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Journal of Biochemistry Advance Access originally published online on July 15, 2009
Journal of Biochemistry 2009 146(5):623-626; doi:10.1093/jb/mvp111
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© The Authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved

Rapid Communications

Vascular Endothelium Expresses 3-Mercaptopyruvate Sulfurtransferase and Produces Hydrogen Sulfide

Norihiro Shibuya1,*, Yoshinori Mikami1,*, Yuka Kimura1, Noriyuki Nagahara2 and Hideo Kimura1,{dagger}

1National Institute of Neuroscience, National Center of Neurology and Psychiatry, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502; and 2Department of Environmental Medicine, Nippon Medical School, 1-1-5 Sendagi, Bunkyo, Tokyo 113-8602, Japan

{dagger}To whom correspondence should be addressed. Tel: +81-42-346-1725, Fax: +81-42-346-1755, E-mail: kimura{at}ncnp.go.jp

Received June 22, 2009; Accepted July 7, 2009


  Abstract

Hydrogen sulfide (H2S) has been recognized as a smooth muscle relaxant. Cystathionine {gamma}-lyase, which is localized to smooth muscle, is thought to be the major H2S-producing enzyme in the thoracic aorta. Here we show that 3-mercaptopyruvate sulfurtransferase (3MST) and cysteine aminotransferase (CAT) are localized to vascular endothelium in the thoracic aorta and produce H2S. Both 3MST and CAT were localized to endothelium. Lysates of vascular endothelial cells produced H2S from cysteine and {alpha}-ketoglutarate. The present study provides a new insight into the production and release of H2S as a smooth muscle relaxant from vascular endothelium.

Key Words: 3-MST, EDRF, endothelium, H2S, relaxation, smooth muscle

Abbreviations: CAT, cysteine aminotransferase; CBS, cystathionine β-synthase; CSE, cystathionine {gamma}-lyase; EDRF, endothelium-derived relaxing factor; H2S, hydrogen sulfide; 3MP, 3-mercaptopyruvate; 3MST, 3-mercaptopyruvate sulfurtransferase; SDS, sodium dodecyl sulfate

*These authors contributed equally to this study.


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