Open AccessHydrogen gas protects IP3Rs by reducing disulfide bridges in human keratinocytes under oxidative stress
Author(s) -
ChiehShan Wu,
Wen Li Hsu,
M. H. Tsai,
Jin-Wei Liang,
Jian Lu,
Chia Jung Yen,
Hsin Su Yu,
Мами Нода,
Cheng-Hsien Lu,
Chu Huang Chen,
Shian Jang Yan,
Tohru Yoshioka
Publication year - 2017
Publication title -
scientific reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.24
H-Index - 213
ISSN - 2045-2322
DOI - 10.1038/s41598-017-03513-2
Subject(s) - oxidative stress , disulfide bond , hydrogen , chemistry , oxidative phosphorylation , biochemistry , organic chemistry
Based on the oxidative stress theory, aging derives from the accumulation of oxidized proteins induced by reactive oxygen species (ROS) in the cytoplasm. Hydrogen peroxide (H 2 O 2 ) elicits ROS that induces skin aging through oxidation of proteins, forming disulfide bridges with cysteine or methionine sulfhydryl groups. Decreased Ca 2+ signaling is observed in aged cells, probably secondary to the formation of disulfide bonds among Ca 2+ signaling-related proteins. Skin aging processes are modeled by treating keratinocytes with H 2 O 2 . In the present study, H 2 O 2 dose-dependently impaired the adenosine triphosphate (ATP)-induced Ca 2+ response, which was partially protected via co-treatment with β-mercaptoethanol, resulting in reduced disulfide bond formation in inositol 1, 4, 5-trisphosphate receptors (IP 3 Rs). Molecular hydrogen (H 2 ) was found to be more effectively protected H 2 O 2 -induced IP 3 R1 dysfunction by reducing disulfide bonds, rather than quenching ROS. In conclusion, skin aging processes may involve ROS-induced protein dysfunction due to disulfide bond formation, and H 2 can protect oxidation of this process.