A novel pathway for the production of hydrogen sulfide from D-cysteine in mammalian cells

Norihiro Shibuya, Shin Koike, Makiko Tanaka, Mari Ishigami-Yuasa, Yuka Kimura, Yuki Ogasawara, Kiyoshi Fukui, Noriyuki Nagahara and Hideo Kimura ()
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Norihiro Shibuya: National Institute of Neuroscience
Shin Koike: National Institute of Neuroscience
Makiko Tanaka: National Institute of Neuroscience
Mari Ishigami-Yuasa: National Institute of Neuroscience
Yuka Kimura: National Institute of Neuroscience
Yuki Ogasawara: Meiji Pharmaceutical University
Kiyoshi Fukui: The Institute for Enzyme Research, The University of Tokushima
Noriyuki Nagahara: Nippon Medical School
Hideo Kimura: National Institute of Neuroscience

Nature Communications, 2013, vol. 4, issue 1, 1-7

Abstract: Abstract In eukaryotes, hydrogen sulphide acts as a signalling molecule and cytoprotectant. Hydrogen sulphide is known to be produced from L-cysteine by cystathionine β-synthase, cystathionine γ-lyase and 3-mercaptopyruvate sulfurtransferase coupled with cysteine aminotransferase. Here we report an additional biosynthetic pathway for the production of hydrogen sulphide from D-cysteine involving 3-mercaptopyruvate sulfurtransferase and D-amino acid oxidase. Unlike the L-cysteine pathway, this D-cysteine-dependent pathway operates predominantly in the cerebellum and the kidney. Our study reveals that administration of D-cysteine protects primary cultures of cerebellar neurons from oxidative stress induced by hydrogen peroxide and attenuates ischaemia-reperfusion injury in the kidney more than L-cysteine. This study presents a novel pathway of hydrogen sulphide production and provides a new therapeutic approach to deliver hydrogen sulphide to specific tissues.

Date: 2013
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DOI: 10.1038/ncomms2371

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