scholarly journals Melanogenesis Inhibitor(s) fromPhyla nodifloraExtract

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Feng-Lin Yen ◽  
Moo-Chin Wang ◽  
Chan-Jung Liang ◽  
Horng-Huey Ko ◽  
Chiang-Wen Lee
Keyword(s):  
Inflammatory Diseases ◽  
Folk Medicine ◽  
Camp Response Element Binding ◽  
Dependent Manner ◽  
Melanin Content ◽  
Camp Response Element ◽  
Alternative Medicines ◽  
Extracellular Signal ◽  
Mitogen Activated Protein ◽  
Element Binding Protein

Overexpression of tyrosinase can cause excessive production of melanin and lead to hyperpigmentation disorders, including melasma and freckles. Recently, agents obtained from plants are being used as alternative medicines to downregulate tyrosinase synthesis and decrease melanin production.Phyla nodifloraGreene (Verbenaceae) is used as a folk medicine in Taiwanese for treating and preventing inflammatory diseases such as hepatitis and dermatitis. However, the antimelanogenesis activity and molecular biological mechanism underlying the activity of the methanolic extract ofP. nodiflora(PNM) have not been investigated to date. Our results showed that PNM treatment was not cytotoxic and significantly reduced the cellular melanin content and tyrosinase activity in a dose-dependent manner (P<0.05). Further, PNM exhibited a significant antimelanogenesis effect (P<0.05) by reducing the levels of phospho-cAMP response element-binding protein and microphthalmia-associated transcription factor (MITF), inhibiting the synthesis of tyrosinase, tyrosinase-related protein-1 (TRP-1), and TRP-2, and decreasing the cellular melanin content. Moreover, PNM significantly activated the phosphorylation of mitogen-activated protein kinases, including phospho-extracellular signal-regulated kinase, c-Jun N-terminal kinase, and phospho-p38, and inhibited the synthesis of MITF, thus decreasing melanogenesis. These properties suggest that PNM could be used as a clinical and cosmetic skin-whitening agent to cure and/or prevent hyperpigmentation.

scholarly journals Extracts ofArtocarpus communisDecreaseα-Melanocyte Stimulating Hormone-Induced Melanogenesis through Activation of ERK and JNK Signaling Pathways

2014 ◽  
Vol 2014 ◽  
pp. 1-8 ◽  
Author(s):  
Yi-Tzu Fu ◽  
Chiang-Wen Lee ◽  
Horng-Huey Ko ◽  
Feng-Lin Yen
Keyword(s):  
Skin Diseases ◽  
Folk Medicine ◽  
Camp Response Element Binding ◽  
Melanin Content ◽  
Agricultural Plant ◽  
Melanocyte Stimulating Hormone ◽  
B16f10 Cells ◽  
Extracellular Signal ◽  
Element Binding Protein ◽  
Stimulating Hormone

Artocarpus communisis an agricultural plant that is also used in folk medicine to prevent skin diseases, including acne and dermatitis. Extracts ofA. communishave been used to effectively inhibit melanogenesis; however, the antimelanogenesis mechanism of these extracts has not yet been investigated. The present study utilized a cell-free tyrosinase assay as well asα-melanocyte stimulating hormone- (-MSH-) induced tyrosinase assay conducted in B16F10 cells, performed a cytotoxicity assay, and determined cellular melanin content to examine the effects of a methanolic extract ofA. communis(ACM) and various organic partition fractions ofA. communison melanogenesis. In addition, we performed western blot analysis to elucidate the mechanism of their antimelanogenesis effect. Our results indicated that, except for the n-hexane extract, ACM and the various partition extracts at noncytotoxic concentrations effectively decreased melanin content and tyrosinase activity by downregulating microphthalmia-associated transcription factor (MITF) and phosphorylated cAMP response element-binding protein (p-CREB). Moreover, ACM and the partition fractions activated phosphorylation of extracellular signal-regulated kinase (ERK) and c-Jun N-terminal kinase (JNK) to inhibit the synthesis of MITF and finally to decrease melanin production. In conclusion, we suggest that noncytotoxic concentrations of ACM and the various partition fractions may be useful as references for developing skin-lighting agents for use in medicines or cosmetics.

scholarly journals Stimulation of Phosphorylation of ERK and CREB by Phellopterin and Auraptene Isolated from Citrus junos

2014 ◽  
Vol 9 (10) ◽  
pp. 1934578X1400901 ◽  
Author(s):  
Mitsuhiro Nakamura ◽  
Tomoko Suzuki ◽  
Mai Takagi ◽  
Hirotoshi Tamura ◽  
Toshiya Masuda
Keyword(s):  
Camp Response Element Binding ◽  
Long Term Memory ◽  
Camp Response Element ◽  
Extracellular Signal Regulated Kinase ◽  
Cellular Processes ◽  
Extracellular Signal ◽  
Citrus Junos ◽  
Element Binding Protein ◽  
Methyl Ferulate

Bioactive compounds from citrus fruits contribute many benefits to human health. Extracellular signal-regulated kinase (ERK) signaling plays an important role in the regulation of multiple cellular processes. Activation of the ERK-cAMP response element binding protein (CREB) signaling is required for long-term memory formation. In this study, auraptene, phellopterin, thymol, coniferyl alcohol 9-methyl ether and methyl ferulate were isolated from Citrus junos. Among the five compounds isolated, auraptene and phellopterin increased the phosphorylation of ERK and CREB. This study provides, to our knowledge, the first evidence that phellopterin potently stimulates the phosphorylation of ERK and CREB. Phellopterin could be a novel neuroprotective agent.

scholarly journals Protocatechuic Aldehyde Inhibits α-MSH-Induced Melanogenesis in B16F10 Melanoma Cells via PKA/CREB–Associated MITF Downregulation

2021 ◽  
Vol 22 (8) ◽  
pp. 3861
Author(s):  
Seok-Chun Ko ◽  
Seung-Hong Lee
Keyword(s):  
Molecular Mechanisms ◽  
3D Structure ◽  
Camp Response Element Binding ◽  
Melanoma Cells ◽  
Dependent Manner ◽  
Camp Response Element ◽  
B16f10 Cells ◽  
Protocatechuic Aldehyde ◽  
Element Binding Protein ◽  
Dependent Protein

Protocatechuic aldehyde (PA) is a naturally occurring phenolic compound that is a potent inhibitor of mushroom tyrosinase. However, the molecular mechanisms of the anti-melanogenesis activity of PA have not yet been reported. The aim of the current study was to clarify the melanogenesis inhibitory effects of PA and its molecular mechanisms in murine melanoma cells (B16F10). We first predicted the 3D structure of tyrosinase and used a molecular docking algorithm to simulate binding between tyrosinase and PA. These molecular modeling studies calculated a binding energy of −527.42 kcal/mol and indicated that PA interacts with Cu400 and 401, Val283, and His263. Furthermore, PA significantly decreased α-MSH-induced intracellular tyrosinase activity and melanin content in a dose-dependent manner. PA also inhibited key melanogenic proteins such as tyrosinase, tyrosinase-related protein 1 (TRP-1), and TRP-2 in α-MSH-stimulated B16F10 cells. In addition, PA decreased MITF expression levels by inhibiting phosphorylation of cAMP response element-binding protein (CREB) and cAMP-dependent protein kinase A (PKA). These results demonstrate that PA can effectively suppress melanin synthesis in melanoma cells. Taken together, our results show that PA could serve as a potential inhibitor of melanogenesis, and hence could be explored as a possible skin-lightening agent.

Action of rolipram on specific PDE4 cAMP phosphodiesterase isoforms and on the phosphorylation of cAMP-response-element-binding protein (CREB) and p38 mitogen-activated protein (MAP) kinase in U937 monocytic cells

2000 ◽  
Vol 347 (2) ◽  
pp. 571-578 ◽  
Author(s):  
Simon J. MACKENZIE ◽  
Miles D. HOUSLAY
Keyword(s):  
Map Kinase ◽  
Camp Response Element Binding ◽  
U937 Cells ◽  
Camp Response Element ◽  
Monocytic Cells ◽  
Ic50 Value ◽  
Protein Map ◽  
Mitogen Activated Protein ◽  
Element Binding Protein ◽  
Ifn Γ

U937 monocytic cells are shown here to express a range of PDE4, cAMP-specific phosphodiesterase (PDE) isoenzymes: the long isoenzymes, PDE4A4, PDE4D5 and PDE4D3, plus the short isoenzyme, PDE4B2. These isoenzymes provide around 76% of the total cAMP PDE activity of U937 cells. The specific activities of the total PDE4A, PDE4B and PDE4D activities were 0.63±0.09, 8.8±0.2 and 34.4±2.9 pmol/min per mg of protein respectively. The PDE4 selective inhibitor, rolipram, inhibited immunopurified PDE4B and PDE4D activities similarly, with IC50 values of approx. 130 nM and 240 nM respectively. In contrast, rolipram inhibited immunopurified PDE4A activity with a dramatically lower IC50 value of around 3 nM. Rolipram increased phosphorylation of cAMP-response-element-binding protein (CREB) in U937 cells in a dose-dependent fashion, which implied the presence of both high affinity (IC50 value approx. 1 nM) and low affinity (IC50 value approx. 120 nM) components. Rolipram dose-dependently inhibited the interferon-γ (IFN-γ)-stimulated phosphorylation of p38 mitogen-activated protein (MAP) kinase in a simple monotonic fashion with an IC50 value of approx. 290 nM. On this basis, it is suggested that rolipram inhibition of PDE4A4 is involved in regulating CREB phosphorylation but not IFN-γ-stimulated p38 MAP kinase phosphorylation. PDE4A4 was also selectively activated by challenge of U937 cells with either bacterial lipopolysaccharide (LPS) or IFN-γ through a process which was attenuated by both wortmannin and rapamycin. It is proposed that the PDE4A4 isoform is involved in compartmentalized cAMP signalling responses in U937 monocytes.

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