Nicotinic Acid Hydroxamate Downregulated the Melanin Synthesis and Tyrosinase Activity through Activating the MEK/ERK and AKT/GSK3β Signaling Pathways

2012 ◽  
Vol 60 (19) ◽  
pp. 4859-4864 ◽  
Author(s):  
Yin-Shiou Lin ◽  
Mao-Te Chuang ◽  
Chao-Hsiang Chen ◽  
Mei-Yin Chien ◽  
Wen-Chi Hou
Keyword(s):  
Nicotinic Acid ◽  
Signaling Pathways ◽  
Tyrosinase Activity ◽  
Melanin Synthesis

scholarly journals Liquiritin and Liquiritigenin Induce Melanogenesis via Enhancement of p38 and PKA Signaling Pathways

Medicines ◽  
2019 ◽  
Vol 6 (2) ◽  
pp. 68 ◽  
Author(s):  
Takuhiro Uto ◽  
Tomoe Ohta ◽  
Akihisa Yamashita ◽  
Shunsuke Fujii ◽  
Yukihiro Shoyama
Keyword(s):  
Signaling Pathways ◽  
Mek Inhibitor ◽  
Tyrosinase Activity ◽  
Licorice Root ◽  
Melanin Synthesis ◽  
Creb Phosphorylation ◽  
Pi3k Inhibitor Ly294002 ◽  
P38 Inhibitor ◽  
Protein Levels ◽  
Mitf Expression

Background: Liquiritin (LQ) and its aglycone, liquiritigenin (LQG), are major flavonoids in licorice root (Glycyrrhiza spp.). Our preliminary screening identified LQ and LQG, which promote melanin synthesis in the melanoma cells. In this study, we investigated the molecular mechanism of melanin synthesis activated by LQ and LQG. Methods: Murine (B16-F1) and human (HMVII) melanoma cell lines were treated with LQ or LQG. After incubation, melanin contents, intracellular tyrosinase activity, and cell viability were evaluated. Protein levels were determined using Western blotting. Results: LQ and LQG activated melanin synthesis and intracellular tyrosinase activity. The induction of melanin and intracellular tyrosinase activity by LQG was higher than that by LQ. LQ and LQG induced the expression of tyrosinase, tyrosinase-related protein (TRP)-1, and TRP-2. LQ and LQG also enhanced microphthalmia-associated transcription factor (MITF) expression, and cyclic AMP-responsive element-binding protein (CREB) phosphorylation. The phosphorylation of p38 and extracellular signal-regulated kinase (ERK), but not Akt, was significantly increased by LQ or LQG. Furthermore, LQ- or LQG-mediated melanin synthesis was partially blocked by p38 inhibitor (SB203580) and protein kinase A (PKA) inhibitor (H-89); however, ERK kinase (MEK) inhibitor (U0126) and phosphatidylinositol-3-kinase (PI3K) inhibitor (LY294002) had no effect. Conclusions: The results suggest that LQ and LQG enhance melanin synthesis by upregulating the expression of melanogenic enzymes, which were activated by p38 and PKA signaling pathways, leading to MITF expression and CREB phosphorylation.

Insight into Mechanistic Action of Thymoquinone Induced Melanogenesis in Cultured Melanocytes

2019 ◽  
Vol 26 (12) ◽  
pp. 910-918
Author(s):  
Kamal U. Zaidi ◽  
Firoz N. Khan ◽  
Sharique A. Ali ◽  
Kausar P. Khan
Keyword(s):  
Western Blot ◽  
Signaling Pathways ◽  
Cell Line ◽  
Melanoma Cell ◽  
Melanoma Cell Line ◽  
Protein Kinase Inhibitors ◽  
Tyrosinase Activity ◽  
Dependent Manner ◽  
B16f10 Melanoma ◽  
B16f10 Melanoma Cell

Background: Melanin plays a crucial role in camouflage, social communication and protection against harmful ultraviolet radiations. Melanin is synthesized by melanocytes through melanogenesis and several intrinsic and extrinsic factors are involved during the process. Any change occuring in the normal melanogenesis process can cause severe pigmentation problems of hypopigmentation or hyperpigmentation. Objective: The present study is based on the evaluation of the effect of thymoquinone on melanogenesis and their possible mechanism of action using the B16F10 melanoma cell line for the production via blocking signaling pathways. Methods: Phase contrast microscopy, cell viability, tyrosinase activity, melanin content and western blot analysis were used in the present study. Results: In the present investigation, cultured melanocytes exhibit that the stimulation of melanin synthesis when treated with thymoquinone. Tyrosinase activity and melanin production in B16F10 melanoma cell line was increased in doze-dependent manner. In western blot, we investigated the involvement of the cAMP/PKA pathway in thymoquinone induced melanogenesis. It was observed protein kinase inhibitors PKA, PKC, PKB and MEK1 decreased the stimulatory effects of thymoquinone from 11.45- fold value to 8.312, 6.631, 4.51, and 7.211-fold value, respectively. However, the results also prove that thymoquinone may partially induce tyrosinase expression via PKA, PKB, PKC and MEK1 signaling pathways. Conclusion: The present finding proposed that thymoquinone is a protective challenger for melanogenesis and it might be useful for the treatment of hypopigmentary disorders.

scholarly journals Inhibitory Effects of Cycloheterophyllin on Melanin Synthesis

Molecules ◽  
2021 ◽  
Vol 26 (9) ◽  
pp. 2526
Author(s):  
Joong-Hyun Shim
Keyword(s):  
Functional Materials ◽  
Tyrosinase Activity ◽  
Melanin Synthesis ◽  
Activity Assay ◽  
Inhibitory Effects ◽  
Melanin Production ◽  
Messenger Ribonucleic Acid ◽  
B16f10 Cells ◽  
Cell Line Cell ◽  
Tyrosinase Related Protein

This study was performed to clarify the inhibitory effects of cycloheterophyllin on melanin synthesis. In order to elucidate the inhibitory effects of cycloheterophyllin on the B16F10 cell line, cell viability, messenger ribonucleic acid (mRNA) expressions, tyrosinase activity assay, and melanin production assay were measured. The effects of cycloheterophyllin on tyrosinase-related protein 1 (TYRP1)/TYRP2/tyrosinase (TYR)/microphthalmia-associated transcription factor (MITF) mRNA expressions and melanin content were determined. Quantitative real-time RT-PCR showed that cycloheterophyllin decreased the mRNA expression level of TYRP1/TYRP2/TYR/MITF genes and melanin production contents than α-MSH-treated B16F10 cells. The tyrosinase activity assay revealed that cycloheterophyllin decreased the melanin production in the B16F10 cells. These data show that cycloheterophyllin increases the whitening effects in the B16F10 cells; thus, cycloheterophyllin is a potent ingredient for skin whitening. Thus, further research on the mechanism of action of cycloheterophyllin for the development of functional materials should be investigated.

scholarly journals The Organogermanium Compound THGP Suppresses Melanin Synthesis via Complex Formation with L-DOPA on Mushroom Tyrosinase and in B16 4A5 Melanoma Cells

2019 ◽  
Vol 20 (19) ◽  
pp. 4785
Author(s):  
Junya Azumi ◽  
Tomoya Takeda ◽  
Yasuhiro Shimada ◽  
Hisashi Aso ◽  
Takashi Nakamura
Keyword(s):  
Gene Expression ◽  
Kojic Acid ◽  
Biological Activities ◽  
Melanoma Cells ◽  
Tyrosinase Activity ◽  
Melanin Synthesis ◽  
Mushroom Tyrosinase ◽  
Melanin Production ◽  
Organogermanium Compound ◽  
Or Gene

The organogermanium compound 3-(trihydroxygermyl)propanoic acid (THGP) has various biological activities. We previously reported that THGP forms a complex with cis-diol structures. L-3,4-Dihydroxyphenylalanine (L-DOPA), a precursor of melanin, contains a cis-diol structure in its catechol skeleton, and excessive melanin production causes skin darkening and staining. Thus, the cosmetic field is investigating substances that suppress melanin production. In this study, we investigated whether THGP inhibits melanin synthesis via the formation of a complex with L-DOPA using mushroom tyrosinase and B16 4A5 melanoma cells. The ability of THGP to interact with L-DOPA was analyzed by 1H-NMR, and the influence of THGP and/or kojic acid on melanin synthesis was investigated. We also examined the effect of THGP on cytotoxicity, tyrosinase activity, and gene expression and found that THGP interacted with L-DOPA, a precursor of melanin with a cis-diol structure. The results also showed that THGP inhibited melanin synthesis, exerted a synergistic effect with kojic acid, and did not affect tyrosinase activity or gene expression. These results suggest that THGP is a useful substrate that functions as an inhibitor of melanogenesis and that its effect is enhanced by combination with kojic acid.

THE MELANOGENIC RESPONSE TO TESTOSTERONE IN SCROTAL EPIDERMIS: EFFECTS ON TYROSINASE ACTIVITY AND PROTEIN SYNTHESIS

1976 ◽  
Vol 81 (2) ◽  
pp. 435-448 ◽  
Author(s):  
Michael J. Wilson ◽  
Eugene Spaziani
Keyword(s):  
Protein Synthesis ◽  
Specific Protein ◽  
Tyrosinase Activity ◽  
Melanin Synthesis ◽  
Testosterone Treatment ◽  
Pre Treatment ◽  
Inhibitor Of Protein Synthesis ◽  
Rate Limiting

ABSTRACT Pigmentation of the scrotum of the black-pelted rat, as expressed through melanocyte melanogenic activity, is controlled by androgens. Castration decreased in vitro incorporation of [14C] tyrosine into melanin. Testosterone pre-treatment for 4 days increased melanin radioactivity over castrate controls; the increment in vitro was prevented by an inhibitor of protein synthesis (cycloheximide) added to the incubation. However, cycloheximide only partially blocked melanin synthesis when added to tissue from animals hormone treated for 6 days in vivo, and was ineffective in tissue from intacts. Bulk protein synthesis in vitro (incorporation of [14C] tyrosine or -leucine) was not affected by castration or testosterone treatment but was uniformly inhibited by cycloheximide. The data suggest that new synthesis of specific protein in vitro was necessary for initial hormone-stimulation of melanogenesis, but with longer exposure to hormone sufficient protein was pre-synthetized in vivo to permit melanogenesis during incubation with the inhibitor. Radioautographs of epidermis incubated with [14C] tyrosine showed grains concentrated over macromolecular aggregates in melanocytes, a pattern not altered by cycloheximide. Though available for incorporation into general tissue protein. [14C] tyrosine was apparently incorporated preferentially into melanin by melanocytes. DOPA (3,4-dihydroxyphenylalanine) added to incubations in cofactor amounts did not affect decreased melanin synthesis after castration and appears, therefore, not to be rate limiting in that decrease. Tissue uptake of free [14C] tyrosine or — leucine during incubation was lower than normal in castrate epidermis; uptake was elevated by testosterone treatment. Concentrations appeared sufficient in all preparations to suggest that availability is not rate limiting for synthesis of melanin or protein; however, a possible influence on amino acid permeability for melanocytes remains undetermined. Tyrosinase activity was present in both particulate and cytosol fractions of epidermis but decreased significantly after castration only in the cytosol. Testosterone increased particulate activity after 4 days and soluble activity after 9 days of treatment. These and findings above are consistent with a model that tyrosinase is synthesized and incorporated into melanosome structure within 4 days testosterone treatment; with longer treatment synthesis may then exceed that required for melanosome assembly and tyrosinase appears in the soluble milieu.

Occurrence of high tyrosinase activity in the non-Peltigeralean lichenDermatocarponminiatum(L.) W. Mann

2012 ◽  
Vol 44 (6) ◽  
pp. 827-832 ◽  
Author(s):  
Richard P. BECKETT ◽  
Farida V. MINIBAYEVA ◽  
Christiane LIERS
Keyword(s):  
Cell Walls ◽  
Redox Cycling ◽  
Tyrosinase Activity ◽  
Melanin Synthesis ◽  
Multicopper Oxidases ◽  
Apparent Absence ◽  
Ph Optimum ◽  
Cellular Location

AbstractIn our earlier work, we demonstrated the presence of the multicopper oxidases tyrosinase and laccase in the cell walls of lichens from thePeltigerales, while these enzymes appeared to be absent in lichens from other orders. Likely roles for tyrosinase in lichens include melanin synthesis, the generation of quinones needed for laccase-mediated redox cycling, and the removal of harmful reactive molecules formed by this cycling. Non-Peltigeralean lichens will not need tyrosinase to detoxify laccase-generated radicals. However, many non-Peltigeralean lichens are often heavily melanized. Apparent absence of tyrosinase activity in these species prompted us to suggest that, in these lichens, melanins are probably synthesized by the polyketide pathway, which does not involve tyrosinase. Here, we surveyed intracellular tyrosinase activity in thallus homogenates from a range of lichens. Results showed that Peltigeralean species generally have much higher activities than species from other orders. However, the non-Peltigeralean lichenDermatocarpon miniatumdisplays significant tyrosinase activity. InD. miniatum, tyrosinase differs from the corresponding enzyme from Peltigeralean lichens with respect to cellular location, substratum specificity, stability and pH optimum. Furthermore, unlike Peltigeralean lichens, inD. miniatumtyrosinase activity increased strongly following the rehydration of dry thalli. These differences are possibly a consequence of the role of tyrosinase in melanin synthesis rather than laccase-mediated redox cycling.

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