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1.
Pharmazie ; 75(11): 565-570, 2020 11 01.
Article in English | MEDLINE | ID: mdl-33239130

ABSTRACT

Torreya nucifera is an evergreen tree in the family Taxaceae, the seeds, leaves, and stems of which have long been used as edible products and herbal medicines in Korea. Previous studies of biological activity have shown that T. nucifera has antioxidant and anti-inflammatory effects. However, the effect of T. nucifera leaves on melanogenesis are yet to be studied. In this investigation, we used B16F10 melanoma cells to test the efficacy of T. nucifera leaf hot water extract (TLWE). α-melanocyte stimulating hormone (α-MSH) stimulated B16F10 melanoma cells were treated with various concentrations of TLWE (50, 100, and 200 µg/mL). The results showed that TLWE reduced the melanin content and cellular tyrosinase activity in a concentration-dependent manner. It also inhibited the phosphorylation of p38 mitogen-activated protein kinase (p38) and c-Jun N-terminal kinase (JNK) in the mitogen-activated protein kinase (MAPK) signaling pathway. The compounds catechin and ρ-coumaric acid, which are known to have a whitening effect on skin, were detected by HPLC analysis. These results suggest that TLWE has an anti-melanogenic effect. In addition, the safety of TLWE was tested. The results of the skin irritation test showed that TLWE is harmless to the human skin, even at higher concentrations than those used in the experiment. Therefore, we suggest that the water extract of T. nucifera leaves has potential for use as a skin-whitening agent.


Subject(s)
MAP Kinase Signaling System/drug effects , Melanins/antagonists & inhibitors , Plant Extracts/pharmacology , Taxaceae/chemistry , Adult , Animals , Cyclic AMP/metabolism , Dose-Response Relationship, Drug , Female , Hot Temperature , Humans , JNK Mitogen-Activated Protein Kinases/metabolism , Male , Melanins/metabolism , Melanoma, Experimental/metabolism , Mice , Plant Extracts/administration & dosage , Plant Extracts/toxicity , Plant Leaves , Signal Transduction/drug effects , Skin Irritancy Tests , alpha-MSH , p38 Mitogen-Activated Protein Kinases/metabolism
2.
Pharmazie ; 75(2): 107-111, 2020 03 20.
Article in English | MEDLINE | ID: mdl-32213243

ABSTRACT

Background: Melanin in the skin is the defense against the harmful UV radiation, which is considered as one of the major risk factors for skin cancer. The compound 7,8-dimethoxycoumarin (DMC, C11H10O4), a natural coumarin molecule present in several medicinal plants, possesses antioxidant and anti-inflammatory activities. However, the mechanism underlying its effects on melanogenesis in melanocytes is unclear. Therefore, we investigated the effect of DMC on melanogenesis activation in B16F10 melanoma cells. Methods: We examined the cytotoxic range of DMC on B16F10 melanoma cells and increased effects of melanogenesis, and intracellular tyrosinase activity. In addition, regulation mechanisms were assessed by Western blot analysis. Results: The results showed that DMC significantly increased melanin content and tyrosinase activity in the cells without being cytotoxic. Furthermore, DMC stimulated the expression of tyrosinase, TRP-1, TRP-2, and MITF thereby activating melanin production and Akt phosphorylation was increased in the Akt signaling pathway. on the contrary, interfering with the phosphorylation of ERK in the MAPKs pathway. Conclusions: These results suggest that DMC may serve as a candidate for potential melanin-producing activator and anti-gray hair applications.


Subject(s)
Coumarins/pharmacology , Melanins/biosynthesis , Microphthalmia-Associated Transcription Factor/metabolism , Mitogen-Activated Protein Kinase Kinases/metabolism , Animals , Cell Line, Tumor , Cell Survival , Extracellular Signal-Regulated MAP Kinases/metabolism , Intramolecular Oxidoreductases/metabolism , Melanocytes/drug effects , Melanocytes/metabolism , Melanoma, Experimental , Membrane Glycoproteins/metabolism , Mice , Monophenol Monooxygenase/metabolism , Oxidoreductases/metabolism
3.
Int J Mol Sci ; 20(6)2019 Mar 25.
Article in English | MEDLINE | ID: mdl-30934595

ABSTRACT

Horse oil products have been used in skin care for a long time in traditional medicine, but the biological effects of horse oil on the skin remain unclear. This study was conducted to evaluate the protective effect of horse oil on ultraviolet B (UVB)-induced oxidative stress in human HaCaT keratinocytes. Horse oil significantly reduced UVB-induced intracellular reactive oxygen species and intracellular oxidative damage to lipids, proteins, and DNA. Horse oil absorbed light in the UVB range of the electromagnetic spectrum and suppressed the generation of cyclobutane pyrimidine dimers, a photoproduct of UVB irradiation. Western blotting showed that horse oil increased the UVB-induced Bcl-2/Bax ratio, inhibited mitochondria-mediated apoptosis and matrix metalloproteinase expression, and altered mitogen-activated protein kinase signaling-related proteins. These effects were conferred by increased phosphorylation of extracellular signal-regulated kinase 1/2 and decreased phosphorylation of p38 and c-Jun N-terminal kinase 1/2. Additionally, horse oil reduced UVB-induced binding of activator protein 1 to the matrix metalloproteinase-1 promoter site. These results indicate that horse oil protects human HaCaT keratinocytes from UVB-induced oxidative stress by absorbing UVB radiation and removing reactive oxygen species, thereby protecting cells from structural damage and preventing cell death and aging. In conclusion, horse oil is a potential skin protectant against skin damage involving oxidative stress.


Subject(s)
Keratinocytes/pathology , Keratinocytes/radiation effects , Oils/pharmacology , Oxidative Stress/radiation effects , Ultraviolet Rays , Absorption, Radiation , Animals , Apoptosis/radiation effects , Cell Line , Enzyme Activation/radiation effects , Horses , Humans , Keratinocytes/enzymology , MAP Kinase Signaling System/radiation effects , Matrix Metalloproteinases/metabolism , Reactive Oxygen Species/metabolism
4.
Fish Shellfish Immunol ; 32(5): 662-9, 2012 May.
Article in English | MEDLINE | ID: mdl-22326761

ABSTRACT

Two paralogous isoform cDNAs of warm-temperature-acclimation-associated 65-kDa protein (Wap65-1 and Wap65-2) were isolated from the cypriniform species, mud loach (Misgurnus mizolepis), and characterized. The deduced amino acid sequences of the two mud loach Wap65 isoforms (mlWap65-1 and mlWap65-2) share moderate levels of sequence homology with their corresponding orthologues from teleosts and with human hemopexin, a possible mammalian homologue. Both isoforms display conserved features, including essential motifs and/or residues that are important for the protein structure of hemopexin. In overall, mlWap65-2 is more homologous to human hemopexin than is mlWap65-1. Both mud loach Wap65 transcripts are predominantly expressed in liver, although the transcripts are ubiquitously detectable in most tissues with variable basal expression. Both mlWap65 isoforms are differentially regulated during embryonic development, and the changes in transcript levels during embryogenesis are greater for mlWap65-2 than for mlWap65-1. The transcription of the mlWap65 genes is differentially modulated by various stimuli, including thermal changes, immune challenge (lipopolysaccharide injection or bacterial infection), and heavy metal exposure (cadmium, copper, or nickel). The isoform mlWap65-1 is more responsive to warm temperature treatments than mlWap65-2, whereas mlWap65-2 is much more strongly stimulated by immune and heavy metal challenges than is mlWap65-1. Taken together, the results of this study suggest that mud loach Wap65 isoforms are potentially involved in multiple cellular pathways and that the two mud loach Wap65 isoforms undergo functional partitioning or subfunctionalization.


Subject(s)
Cypriniformes/genetics , Fish Proteins/metabolism , Hemopexin/analogs & derivatives , Hemopexin/metabolism , Liver/metabolism , Acclimatization , Amino Acid Sequence , Animals , Cypriniformes/metabolism , DNA, Complementary/chemistry , DNA, Complementary/genetics , DNA, Complementary/metabolism , Fish Proteins/chemistry , Fish Proteins/genetics , Hemopexin/chemistry , Hemopexin/genetics , Hot Temperature , Molecular Sequence Data , Protein Isoforms/chemistry , Protein Isoforms/genetics , Protein Isoforms/metabolism , Real-Time Polymerase Chain Reaction/veterinary
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