Volume 45, Issue 6 pp. 547-555
ORIGINAL ARTICLE

Gomisin A modulates aging progress via mitochondrial biogenesis in human diploid fibroblast cells

Jeong-Seok Kim

Jeong-Seok Kim

Department of Physical Education, College of Education, Chonbuk National University, Jeonju, South Korea

Department of Oral Biochemistry, Institute of Oral Bioscience, School of Dentistry, Chonbuk National University, Jeonju, South Korea

Search for more papers by this author
Seon-Hwa Jeong

Seon-Hwa Jeong

Department of Oral Biochemistry, Institute of Oral Bioscience, School of Dentistry, Chonbuk National University, Jeonju, South Korea

Search for more papers by this author
Sin-Hee Han

Sin-Hee Han

Department of Herbal Crop Research, National Institute of Horticultural & Herbal Science, RDA, Chungbuk, South Korea

Search for more papers by this author
Ho-Keun Yi

Corresponding Author

Ho-Keun Yi

Department of Oral Biochemistry, Institute of Oral Bioscience, School of Dentistry, Chonbuk National University, Jeonju, South Korea

Correspondence

Ho-Keun Yi, Department of Oral Biochemistry, School of Dentistry, Chonbuk National University, Jeonju, South Korea.

Email: [email protected]

Search for more papers by this author
First published: 10 January 2018
Citations: 14

Summary

Gomisin A from the fruit of Schisandra chinensis has many pharmacological properties, including hepato-protective, anti-diabetic, and anti-oxidative stress. However, the potential benefit of gomisin A is still not well understood, especially in aging progression. Therefore, the aim of this study was to clarify whether the promotion of mitochondrial biogenesis and autophagy of gomisin A affects anti-aging progression, and its mechanism. Intermediate (PD32) human diploid fibroblast (HDF) cells were brought to stress-induced premature senescence (SIPS) using hydrogen peroxide. Gomisin A inhibited reactive oxygen species production even in the SIPS-HDF cells. Gomisin A was also able to attenuate the activity of senescence-associated β-galactosidase and the production of pro-inflammatory molecules in the SIPS as well as aged HDF cells. The antioxidant activity of gomisin A was determined by recovering the Cu/Zn, Mn-SOD, and HO-1 expression in the SIPS-HDF cells. In mechanistic aspect, gomisin A inhibited the mitogen-activated protein kinase pathway and the translocation of nuclear factor kappa B to the nucleus. In addition, gomisin A promoted the autophagy and mitochondrial biogenesis factors through the translocation of nuclear factor erythroid 2-related factor-2, and inhibited aging progression in the SIPS-HDF cells. In summary, the enhanced properties of mitochondrial biogenesis and autophagy of gomisin A has a benefit to control age-related molecules against SIPS-induced chronic oxidative stress, and gomisin A may be a potential therapeutic compound for the enhancement of intracellular homeostasis to aging progression.

CONFLICT OF INTEREST

The authors declare that they have no conflict of interest.

The full text of this article hosted at iucr.org is unavailable due to technical difficulties.