Asiaticoside induces cell proliferation and collagen synthesis in human dermal fibroblasts

Background Asiatiocoside, a saponin component isolated from Centella asiatica can improve wound healing by promoting the proliferation of human dermal fibroblasts (HDF) and synthesis of collagen. The skin-renewing cells and type I and III collagen synthesis decrease with aging, resulting in the reduction of skin elasticity and delayed wound healing. Usage of natural active compounds from plants in wound healing should be evaluated and compared to retinoic acid as an active agent that regulates wound healing. The aim of this study was to compare and evaluate the effect of asiaticoside and retinoic acid to induce greater cell proliferation and type I and III collagen synthesis in human dermal fibroblast. Methods Laboratory experiments were conducted using human dermal fibroblasts (HDF) isolated from human foreskin explants. Seven passages of HDF were treated with asiaticoside and retinoic acid at several doses and incubated for 24 and 48 hours. Cell viability in all groups was tested with the MTT assay to assess HDF proliferation. Type I and III collagen synthesis was examined using the respective ELISA kits. Analysis of variance was performed to compare the treatment groups. Results Asiaticoside had significantly stronger effects on HDF proliferation than retinoic acid (p<0.05). The type III collagen production was significantly greater induction with asiaticoside compared to retinoic acid (p<0.05). Conclusion Asiaticoside induces HDF proliferation and type I and III collagen synthesis in a time- and dose-dependent pattern. Asiaticoside has a similar effect as retinoic acid on type I and type III collagen synthesis.

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The effect of heparin on cell proliferation and type-I collagen synthesis by adult human dermal fibroblasts

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease ◽

10.1016/0925-4439(93)90042-y ◽

1993 ◽

Vol 1180 (3) ◽

pp. 225-230 ◽

Cited By ~ 34

Author(s):

Agatha V. Ferrao ◽

Roger M. Mason

Keyword(s):

Cell Proliferation ◽

Collagen Synthesis ◽

Type I Collagen ◽

Dermal Fibroblasts ◽

Type I ◽

Human Dermal Fibroblasts ◽

Adult Human

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Human collagen alpha-2 type I stimulates collagen synthesis, wound healing, and elastin production in normal human dermal fibroblasts (HDFs)

BMB Reports ◽

10.5483/bmbrep.2020.53.10.120 ◽

2020 ◽

Vol 53 (10) ◽

pp. 539-544

Author(s):

Su Jin Hwang ◽

Geun-Hyoung Ha ◽

Woo-Young Seo ◽

Chung Kwon Kim ◽

KyeongJin Kim ◽

...

Keyword(s):

Wound Healing ◽

Collagen Synthesis ◽

Dermal Fibroblasts ◽

Type I ◽

Human Dermal Fibroblasts ◽

Normal Human ◽

Human Collagen ◽

Normal Human Dermal Fibroblasts

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Non pharmacological high-intensity ultrasound treatment of human dermal fibroblasts to accelerate wound healing

Scientific Reports ◽

10.1038/s41598-021-81878-1 ◽

2021 ◽

Vol 11 (1) ◽

Author(s):

Jeong Yu Lee ◽

Dae-Jin Min ◽

Wanil Kim ◽

Bum-Ho Bin ◽

Kyuhan Kim ◽

...

Keyword(s):

Wound Healing ◽

High Intensity ◽

Mapk Pathway ◽

Dermal Fibroblasts ◽

Ultrasound Treatment ◽

Type I ◽

Human Dermal Fibroblasts ◽

Short Term ◽

High Intensity Ultrasound ◽

Extracellular Matrix Components

AbstractInspired by the effectiveness of low-intensity ultrasound on tissue regeneration, we investigated the potential effect of short-term high-intensity ultrasound treatment for acceleration of wound healing in an in vitro wound model and dermal equivalent, both comprising human dermal fibroblasts. Short-term ultrasound of various amplitudes significantly increased the proliferation and migration of fibroblasts and subsequently increased the production of the extracellular matrix components fibronectin and collagen type I, both of which are important for wound healing and are secreted by fibroblasts. In addition, ultrasound treatment increased the contraction of a fibroblast-embedded three-dimensional collagen matrix, and the effect was synergistically increased in the presence of TGF-β. RNA-sequencing and bioinformatics analyses revealed changes in gene expression and p38 and ERK1/2 MAPK pathway activation in the ultrasound-stimulated fibroblasts. Our findings suggest that ultrasound as a mechanical stimulus can activate human dermal fibroblasts. Therefore, the activation of fibroblasts using ultrasound may improve the healing of various types of wounds and increase skin regeneration.

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Effects of simulated solar radiation on type I and type III collagens, collagenase (MMP-1) and stromelysin (MMP-3) gene expression in human dermal fibroblasts cultured in collagen gels

Journal of Photochemistry and Photobiology B Biology ◽

10.1016/s1011-1344(98)00075-x ◽

1998 ◽

Vol 42 (3) ◽

pp. 226-232 ◽

Cited By ~ 16

Author(s):

Laurent Pascual-Le Tallec ◽

Carla Korwin-Zmijowska ◽

Monique Adolphe

Keyword(s):

Gene Expression ◽

Solar Radiation ◽

Dermal Fibroblasts ◽

Type I ◽

Human Dermal Fibroblasts ◽

Collagen Gels ◽

Type Iii ◽

Simulated Solar Radiation

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Change in phenotype in long-term cultures of a clonal rat bone cell line: switch to the synthesis of α1 (I)-trimer collagen

Canadian Journal of Biochemistry and Cell Biology ◽

10.1139/o84-063 ◽

1984 ◽

Vol 62 (6) ◽

pp. 462-469 ◽

Cited By ~ 2

Author(s):

Hardy Limeback ◽

Kichibee Otsuka ◽

Kam-Ling Yao ◽

Jane E. Aubin ◽

Jaro Sodek

Keyword(s):

Collagen Synthesis ◽

Type I Collagen ◽

Bone Cell ◽

Detectable Effect ◽

Prostaglandin E ◽

Intracellular Camp ◽

Type Iii Collagen ◽

Type I ◽

Type Iii ◽

Type V

A number of bone cell clones isolated from rat calvaria have been maintained in culture for more than 3 years. Several of these clones have undergone dramatic changes in phenotype. One of these clones, RGB 2.2, was observed originally to have a fibroblastic morphology in culture and to respond to parathyroid hormone (PTH), but not prostaglandin E2 (PGE2), with an increase in intracellular cAMP. Throughout several passages in early subcultures, these cells synthesized mostly type I collagen, with small amounts of type III and type V collagens. Whereas PTH had no detectable effect on collagen synthesis, PGE2 decreased the amount of total cell layer collagen, with the greatest effect on type III collagen, while increasing the proportion of type V collagen. Subsequent studies on these cells during 3 years in culture have indicated changes in their phenotype including a progressive change in morphology to a more cuboidal shape and a change in collagen synthesis, the cells producing large amounts of the "embryonic" collagen, α1(I) trimer. The reason(s) for the change in collagen expression is unknown, but may be the result of a change in which gene(s) is being expressed.

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Metabolism of rabbit skin collagen. Differences in the apparent turnover rates of type-I- and type-III-collagen precursors determined by constant intravenous infusion of labelled amino acids

Biochemical Journal ◽

10.1042/bj1810075 ◽

1979 ◽

Vol 181 (1) ◽

pp. 75-82 ◽

Cited By ~ 23

Author(s):

S P Robins

Keyword(s):

Amino Acid ◽

Collagen Synthesis ◽

Specific Radioactivity ◽

Deae Cellulose ◽

Type Iii Collagen ◽

Type I ◽

Turnover Rates ◽

Type Iii ◽

Type I Procollagen ◽

Skin Collagen

Growing rabbits were infused for up to 10 h with labelled proline, tyrosine and leucine to achieve plateau conditions within body free pools, for [3H]proline infusion, blood free-proline specific radioactivity remained constant after about 1 h. For individual animals, type-I- and type-III-collagen precursors were isolated by precipitation with (NH4)2SO4 and DEAE-cellulose chromatography. Experiments where 3H- and 14C-labelled proline and tyrosine were infused concurrently for different periods of time showed that type I procollagen reached plateau specific radioactivity within 3 h and 90% of the plateau value after 2 h infusion, corresponding to a calculated apparent t 1/2 of less than 26 min. Plateau values for type I procollagen were taken as precursor amino acid pool specific radioactivities. The type-III-collagen-precursor fractions consistently showed lower rates of label incorporation and, by assuming that both type I and type III collagens are synthesized from the same amino acid pools, kinetic analysis revealed an apparent t 1/2 for the isolated type-III-collagen precursors of 3.9 h. For proline, there were large variations between animals in the ratio between the precursor pool for collagen synthesis and the skin homogenate free pool (0.31 +/- 0.13, mean +/- S.D.), so that collagen-synthesis rates based solely on total tissue free-pool values for proline are subject to large and inconsistent errors.

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