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Toxicology and Environmental Health Sciences

, Volume 11, Issue 4, pp 327–334 | Cite as

Effect of Alginate Oligosaccharides on Collagen Expression in HS 27 Human Dermal Fibroblasts

  • Ra-Mi ParkEmail author
  • Ji-Young AhnEmail author
  • Sang Yong Kim
  • Ji-Hyang Wee
  • Yang-Hoon Kim
  • Jiho Min
Original article
  • 7 Downloads

Abstract

Objective: To examine how three types of AOs affected fibroblasts and whether AOs could induce the synthesis of Col-I and Col-Ill, components of human dermis.

Methods: Three types of alginate oligosaccharides (AOs) were prepared from sodium alginate after treatment with alginate lyase with various time periods (6, 12, and 24 hours, called "Type 1, Type 2, Type 3" respectively) and their effects on collagen expression in HS27 human dermal fibroblasts were examined. Cytotoxicity of alginate oligosaccharides was confirmed by MTT assay. Also expression levels at mRNA and protein levels were determined by reverse tran-scription-PCR (RT-PCR) and western blot, respectively. Results: AOs do not show any cellular toxicity, so they were applied directly to the cells. Treatment with Type 3 AOs resulted in the highlighted expression level of collagen type I (Col-I) mRNA while exposure with Type 1 AOs lead to the highest expression of Collagen type III (Col-Ill) mRNA in HS27 fibroblasts. In addition, the mRNA expression level of matrix metalloprotein-ase-1 (MMP-1), an enzyme involved in collagen degradation, was found to increase in cells treated with AOs at low concentrations but decrease in cells treated with AOs at higher concentrations. Moreover, mRNA expression level of tissue inhibitor metalloproteinase-1 (TIMP-1), an antagonist of MMP-1, was found to be increased by AOs in a concentration-dependent manner.

Conclusion: These results suggest that this AOs might have potential to prevent skin aging by promoting collagen synthesis through the inhibition of collagen degrading enzyme.

Keywords

Alginate oligosaccharide Collagen type I Collagen type III Matrix metalloproteinase-1 Tissue inhibitor metalloproteinase-1 

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Notes

Acknowledgments

This work was carried out with the support of “Cooperative Research Program for agriculture Science & Technology Development (Project No: PJ01267701)” funded by Rural Development Administration, Republic of Korea. The authors are grateful for their support.

Ethical Approval

This article does not contain any studies with human participants or animals performed by any of the authors.

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Copyright information

© The Korean Society of Environmental Risk Assessment and Health Science and Springer 2019

Authors and Affiliations

  1. 1.School of Chemical EngineeringJeonbuk National UniversityJeonjuRepublic of Korea
  2. 2.School of Biological SciencesChungbuk National UniversityCheongjuRepublic of Korea
  3. 3.Department of Food Science and BiotechnologyShin Ansan UniversityAnsanRepublic of Korea

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