Related Experiment Video
Updated: Jun 21, 2026

A Sensitive Visual Method for the Detection of Hydrogen Sulfide Producing Bacteria
Published on: June 27, 2022
Vascular endothelium expresses 3-mercaptopyruvate sulfurtransferase and produces hydrogen sulfide
Norihiro Shibuya1, Yoshinori Mikami, Yuka Kimura
1National Institute of Neuroscience, National Center of Neurology and Psychiatry, 4-1-1 Ogawahigashi, Kodaira, Tokyo 187-8502, Japan.
Abstract:
Hydrogen sulfide (H(2)S) has been recognized as a smooth muscle relaxant. Cystathionine gamma-lyase, which is localized to smooth muscle, is thought to be the major H(2)S-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 H(2)S. Both 3MST and CAT were localized to endothelium. Lysates of vascular endothelial cells produced H(2)S from cysteine and alpha-ketoglutarate. The present study provides a new insight into the production and release of H(2)S as a smooth muscle relaxant from vascular endothelium.
More Related Videos
08:57Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
Published on: February 24, 2018
06:53Visualization of Mitochondrial Respiratory Function using Cytochrome C Oxidase / Succinate Dehydrogenase (COX/SDH) Double-labeling Histochemistry
Published on: November 23, 2011
Related Concept Videos
Sulfur Assimilation
Microbes and the Sulfur Cycle
Regulation of Angiogenesis and Blood Supply
Electron Transport Chain: Complex III and IV
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Preparation and Reactions of Thiols