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1.
Annals of Dermatology ; : 315-320, 2013.
Article in English | WPRIM | ID: wpr-131880

ABSTRACT

BACKGROUND: The fibrous proteins of extracellular matrix (ECM) produced by dermal fibroblast contributes to the maintenance of connective tissue integrity. OBJECTIVE: This study is carried out to identify the bioactive ingredient from natural products that enhances ECM production in dermal fibroblasts. METHODS: Bioassay-directed fractionation was used to isolate the active ingredient from natural extracts. The effects of rasatiol (isolated from Raphanus sativus) on ECM production in primary cultured human dermal fibroblasts was investigated by enzyme linked immunosorbent assay and western blot analysis. RESULTS: Rasatiol accelerated fibroblast growth in a dose-dependent manner and increased the production of type 1 collagen, fibronectin and elastin. Phosphorylation of p42/44 extracellular signal-regulated kinase, p38 mitogen-activated protein kinase, and Akt was remarkably increased by rasatiol, indicating that enhanced ECM production is linked to the activation of intracellular signaling cascades. CONCLUSION: These results indicate that rasatiol stimulates the fibrous components of ECM production, and may be applied to the maintenance of skin texture.


Subject(s)
Humans , Blotting, Western , Collagen Type I , Connective Tissue , Elastin , Enzyme-Linked Immunosorbent Assay , Extracellular Matrix , Fibroblasts , Fibronectins , Phosphorylation , Phosphotransferases , Protein Kinases , Raphanus , Scleroproteins , Skin
2.
Annals of Dermatology ; : 315-320, 2013.
Article in English | WPRIM | ID: wpr-131877

ABSTRACT

BACKGROUND: The fibrous proteins of extracellular matrix (ECM) produced by dermal fibroblast contributes to the maintenance of connective tissue integrity. OBJECTIVE: This study is carried out to identify the bioactive ingredient from natural products that enhances ECM production in dermal fibroblasts. METHODS: Bioassay-directed fractionation was used to isolate the active ingredient from natural extracts. The effects of rasatiol (isolated from Raphanus sativus) on ECM production in primary cultured human dermal fibroblasts was investigated by enzyme linked immunosorbent assay and western blot analysis. RESULTS: Rasatiol accelerated fibroblast growth in a dose-dependent manner and increased the production of type 1 collagen, fibronectin and elastin. Phosphorylation of p42/44 extracellular signal-regulated kinase, p38 mitogen-activated protein kinase, and Akt was remarkably increased by rasatiol, indicating that enhanced ECM production is linked to the activation of intracellular signaling cascades. CONCLUSION: These results indicate that rasatiol stimulates the fibrous components of ECM production, and may be applied to the maintenance of skin texture.


Subject(s)
Humans , Blotting, Western , Collagen Type I , Connective Tissue , Elastin , Enzyme-Linked Immunosorbent Assay , Extracellular Matrix , Fibroblasts , Fibronectins , Phosphorylation , Phosphotransferases , Protein Kinases , Raphanus , Scleroproteins , Skin
3.
Annals of Dermatology ; : 16-21, 2012.
Article in English | WPRIM | ID: wpr-122683

ABSTRACT

BACKGROUND: The extracellular matrix (ECM) produced by dermal fibroblasts supports skin structure, and degradation and/or reduced production of ECM are the main causes of wrinkle formation. OBJECTIVE: The aim of this study was to identify the active ingredient that enhances ECM production in dermal fibroblasts. METHODS: Polarity-based fractionation was used to isolate the active ingredient from natural extracts, and the effects of cedrol (isolated from Pterocarpus indicusirginia) on ECM production in cultured human dermal fibroblasts was investigated by reverse transcription-polymerase chain reaction, enzyme linked immunosorbent assay, and Western blot analysis. RESULTS: Cedrol accelerated fibroblast growth in a dose-dependent manner and increased the production of type 1 collagen and elastin. Phosphorylation of p42/44 extracellular signal-regulated kinase, p38 mitogen-activated protein kinase, and Akt was markedly increased by cedrol, indicating that enhanced ECM production is linked to activation of intracellular signaling cascades. CONCLUSION: These results indicate that cedrol stimulates ECM production, with possible applications to the maintenance of skin texture.


Subject(s)
Humans , Blotting, Western , Collagen , Collagen Type I , Elastin , Enzyme-Linked Immunosorbent Assay , Extracellular Matrix , Fibroblasts , Phosphorylation , Phosphotransferases , Protein Kinases , Pterocarpus , Skin , Terpenes
4.
Annals of Dermatology ; : 173-179, 2010.
Article in English | WPRIM | ID: wpr-54706

ABSTRACT

BACKGROUND: Fibroblasts produce many components of the extracellular matrix (ECM) and so they contribute to the maintenance of connective tissue integrity. OBJECTIVE: The aim of this study is to evaluate the effect of velvet antler extract (VAE) on the ECM production of dermal fibroblasts cultured in vitro. METHODS: Primary cultured human dermal fibroblasts were treated with VAE, and then the ECM production was determined by RT-PCR, ELISA and Western blot analysis. Furthermore, the change of gene expression according to VAE treatment was evaluated by cDNA microarray. RESULTS: VAE accelerated the growth of fibroblasts in a dose-dependent manner. VAE increased the production of several ECM components, including type 1 collagen, fibronectin and elastin. In line with these results, the phosphorylations of p42/44 ERK and p38 mitogen-activated protein kinase were markedly increased by VAE, suggesting that the enhancement of ECM production may be linked to the activation of intracellular signaling cascades. VAE also significantly increased cell migration on an in vitro scratch wound test. In cDNA microarray, many genes related with connective tissue integrity were identified to be up-regulated by VAE. CONCLUSION: These results suggest that VAE has a potential to stimulate ECM production, and VAE may be applicable for maintaining the skin's texture.


Subject(s)
Animals , Humans , Antlers , Blotting, Western , Cell Movement , Collagen Type I , Connective Tissue , Elastin , Enzyme-Linked Immunosorbent Assay , Extracellular Matrix , Fibroblasts , Fibronectins , Gene Expression , Oligonucleotide Array Sequence Analysis , Phosphorylation , Protein Kinases
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