. Traldi, Laser desorption ionization mass spectrometry in the study of natural and synthetic melanins. 11-Serotonin melanins.Biot Mass Spectrom. 23,391–398 (1994).
G. Allegri, A. Bertazzo, C. Costa, R. Seraglia and P. Traldi, Investigation on melanin biosynthesis from 5,6dihydroxytryptamine by matrix assisted laser desorption/ionization mass spectrontetrRapid Commun.Mass Spectrom. 10419–423 (1996).
A. Bertazzo, C. Costa, G. Allegri, D. Favretto and P. Traldi, A study on the enzymatic oligomerization of 5,7-dihydroxytryptamine by MALDI/MSRapid Commun. Mass Spectrom. 101299–1303 (1996).
G. Allegri, G. Frison, B. Pelli and P. Traldi, Collisional spectroscopy in structural characterization of melanins: I. A first study on [CsH7ON]’ ions originating from pyrolysis of biosynthetic and synthetic thryptophan melaninsPigment Cell Res. 1,87–93 (1987).
A. Bertazzo, D. Favretto, C.V.L. Costa, G. Allegri and P. Traldi, Influence of peroxidase on the oligomerization of 5,6- and 5,7-dihydroxytryptamine investigated by Matrix-assisted Laser Desorption/Ionization Mass SpectrometryRapid Commun. Mass Spectrom. 12,767–772 (1998).
L.M. Ambani and M.H. Van Woert, Catalase and peroxidase in human brainTrans. Am.Neurol. Assoc. 98.7–10 (1973).
A.D. Rodgers and G. Curzon, Melanin formation by human brain in vitro.J.Neurochem. 24,1123–1129 (1975)
K.C. Das, M.B. Abramson and R. Katzman, Neuronal pigments: spectroscopic characterization of human brain melan inJ.Neurochen. 30601–606 (1978).
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2003 Springer Science+Business Media New York
About this chapter
Cite this chapter
Allegri, G., Vogliardi, S., Bertazzo, A., Costa, C.V.L., Seraglia, R., Traldi, P. (2003). Involvement of 5-hydroxytryptophan in Melanogenesis. In: Allegri, G., Costa, C.V.L., Ragazzi, E., Steinhart, H., Varesio, L. (eds) Developments in Tryptophan and Serotonin Metabolism. Advances in Experimental Medicine and Biology, vol 527. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-0135-0_85
Download citation
DOI: https://doi.org/10.1007/978-1-4615-0135-0_85
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-4939-6
Online ISBN: 978-1-4615-0135-0
eBook Packages: Springer Book Archive