Melanin biosynthesis (Homo sapiens)

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8, 1367511, 12, 151, 3, 4, 10, 14299169melanosome lumencytosolDopachromeL-DopaDCT pheomelanin2-S-Cysteinyl-DOPA CO2O2TYR:2xCu2+H2OSLC45A2Cu2+ Benzothiazine EumelaninTYR benzothiazole DHIDCT:2xZn2+IQCAL-Dopa7-(2-amino-2-carboxyethyl)-5-hydroxy-3,4-dihydro-2H-1,4-benzothiazin-3-one 7-(2-amino-2-carboxyethyl)-5-hydroxy-2H-1,4-benzothiazine-3-carboxylic acid DHICA L-Dopa2,5-S,S'-dicysteinyldopa Zn2+ L-TyrDHICAhydroxylH+DHI DHI, DHICAL-DopaquinoneO2CysteinyldopaisomersLeucodopachrome5-S-Cysteinyldopa TYRP1OCA2H2OBT, BTCA, BZ, ODHBTL-Cys


Description

Melanin biosynthesis takes place in specialized cells called melanocytes, within membrane-bound organelles referred to as melanosomes. Melanosomes are transferred via dendrites to surrounding keratinocytes. Keratinocytes and melanocytes are collectively known as 'the epidermal melanin unit'. Each melanocyte is in contact with approximately 40 keratinocytes in the basal and suprabasal layers (Cichorek et al. 2013). Melanocytes are distributed in the epidermis, hair follicles, the inner ear and the eye (Yamaguchi et al. 2007, Tolleson 2005).

Melanocytes in mammals and birds produce two chemically distinct types of melanin, black to brown eumelanin and yellow to reddish-brown pheomelanin (Ito & Wakamatsu 2008, Simon et al. 2009, d'Ischia et al. 2013). These differ in their responses to UV radiation; eumelanin has the ability to convert absorbed light energy into heat energy (Meredith & Riesz 2004) and to detoxify reactive oxygen species (ROS) (Bustamante et al. 1993), while pheomelanin is a phototoxic pro-oxidant (Samokhvalov 2005). Most natural melanin pigments contain eumelanin and pheomelanin (Ito & Wakamatsu 2003) and are termed 'mixed' melanins. Neuromelanins are mixed melanin-like pigments which are mainly found in neurons of the substantia nigra and locus coeruleus (Fedorow et al. 2005). Synthesis of NM may prevent the accumulation of toxic catechol derivatives (Zecca et al. 2003). NM can sequester a variety of potentially damaging molecules such as beta-carbolines, heavy metal ions and 1-methyl-4-phenylpyridinium (MPP+) (D'Amato et al. 1986), a drug which causes Parkinson's Disease-like symptoms. Models suggest that mixed melanogenesis occurs in three stages (Ito et al. 2000). The initial stage of melanin biosynthesis is the production of cysteinyldopas, which continues while sufficient cysteine is available. The second stage is the oxidation of cysteinyldopas to produce pheomelanin, which continues while cysteinyldopa concentration is sufficiently high. The last stage is the production of eumelanin, which begins when cysteinyldopas and cysteine are depleted. The ratio of eumelanin to pheomelanin is determined by tyrosinase activity and the availability of tyrosine and cysteine (Land et al. 2003). View original pathway at Reactome.

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Pathway is converted from Reactome ID: 5662702
Reactome-version 
Reactome version: 75
Reactome Author 
Reactome Author: Jupe, Steve

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Bibliography

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  1. Cullinane AR, Vilboux T, O'Brien K, Curry JA, Maynard DM, Carlson-Donohoe H, Ciccone C, NISC Comparative Sequencing Program, Markello TC, Gunay-Aygun M, Huizing M, Gahl WA.; ''Homozygosity mapping and whole-exome sequencing to detect SLC45A2 and G6PC3 mutations in a single patient with oculocutaneous albinism and neutropenia.''; PubMed Europe PMC Scholia
  2. Young TE, Griswold JR, Hulbert MH.; ''Melanin. I. Kinetics of the oxidative cyclization of dopa to dopachrome.''; PubMed Europe PMC Scholia
  3. Potterf SB, Furumura M, Sviderskaya EV, Santis C, Bennett DC, Hearing VJ.; ''Normal tyrosine transport and abnormal tyrosinase routing in pink-eyed dilution melanocytes.''; PubMed Europe PMC Scholia
  4. Hearing VJ, Ekel TM, Montague PM, Nicholson JM.; ''Mammalin tyrosinase. Stoichiometry and measurement of reaction products.''; PubMed Europe PMC Scholia
  5. Land EJ, Riley PA.; ''Spontaneous redox reactions of dopaquinone and the balance between the eumelanic and phaeomelanic pathways.''; PubMed Europe PMC Scholia
  6. Wakamatsu K, Ohtara K, Ito S.; ''Chemical analysis of late stages of pheomelanogenesis: conversion of dihydrobenzothiazine to a benzothiazole structure.''; PubMed Europe PMC Scholia
  7. Meredith P, Sarna T.; ''The physical and chemical properties of eumelanin.''; PubMed Europe PMC Scholia
  8. d'Ischia M, Wakamatsu K, Napolitano A, Briganti S, Garcia-Borron JC, Kovacs D, Meredith P, Pezzella A, Picardo M, Sarna T, Simon JD, Ito S.; ''Melanins and melanogenesis: methods, standards, protocols.''; PubMed Europe PMC Scholia
  9. MASON HS.; ''The chemistry of melanin; mechanism of the oxidation of dihydroxyphenylalanine by tyrosinase.''; PubMed Europe PMC Scholia
  10. Toyofuku K, Valencia JC, Kushimoto T, Costin GE, Virador VM, Vieira WD, Ferrans VJ, Hearing VJ.; ''The etiology of oculocutaneous albinism (OCA) type II: the pink protein modulates the processing and transport of tyrosinase.''; PubMed Europe PMC Scholia
  11. Rooryck C, Roudaut C, Robine E, Müsebeck J, Arveiler B.; ''Oculocutaneous albinism with TYRP1 gene mutations in a Caucasian patient.''; PubMed Europe PMC Scholia
  12. Kamaraj B, Purohit R.; ''Mutational analysis of oculocutaneous albinism: a compact review.''; PubMed Europe PMC Scholia
  13. Ito S, Wakamatsu K.; ''Chemistry of mixed melanogenesis--pivotal roles of dopaquinone.''; PubMed Europe PMC Scholia
  14. Sturm RA.; ''Molecular genetics of human pigmentation diversity.''; PubMed Europe PMC Scholia
  15. Olivares C, Jiménez-Cervantes C, Lozano JA, Solano F, García-Borrón JC.; ''The 5,6-dihydroxyindole-2-carboxylic acid (DHICA) oxidase activity of human tyrosinase.''; PubMed Europe PMC Scholia
  16. Kroumpouzos G, Urabe K, Kobayashi T, Sakai C, Hearing VJ.; ''Functional analysis of the slaty gene product (TRP2) as dopachrome tautomerase and the effect of a point mutation on its catalytic function.''; PubMed Europe PMC Scholia

History

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CompareRevisionActionTimeUserComment
114713view16:19, 25 January 2021ReactomeTeamReactome version 75
113158view11:22, 2 November 2020ReactomeTeamReactome version 74
112386view15:32, 9 October 2020ReactomeTeamReactome version 73
101290view11:17, 1 November 2018ReactomeTeamreactome version 66
100827view20:48, 31 October 2018ReactomeTeamreactome version 65
100368view19:23, 31 October 2018ReactomeTeamreactome version 64
99915view16:07, 31 October 2018ReactomeTeamreactome version 63
99470view14:39, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99124view12:40, 31 October 2018ReactomeTeamreactome version 62
93931view13:45, 16 August 2017ReactomeTeamreactome version 61
93517view11:25, 9 August 2017ReactomeTeamreactome version 61
87884view12:23, 25 July 2016RyanmillerOntology Term : 'amino acid metabolic pathway' added !
87883view12:21, 25 July 2016RyanmillerOntology Term : 'classic metabolic pathway' added !
86614view09:22, 11 July 2016ReactomeTeamreactome version 56
83175view10:17, 18 November 2015ReactomeTeamVersion54
81544view13:05, 21 August 2015ReactomeTeamNew pathway

External references

DataNodes

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NameTypeDatabase referenceComment
2,5-S,S'-dicysteinyldopa MetaboliteCHEBI:84298 (ChEBI)
2-S-Cysteinyl-DOPA MetaboliteCHEBI:84296 (ChEBI)
5-S-Cysteinyldopa MetaboliteCHEBI:81392 (ChEBI)
7-(2-amino-2-carboxyethyl)-5-hydroxy-2H-1,4-benzothiazine-3-carboxylic acid MetaboliteCHEBI:84301 (ChEBI)
7-(2-amino-2-carboxyethyl)-5-hydroxy-3,4-dihydro-2H-1,4-benzothiazin-3-one MetaboliteCHEBI:84344 (ChEBI)
BT, BTCA, BZ, ODHBTComplexR-ALL-5662955 (Reactome)
Benzothiazine MetaboliteCHEBI:46899 (ChEBI)
CO2MetaboliteCHEBI:16526 (ChEBI)
Cu2+ MetaboliteCHEBI:29036 (ChEBI)
Cysteinyldopa isomersComplexR-ALL-5662956 (Reactome)
DCT ProteinP40126 (Uniprot-TrEMBL)
DCT:2xZn2+ComplexR-HSA-5662858 (Reactome)
DHI MetaboliteCHEBI:27404 (ChEBI)
DHI, DHICAComplexR-ALL-5662708 (Reactome)
DHICA MetaboliteCHEBI:2003 (ChEBI)
DHICAMetaboliteCHEBI:2003 (ChEBI)
DHIMetaboliteCHEBI:27404 (ChEBI)
DopachromeMetaboliteCHEBI:49108 (ChEBI)
EumelaninR-HSA-5662678 (Reactome)
H+MetaboliteCHEBI:15378 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
IQCAMetaboliteCHEBI:81394 (ChEBI)
L-CysMetaboliteCHEBI:35235 (ChEBI)
L-DopaMetaboliteCHEBI:15765 (ChEBI)
L-DopaquinoneMetaboliteCHEBI:16852 (ChEBI)
L-TyrMetaboliteCHEBI:58315 (ChEBI)
LeucodopachromeMetaboliteCHEBI:60872 (ChEBI)
O2MetaboliteCHEBI:15379 (ChEBI)
OCA2ProteinQ04671 (Uniprot-TrEMBL)
SLC45A2ProteinQ9UMX9 (Uniprot-TrEMBL)
TYR ProteinP14679 (Uniprot-TrEMBL)
TYR:2xCu2+ComplexR-HSA-5662696 (Reactome)
TYRP1ProteinP17643 (Uniprot-TrEMBL)
Zn2+ MetaboliteCHEBI:29105 (ChEBI)
benzothiazole MetaboliteCHEBI:84343 (ChEBI)
hydroxylMetaboliteCHEBI:29191 (ChEBI)
pheomelaninR-HSA-5665848 (Reactome)

Annotated Interactions

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SourceTargetTypeDatabase referenceComment
BT, BTCA, BZ, ODHBTArrowR-HSA-5662904 (Reactome)
BT, BTCA, BZ, ODHBTR-HSA-5662891 (Reactome)
CO2ArrowR-HSA-5662706 (Reactome)
Cysteinyldopa isomersArrowR-HSA-5662908 (Reactome)
Cysteinyldopa isomersR-HSA-5662904 (Reactome)
DCT:2xZn2+mim-catalysisR-HSA-5662660 (Reactome)
DHI, DHICAR-HSA-5663050 (Reactome)
DHIArrowR-HSA-5662706 (Reactome)
DHICAArrowR-HSA-5662660 (Reactome)
DHICAR-HSA-8878581 (Reactome)
DopachromeArrowR-HSA-5672019 (Reactome)
DopachromeR-HSA-5662660 (Reactome)
DopachromeR-HSA-5662706 (Reactome)
EumelaninArrowR-HSA-5663050 (Reactome)
H+ArrowR-HSA-5662662 (Reactome)
H2OArrowR-HSA-5662692 (Reactome)
H2OArrowR-HSA-8878581 (Reactome)
IQCAArrowR-HSA-8878581 (Reactome)
L-CysR-HSA-5662908 (Reactome)
L-DopaArrowR-HSA-5662904 (Reactome)
L-DopaArrowR-HSA-5663050 (Reactome)
L-DopaArrowR-HSA-5672019 (Reactome)
L-DopaR-HSA-5662692 (Reactome)
L-DopaquinoneArrowR-HSA-5662662 (Reactome)
L-DopaquinoneArrowR-HSA-5662692 (Reactome)
L-DopaquinoneR-HSA-5662669 (Reactome)
L-DopaquinoneR-HSA-5662904 (Reactome)
L-DopaquinoneR-HSA-5662908 (Reactome)
L-DopaquinoneR-HSA-5663050 (Reactome)
L-DopaquinoneR-HSA-5672019 (Reactome)
L-TyrR-HSA-5662662 (Reactome)
LeucodopachromeArrowR-HSA-5662669 (Reactome)
LeucodopachromeR-HSA-5672019 (Reactome)
O2R-HSA-5662692 (Reactome)
O2R-HSA-8878581 (Reactome)
OCA2ArrowR-HSA-5662662 (Reactome)
R-HSA-5662660 (Reactome) Dopachrome is converted to DHICA by DCT (Dopachrome tautomerase, Tyrosinase-related protein 2) (Tsukamoto et al. 1992, Kroumpouzos et al. 1994, Bouchard et al. 1994).
R-HSA-5662662 (Reactome) Melanogenesis is initiated with the first step of tyrosine oxidation to dopaquinone, catalyzed by tyrosinase (Mason 1948, Hearing et al. 1980). This first step is the rate-limiting step in melanin synthesis; the remainder of the reaction sequence can proceed spontaneously at a physiological pH value (Halaban et al. 2002, Land et al. 2003).

The melanocyte-specific transporter protein (OCA2, aka P protein, pink-eyed dilution protein homolog) is postulated to play a role in the processing and intracellular trafficking of tyrosinase (TYR) in the melanosome (Potterf et al. 1998, Toyofuku et al. 2002). It is a 110-kDa integral melanosomal protein with 12 predicted transmembrane domains, suggesting a transport function but its exact physiological role is still unknown. In humans, mutations in the OCA2 gene result in oculocutaneous albinism type 2, a disorder of pigmentation characterised by reduced biosynthesis of melanin in the skin, hair and eyes. This disorder is analogous to the pink-eyed dilution phenotype seen in mice with defective Oca2 (Toyofuku et al. 2002). A single SNP in the OCA2 gene is the major determinant of brown and/or blue eye colour (Sturm 2009).

The membrane-associated transporter protein SLC45A2 (melanoma antigen AIM1, MATP) shows sequence and structural similarity to sucrose transport proteins yet its actual physiological substrate and role is still unclear. Mutations in SLC45A2 cause misrouting of tyrosinase similar to the cellular phenotype of OCA2 and cause oculocutaneous albinism type 4 (OCA4) (Cullinane et al. 2011).
R-HSA-5662669 (Reactome) Dopaquinone is highly reactive and in the absence of sulfhydryl compounds it undergoes the intramolecular addition of the amino group to produce an intermediate, leucodopachrome (also termed cyclodopa). A redox exchange between cyclodopa and dopaquinone then gives rise to dopachrome, an orange-red intermediate (Raper 1927, Mason et al. 1948) and dopa. This latter reaction is considered the source of dopa formed during melanogenesis (Ito & Wakamatsu 2008).
R-HSA-5662692 (Reactome) Dopa is a substrate of tyrosinase, which can oxidize it to dopaquinone (Young et al. 1974).
R-HSA-5662706 (Reactome) Dopachrome spontaneously tautomerizes into 5,6-dihydroxyindole (DHI) via decarboxylation at physiological pH (Mason et al. 1948, Wakamatsu & Ito 1988, Kishida et al. 2015). This is usually a minor process of melanin synthesis in vivo. However, in human hair follicular melanocytes, it predominates (Commo et al. 2012).
R-HSA-5662891 (Reactome) The last stage of pheomelanogenesis is the oxidative polymerization of BT, BTCA, and the products of secondary modifications of the benzothiazine moieties of these to form pheomelanin. Several dimeric and trimeric intermediates have been identified (Napolitano et al. 2001) but it is unclear whether these are major components of natural pheomelanin pigments. Most studies have used powerful chemical oxidants (Di Donato et al. 2002, Napolitano et al. 2008). which may lead to a pheomelanogenesis process that differs from the in vivo process (Wakamatsu et al. 2008).
R-HSA-5662904 (Reactome) Following the formation of cysteinyldopa (CD) isomers, pheomelanogenesis continues with the redox exchange of CD isomers with dopaquinone (DQ), generating cysteinyldopaquinone (CDQ). Once formed, CDQ rapidly cyclizes via attack of the cysteinyl side-chain amino group on the carbonyl group to produce a cyclic ortho-quinonimine intermediate (QI) (Napolitano et al. 1994, Land & Riley 2000). Redox exchange between CD and QI leads to the production of a reduced form of QI, 3,4-dihydro-1,4-benzothiazine-3-carboxylic acid (DHBTCA) and CDQ (Napolitano et al. 2000, Wakamatsu et al. 2009). QI rapidly undergoes rearrangement, with or without decarboxylation, leading to 2H-1,4-benzothiazine (BT) and its 3-carboxy derivative, 2H-1,4-benzothiazine-3-carboxylic acid (BTCA) (Napolitano et al. 1994, 2008). The ratio of BT to BTCA depends on many factors including the pH of the medium and the presence or absence of metal ions (Di Donato et al. 2002, Napolitano et al. 2000). BT and BTCA are unstable, decaying in seconds. Modifications of the benzothiazine moiety of BT and BTCA lead to the formation of 3-oxo-3,4-dihydro-1,4-benzothiazine (ODHBT) and benzothiazole (BZ) (Napolitano et al. 1999, 2008).

The reactions beyond BT and BTCA which ultimately lead to the production of pheomelanin appear to be very complex (Di Donato & Napolitano 2003). Zn2+ promotes retention of the carboxyl group in BTCA while Fe3+ accelerates the ring contraction of BT to BZ (Di Donato et al. 2002). Production of ODHBT is increased by the presence of hydrogen peroxide (Di Donato et al. 2002).
R-HSA-5662908 (Reactome) In the presence of sulfhydryl compounds such as cysteine, dopaquinone reacts to produce several cysteinyldopa (CD) isomers, 5-S-cysteinyldopa (5SCD) and 2-S-cysteinyldopa (2SCD) in 74% and 14% yields, respectively (Ito & Prota 1977, Thompson et al. 1985). 2,5-S,S'-dicysteinyldopa (DiCD) is produced in a 5% yield. Further oxidation of the thiol adducts leads to the formation of pheomelanin via benzothiazine intermediates.
R-HSA-5663050 (Reactome) Eumelanin is a stacked, aggregated oligomer, or heterogeneous polymer consisting of units representing different oxidative states of 5,6-dihydroxyindole (DHI) and 5,6-dihydroxyindole-2-carboxylic acid (DHICA), plus pyrrole units derived from their peroxidative cleavage (Meredith & Sarna 2006, Ito & Wakamatsu 2008). Eumelanin was thought to consist mostly of DHI but this was reconsidered when chemical degradation revealed that natural eumelanins include DHI and DHICA units in a nearly equal ratio (Ito 1986, d'Ischia et al. 2013). DHICA is produced by tautomerization of dopachrome.The oxidative polymerization of DHI can be catalyzed by Tyrosinase (TYR) (Tripathi et al. 1992) but may also be effectively catalysed by redox exchange with dopaquinone (Edge et al. 2006). Redox is likely to be less efficient for DHICA. In mice, the tyrosinase-related protein Tyrp1 can oxidize DHICA (Kobayashi et al. 1994) but human TYRP1 is unable to catalyze the same reaction (Boissy et al. 1998). Instead, human TYR oxidizes DHICA, DHI, tyrosine and dopa.
R-HSA-5672019 (Reactome) A redox exchange between leucodopachrome (cyclodopa) and dopaquinone gives rise to dopachrome, an orange-red intermediate (Raper 1927, Mason et al. 1948) and dopa. This reaction is considered the source of dopa formed during melanogenesis (Ito & Wakamatsu 2008).
R-HSA-8878581 (Reactome) 5,6-dihydroxyindole-2-carboxylic acid oxidase (TYRP1, aka gp75, CAS2, TRP-1) is an abundant protein in the melanosome membrane which, amongst other functions, can oxidise 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into the corresponding 5,6-indolequinone-2-carboxylic acid (IQCA), thus promoting the incorporation of DHICA units into eumelanin (Olivares et al. 2001). Oculocutaneous albinism (OCA) is an autosomal recessive disorder caused by either complete lack of or a reduction of melanin biosynthesis in melanocytes. Mutations in TYRP1 cause OCA3, aka Rufous oculocutaneous albinism. Tyrosinase activity is normal and patients have only a moderate reduction of melanin. Darker-skinned sufferers have bright copper-red colouration of the skin and hair (Kamaraj & Purohit 2014, Rooryck et al. 2006).
SLC45A2ArrowR-HSA-5662662 (Reactome)
TYR:2xCu2+mim-catalysisR-HSA-5662662 (Reactome)
TYR:2xCu2+mim-catalysisR-HSA-5662692 (Reactome)
TYR:2xCu2+mim-catalysisR-HSA-5663050 (Reactome)
TYRP1mim-catalysisR-HSA-8878581 (Reactome)
hydroxylR-HSA-5662662 (Reactome)
pheomelaninArrowR-HSA-5662891 (Reactome)
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