E-Mail Alert

Add your e-mail address to receive forthcoming issues of this journal:

Journal Browser

Journal Browser

Special Issue "Inhibitors of Melanogenesis Related Processes: Application to Food and Cosmetic Industry"

Quicklinks

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Bioactives and Nutraceuticals".

Deadline for manuscript submissions: closed (31 March 2010)

Special Issue Editor

Guest Editor
Prof. Dr. Manickam Sugumaran (Website)

Department of Biology, University of Massachusetts Boston, 100 Morrissey Blvd, Boston, MA 02125, USA
Phone: +1 617-287-6598
Fax: +1 617 287 6650
Interests: enzymology; post translational modifications; aromatic metabolism; phenolic biochemistry; reactions of quinonoid compounds; invertebrate immunity; insect cuticular sclerotization; phenoloxidase; quinone isomerases; oxidative browning; melanin biosynthesis; catecholic antibiotics

Special Issue Information

Dear Colleagues,

Melanogenesis occurs ubiquitously in microorganism, plants and all animals. The enzyme tyrosinase also known as phenoloxidase initiates this process by hydroxylating monphenols to o-diphenols and further oxidizing o-diphenols to o-quinones. O-Quinones being unstable, undergo rapid nonenzymatic as well as enzyme catalyzed transformations to eventually produce different kinds of polymeric products. Quinones in general are very reactive and tend to deplete cellular antioxidant pools as well as cause deleterious effects on cellular macromolecules. In plants, such oxidative browning reactions reduce the nutritive values thereby helping the plant to cope up with infections and invasions. Oxidative browning certainly reduces the consume ability and hence their market value. The melanosis observed in crustaceans similarly reduces the market value of sea food drastically. In arthropods and especially insects, melanogenesis is used for wound healing and defense reactions. Mammals use melanin mostly as skin, coat and eye pigments. Therefore, prevention of oxidative browning of plant products as well as sea food, alteration of skin color, and prevention and/or reduction of melanogenesis in animals has great commercial potentials. This special edition will cover a broad range of phenoloxidase/tyrosinase chemistry, biochemistry of inhibitor and ways to develop new and novel natural and synthetic bioactive compounds against melanogenesis and related process.

Prof. Dr. Manickam Sugumaran
Guest Editor

Keywords

  • phenoloxidase inhibitors
  • tyrosinase inhibitors
  • inhibitors of melanogenesis
  • skin color lightening

Related Special Issue

Published Papers (9 papers)

View options order results:
result details:
Displaying articles 1-9
Export citation of selected articles as:

Research

Jump to: Review, Other

Open AccessArticle Evaluation of Depigmenting Activity by 8-Hydroxydaidzein in Mouse B16 Melanoma Cells and Human Volunteers
Int. J. Mol. Sci. 2009, 10(10), 4257-4266; doi:10.3390/ijms10104257
Received: 27 August 2009 / Revised: 22 September 2009 / Accepted: 24 September 2009 / Published: 29 September 2009
Cited by 31 | PDF Full-text (78 KB) | HTML Full-text | XML Full-text
Abstract
In our previous study, 8-hydroxydaidzein (8-OHDe) was demonstrated to be a potent and unique suicide substrate of mushroom tyrosinase. In this study, the compound was evaluated for in vitro cellular tyrosinase and melanogenesis inhibitory activities in mouse B16 melanoma cells and for [...] Read more.
In our previous study, 8-hydroxydaidzein (8-OHDe) was demonstrated to be a potent and unique suicide substrate of mushroom tyrosinase. In this study, the compound was evaluated for in vitro cellular tyrosinase and melanogenesis inhibitory activities in mouse B16 melanoma cells and for in vivo skin-whitening activity in human volunteers. Tyrosinase activity and melanogenesis in the cell culture incubated with 10 µM of 8-OHDe were decreased to 20.1% and 51.8% of control, respectively, while no obvious cytotoxicity was observed in this concentration. In contrast, a standard tyrosinase inhibitor, kojic acid, showed 69.9% and 71.3% of control in cellular tyrosinase and melanogenesis activity, respectively, at a concentration as high as 100 µM. Hence, 8-OHDe exhibited more than an inhibitory effects on melanin production in B16 cells 10-fold stronger than kojic acid. In addition, when a cream containing 4% 8-OHDe was applied to human skin in an in vivo study, significant increases in the dL*-values were observed after three weeks. Moreover, the increase in the dL*-values after 8-week treatment with 4% 8-OHDe (from -0.57 to 1.94) is stronger than those of 2% 8-OHDe treatment (from 0.26 to 0.94) and 2% ascorbic acid-2-glucoside treatment (from 0.07 to 1.54). From the results of the study, it was concluded that 8-OHDe, the potent suicide substrate of mushroom tyrosinase, has depigmenting activities in both mouse melanoma cells and in human volunteers. Thus, the compound has significant potential for use in cosmetics as a skin-whitening ingredient. Full article
Figures

Open AccessArticle Variations in IC50 Values with Purity of Mushroom Tyrosinase
Int. J. Mol. Sci. 2009, 10(9), 3811-3823; doi:10.3390/ijms10093811
Received: 5 August 2009 / Revised: 19 August 2009 / Accepted: 31 August 2009 / Published: 2 September 2009
Cited by 24 | PDF Full-text (155 KB) | HTML Full-text | XML Full-text
Abstract
The effects of various inhibitors on crude, commercial and partially purified commercial mushroom tyrosinase were examined by comparing IC50 values. Kojic acid, salicylhydroxamic acid, tropolone, methimazole, and ammonium tetrathiomolybdate had relatively similar IC50 values for the crude, commercial and partially [...] Read more.
The effects of various inhibitors on crude, commercial and partially purified commercial mushroom tyrosinase were examined by comparing IC50 values. Kojic acid, salicylhydroxamic acid, tropolone, methimazole, and ammonium tetrathiomolybdate had relatively similar IC50 values for the crude, commercial and partially purified enzyme. 4-Hexylresorcinol seemed to have a somewhat higher IC50 value using crude extracts, compared to commercial or purified tyrosinase. Some inhibitors (NaCl, esculetin, biphenol, phloridzin) showed variations in IC50 values between the enzyme samples. In contrast, hydroquinone, lysozyme, Zn2+, and anisaldehyde showed little or no inhibition in concentration ranges reported to be effective inhibitors. Organic solvents (DMSO and ethanol) had IC50 values that were similar for some of the tyrosinase samples. Depending of the source of tyrosinase and choice of inhibitor, variations in IC50 values were observed. Full article

Review

Jump to: Research, Other

Open AccessReview Quasi-Drugs Developed in Japan for the Prevention or Treatment of Hyperpigmentary Disorders
Int. J. Mol. Sci. 2010, 11(6), 2566-2575; doi:10.3390/ijms11062566
Received: 1 May 2010 / Revised: 9 June 2010 / Accepted: 10 June 2010 / Published: 18 June 2010
Cited by 17 | PDF Full-text (105 KB) | HTML Full-text | XML Full-text
Abstract
Excess production of melanin or its abnormal distribution, or both, can cause irregular hyperpigmentation of the skin, leading to melasma and age spots. To date, various quasi-drugs that prevent or improve hyperpigmentary disorders have been developed and officially approved by the Ministry [...] Read more.
Excess production of melanin or its abnormal distribution, or both, can cause irregular hyperpigmentation of the skin, leading to melasma and age spots. To date, various quasi-drugs that prevent or improve hyperpigmentary disorders have been developed and officially approved by the Ministry of Health, Labor and Welfare of Japan. Many of these inhibit the activity of tyrosinase, an enzyme required for melanin synthesis, for example, by competitive or non-competitive inhibition of its catalytic activity, by inhibiting its maturation, or by accelerating its degradation. In this review, we categorize the quasi-drugs developed in Japan to prevent or treat hyperpigmentary disorders, or both, and discuss perspectives for future development. Full article
Open AccessReview Tyrosinase-Expressing Neuronal Cell Line as in Vitro Model of Parkinson’s Disease
Int. J. Mol. Sci. 2010, 11(3), 1082-1089; doi:10.3390/ijms11031082
Received: 18 January 2010 / Accepted: 3 March 2010 / Published: 12 March 2010
Cited by 20 | PDF Full-text (468 KB) | HTML Full-text | XML Full-text
Abstract
Oxidized metabolites of dopamine known as dopamine quinone derivatives are thought to play a pivotal role in the degeneration of nigrostriatal dopaminergic neurons in Parkinson’s disease. Although such quinone derivatives are usually produced via the autoxidation of catecholamines, tyrosinase, which is a [...] Read more.
Oxidized metabolites of dopamine known as dopamine quinone derivatives are thought to play a pivotal role in the degeneration of nigrostriatal dopaminergic neurons in Parkinson’s disease. Although such quinone derivatives are usually produced via the autoxidation of catecholamines, tyrosinase, which is a key enzyme in melanin biosynthesis via the production of DOPA and subsequent molecules, can potentially accelerate the induction of catecholamine quinone derivatives by its oxidase activity. We have developed neuronal cell lines in which the expression of human tyrosinase was inducible. Overexpression of tyrosinase resulted in increased intracellular dopamine content in association with the formation of melanin pigments in neuronal somata, which eventually causes apoptotic cell death. This cellular model will provide a useful tool for detailed analyses of the neurotoxicity of oxidized catechol metabolites. Full article
Open AccessReview The Hunt for Natural Skin Whitening Agents
Int. J. Mol. Sci. 2009, 10(12), 5326-5349; doi:10.3390/ijms10125326
Received: 5 November 2009 / Revised: 24 November 2009 / Accepted: 9 December 2009 / Published: 10 December 2009
Cited by 50 | PDF Full-text (166 KB) | HTML Full-text | XML Full-text
Abstract
Skin whitening products are commercially available for cosmetic purposes in order to obtain a lighter skin appearance. They are also utilized for clinical treatment of pigmentary disorders such as melasma or postinflammatory hyperpigmentation. Whitening agents act at various levels of melanin production [...] Read more.
Skin whitening products are commercially available for cosmetic purposes in order to obtain a lighter skin appearance. They are also utilized for clinical treatment of pigmentary disorders such as melasma or postinflammatory hyperpigmentation. Whitening agents act at various levels of melanin production in the skin. Many of them are known as competitive inhibitors of tyrosinase, the key enzyme in melanogenesis. Others inhibit the maturation of this enzyme or the transport of pigment granules (melanosomes) from melanocytes to surrounding keratinocytes. In this review we present an overview of (natural) whitening products that may decrease skin pigmentation by their interference with the pigmentary processes. Full article
Open AccessReview Role of the Ubiquitin Proteasome System in Regulating Skin Pigmentation
Int. J. Mol. Sci. 2009, 10(10), 4428-4434; doi:10.3390/ijms10104428
Received: 3 September 2009 / Revised: 29 September 2009 / Accepted: 9 October 2009 / Published: 15 October 2009
Cited by 15 | PDF Full-text (120 KB) | HTML Full-text | XML Full-text
Abstract
Pigmentation of the skin, hair and eyes is regulated by tyrosinase, the critical rate-limiting enzyme in melanin synthesis by melanocytes. Tyrosinase is degraded endogenously, at least in part, by the ubiquitin proteasome system (UPS). Several types of inherited hypopigmentary diseases, such as [...] Read more.
Pigmentation of the skin, hair and eyes is regulated by tyrosinase, the critical rate-limiting enzyme in melanin synthesis by melanocytes. Tyrosinase is degraded endogenously, at least in part, by the ubiquitin proteasome system (UPS). Several types of inherited hypopigmentary diseases, such as oculocutaneous albinism and Hermansky-Pudlak syndrome, involve the aberrant processing and/or trafficking of tyrosinase and its subsequent degradation which can occur due to the quality-control machinery. Studies on carbohydrate modifications have revealed that tyrosinase in the endoplasmic reticulum (ER) is proteolyzed via ER-associated protein degradation and that tyrosinase degradation can also occur following its complete maturation in the Golgi. Among intrinsic factors that regulate the UPS, fatty acids have been shown to modulate tyrosinase degradation in contrasting manners through increased or decreased amounts of ubiquitinated tyrosinase that leads to its accelerated or decelerated degradation by proteasomes. Full article
Open AccessReview Mechanisms Regulating Skin Pigmentation: The Rise and Fall of Complexion Coloration
Int. J. Mol. Sci. 2009, 10(9), 4066-4087; doi:10.3390/ijms10094066
Received: 21 August 2009 / Revised: 9 September 2009 / Accepted: 11 September 2009 / Published: 15 September 2009
Cited by 53 | PDF Full-text (232 KB) | HTML Full-text | XML Full-text
Abstract
Skin pigmentary abnormalities are seen as aesthetically unfavorable and have led to the development of cosmetic and therapeutic treatment modalities of varying efficacy. Hence, several putative depigmenting agents aimed at modulating skin pigmentation are currently being researched or sold in commercially available [...] Read more.
Skin pigmentary abnormalities are seen as aesthetically unfavorable and have led to the development of cosmetic and therapeutic treatment modalities of varying efficacy. Hence, several putative depigmenting agents aimed at modulating skin pigmentation are currently being researched or sold in commercially available products. In this review we will discuss the regulation of processes that control skin complexion coloration. This includes direct inhibition of tyrosinase and related melanogenic enzymes, regulation of melanocyte homeostasis, alteration of constitutive and facultative pigmentation and down-regulation of melanosome transfer to the keratinocytes. These various processes, in the complex mechanism of skin pigmentation, can be regulated individually or concomitantly to alter complexion coloration and thus ameliorate skin complexion diseases. Full article
Open AccessReview An Updated Review of Tyrosinase Inhibitors
Int. J. Mol. Sci. 2009, 10(6), 2440-2475; doi:10.3390/ijms10062440
Received: 21 April 2009 / Revised: 8 May 2009 / Accepted: 21 May 2009 / Published: 26 May 2009
Cited by 330 | PDF Full-text (383 KB) | HTML Full-text | XML Full-text
Abstract
Tyrosinase is a multifunctional, glycosylated, and copper-containing oxidase, which catalyzes the first two steps in mammalian melanogenesis and is responsible for enzymatic browning reactions in damaged fruits during post-harvest handling and processing. Neither hyperpigmentation in human skin nor enzymatic browning in fruits [...] Read more.
Tyrosinase is a multifunctional, glycosylated, and copper-containing oxidase, which catalyzes the first two steps in mammalian melanogenesis and is responsible for enzymatic browning reactions in damaged fruits during post-harvest handling and processing. Neither hyperpigmentation in human skin nor enzymatic browning in fruits are desirable. These phenomena have encouraged researchers to seek new potent tyrosinase inhibitors for use in foods and cosmetics. This article surveys tyrosinase inhibitors newly discovered from natural and synthetic sources. The inhibitory strength is compared with that of a standard inhibitor, kojic acid, and their inhibitory mechanisms are discussed. Full article

Other

Jump to: Research, Review

Open AccessAddendum Addendum: Quasi-Drugs Developed in Japan for the Prevention or Treatment of Hyperpigmentary Disorders. Int. J. Mol. Sci. 2010, 11, 2566–2575
Int. J. Mol. Sci. 2010, 11(7), 2699-2700; doi:10.3390/ijms11072699
Received: 5 July 2010 / Accepted: 8 July 2010 / Published: 12 July 2010
PDF Full-text (23 KB) | HTML Full-text | XML Full-text
Abstract One additional skin lightening or whitening quasi-drug (QD) has been developed and officially approved by the Ministry of Health, Labor and Welfare of Japan. Full article

Journal Contact

MDPI AG
IJMS Editorial Office
St. Alban-Anlage 66, 4052 Basel, Switzerland
ijms@mdpi.com
Tel. +41 61 683 77 34
Fax: +41 61 302 89 18
Editorial Board
Contact Details Submit to IJMS
Back to Top