Synthesis of N-hydroxycinnamoyl amide derivatives and evaluation of their anti-oxidative and anti-tyrosinase activities.
Wang D, Zhu J, Xu JR, Ji DD.
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Novel morpholine containing cinnamoyl amides as potent tyrosinase inhibitors.
Ghafari S, Ranjbar S, Larijani B, Amini M, Biglar M, Mahdavi M, Bakhshaei M, Khoshneviszadeh M, Sakhteman A, Khoshneviszadeh M.
Int J Biol Macromol. 2019 May 29;135:978-985. doi: 10.1016/j.ijbiomac.2019.05.201.

Transdermal BQ-788/EA@ZnO quantum dots as targeting and smart tyrosinase inhibitors in melanocytes.
Huang X, Chen C, Zhu X, Zheng X, Li S, Gong X, Xiao Z, Jiang N, Yu C, Yi C.
Mater Sci Eng C Mater Biol Appl. 2019 Sep;102:45-52. doi: 10.1016/j.msec.2019.04.042

Phosphonic and phosphinic acid derivatives as novel tyrosinase inhibitors: Kinetic studies and molecular docking.
Wolińska E, Hałdys K, Góra J, Olszewski TK, Boduszek B, Latajka R.
Chem Biodivers. 2019 May 30. doi: 10.1002/cbdv.201900167 

Optimization of Bacillus licheniformis MAL tyrosinase: in vitro anticancer activity for brown and black eumelanin.
Gamal Shalaby AS, Ragab TIM, Helal MMI, Esawy MA.
Heliyon. 2019 May 8;5(5):e01657. doi: 10.1016/j.heliyon.2019.e01657

A New Tyrosinase Inhibitor from the Red Alga Symphyocladia latiuscula (Harvey) Yamada (Rhodomelaceae).
Paudel P, Wagle A, Seong SH, Park HJ, Jung HA, Choi JS.
Mar Drugs. 2019 May 17;17(5). pii: E295. doi: 10.3390/md17050295.

Tyrosinase-encapsulated liposomes: Toward enzyme-induced in situ sensitization of semiconductor for sensitive photoelectrochemical immunoassay.
Yu SY, Xue TY, Zhu LB, Fan GC, Han DM, Wang C, Zhao WW.
Biosens Bioelectron. 2019 Jul 1;136:128-131. doi: 10.1016/j.bios.2019.04.037.

The TYRP1-mediated protection of human tyrosinase activity does not involve stable interactions of tyrosinase domains.
Dolinska MB, Wingfield PT, Young KL 2nd, Sergeev YV.
Pigment Cell Melanoma Res. 2019 May 11. doi: 10.1111/pcmr.12791

Tyrosinase immunohistochemistry can be employed for the diagnosis of atypical teratoid/rhabdoid tumours of the tyrosinase subgroup (ATRT-TYR).
Hasselblatt M, Thomas C, Nemes K, Monoranu CM, Riemenschneider MJ, Koch A, Sumerauer D, Hauser P, Paulus W, Johann PD, Kool M, Frühwald MC.
Neuropathol Appl Neurobiol. 2019 May 11. doi: 10.1111/nan.12560.

Inhibitory effects of shell of Camellia oleifera Abel extract on mushroom tyrosinase and human skin melanin.
Liu W, Wang M, Xu S, Gao C, Liu J.
J Cosmet Dermatol. 2019 Apr 29. doi: 10.1111/jocd.12921.

Antioxidant, anti-tyrosinase and anti-melanogenic effects of (E)-2,3-diphenylacrylic acid derivatives.
Ullah S, Park Y, Park C, Lee S, Kang D, Yang J, Akter J, Chun P, Moon HR.
Bioorg Med Chem. 2019 Jun 1;27(11):2192-2200. doi: 10.1016/j.bmc.2019.04.020.

Melanin production by tyrosinase activity on a tyrosine-rich peptide fragment and pH-dependent self-assembly of its lipidated analogue.
Hutchinson JA, Hamley IW, Edwards-Gayle CJC, Castelletto V, Piras C, Cramer R, Kowalczyk R, Seitsonen J, Ruokolainen J, Rambo RP.
Org Biomol Chem. 2019 May 8;17(18):4543-4553. doi: 10.1039/c9ob00550a.

Tyrosinase is an enzyme, it affects the rate of melanin formation.

Melanogenesis is a physiological process that results in the synthesis of melanin pigments, which play a crucial protective role against skin photocarcinogenesis. In order to determine the effects of rosmarinic acid on melanogenesis and elucidate the molecular events of melanogenesis induced by rosmarinic acid, several experiments were performed in B16 melanoma cells. In this study, we showed that the melanin content and tyrosinase expression were increased by rosmarinic acid in a concentration-dependent manner. In addition, after the melanin content was increased by rosmarinic acid, it was reduced by H-89 and KT 5720, protein kinase A (PKA) inhibitors, but not by SB203580, a p38(mapk) inhibitor, or Ro-32-0432, a PKC inhibitor, which suggests the involvement of PKA in rosmarinic acid-induced melanogenesis. Consistent with this, rosmarinic acid induced the phosphorylation of CRE-binding protein (CREB), but had no effect on the phosphorylation of p38(mapk) or the inhibition of Akt phosphorylation. Additionally, rosmarinic acid induced the activation of cAMP response element (CRE) without having any effect on cAMP production, which suggests that rosmarinic acid-induced melanogenesis is mediated by PKA, which occurs downstream of cAMP production. This result was further confirmed by the fact that rosmarinic acid-induced phosphorylation of CREB was inhibited by H-89, but not by PD98059, a MEK1 inhibitor, or by LY294002, a phosphatidylinositol-3-kinase (PI3K) inhibitor. Rosmarinic acid-induced expression of tyrosinase protein was attenuated by H-89. Based on these results, we report for the first time that rosmarinic acid induces melanogenesis through PKA activation signaling (1).

On the other hand Tyrosinase inhibitors could represent an efficacious strategy for pharmacological intervention on skin pathologies related to aberrant production of melanin (2).

Tyrosinase studies

References_________________________________________

(1) Rosmarinic acid induces melanogenesis through protein kinase A activation signaling. Lee J., Kim Y. S., Park D. Biochem Pharmacol. 2007 Oct 1;74(7):960-8.

(2) Exploiting the 1-(4-fluorobenzyl)piperazine fragment for the development of novel tyrosinase inhibitors as anti-melanogenic agents: Design, synthesis, structural insights and biological profile.  Ielo L, Deri B, Germanò MP, Vittorio S, Mirabile S, Gitto R, Rapisarda A, Ronsisvalle S, Floris S, Pazy Y, Fais A, Fishman A, De Luca L.  Eur J Med Chem. 2019 Jun 6;178:380-389. doi: 10.1016/j.ejmech.2019.06.019.