{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T04:38:43Z","timestamp":1790483923387,"version":"4.1.0"},"reference-count":28,"publisher":"MDPI AG","issue":"12","license":[{"start":{"date-parts":[[2016,12,11]],"date-time":"2016-12-11T00:00:00Z","timestamp":1481414400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>3-Mercaptopyruvate sulfurtransferase (MST) is one of the principal enzymes for the production of hydrogen sulfide and polysulfides in mammalians, and emerging evidence supports the physiological significance of MST. As a fundamental study of the physiology and pathobiology of MST, it is necessary to establish the tissue distribution of MST in mice. In the present study, the expression of MST in various organs of adult and fetal mice was analyzed by Western blotting and enzyme-immunohistochemistry. Moreover, the histology of MST gene\u2013deficient mice was examined. Western blotting revealed that all organs examined had MST. The brain, liver, kidneys testes, and endocrine organs contained large amounts of MST, but the lungs, spleen, thymus, and small intestine did not. Immunohistochemically, the MST expression pattern varies in a cell-specific manner. In the brain, neural and glial cells are positively stained; in the lung, bronchiolar cells are preferentially stained; in the liver, hepatocytes around central veins are more strongly stained; renal convoluted cells are strongly stained; and pancreatic islets are strongly stained. Fetal tissues were studied, and MST expression was found to be similar before and after birth. Histological observation revealed no remarkable findings in MST gene\u2013deficient mice. The present study revealed fundamental information regarding the MST expression of various organs in adult and fetal mice, and the morphological phenotype of MST gene\u2013deficient mice.<\/jats:p>","DOI":"10.3390\/molecules21121707","type":"journal-article","created":{"date-parts":[[2016,12,12]],"date-time":"2016-12-12T14:43:57Z","timestamp":1481553837000},"page":"1707","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":48,"title":["Expression of 3-Mercaptopyruvate Sulfurtransferase in the Mouse"],"prefix":"10.3390","volume":"21","author":[{"given":"Masahiro","family":"Tomita","sequence":"first","affiliation":[{"name":"Department of Pathology and Experimental Medicine, Kumamoto University Graduate School of Medical Sciences, 1-1-1 Honjo Chuo-ku, Kumamoto 860-8556, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Noriyuki","family":"Nagahara","sequence":"additional","affiliation":[{"name":"Isotope Research Center, Nippon Medical School; Tokyo 113-8602, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takaaki","family":"Ito","sequence":"additional","affiliation":[{"name":"Department of Pathology and Experimental Medicine, Kumamoto University Graduate School of Medical Sciences, 1-1-1 Honjo Chuo-ku, Kumamoto 860-8556, Japan"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2016,12,11]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"1066","DOI":"10.1523\/JNEUROSCI.16-03-01066.1996","article-title":"The possible role of hydrogen sulfide as an endogenous neuromodulator","volume":"6","author":"Abe","year":"1996","journal-title":"J. Neurosci."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1038\/nrm3391","article-title":"H2S signalling through protein sulfhydration and beyond","volume":"13","author":"Paul","year":"2012","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"986","DOI":"10.1126\/science.1209855","article-title":"H2S: A universal defense against antibiotics in bacteria","volume":"334","author":"Shatalin","year":"2011","journal-title":"Science"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1089\/ars.2009.2657","article-title":"Interactions of Multiple Gas-Transducing Systems: Hallmarks and Uncertainties of CO, NO, and H2S Gas Biology","volume":"13","author":"Kajimura","year":"2010","journal-title":"Antioxid. Redox Signal."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1089\/ars.2011.4349","article-title":"Role of Cystathionine \u03b3-Lyase\/Hydrogen Sulfide Pathway in Cardiovascular Disease: A Novel Therapeutic Strategy?","volume":"17","author":"Pan","year":"2012","journal-title":"Antioxid. Redox Signal."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1016\/j.niox.2013.07.002","article-title":"Hydrogen sulfide chemical biology: Pathophysiological roles and detection","volume":"35","author":"Kolluru","year":"2013","journal-title":"Nitric Oxide"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"16146","DOI":"10.3390\/molecules191016146","article-title":"Hydrogen sulfide and polysulfides as biological mediators","volume":"19","author":"Kimura","year":"2014","journal-title":"Molecules"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1089\/ars.2013.5324","article-title":"Hydrogen sulfide and the pathogenesis of atherosclerosis","volume":"20","author":"Mani","year":"2014","journal-title":"Antioxid. Redox Signal."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1038\/nrd4433","article-title":"Hydrogen sulfide-based therapeutics: Exploiting a unique but ubiquitous gasotransmitter","volume":"14","author":"Wallace","year":"2015","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"21903","DOI":"10.1074\/jbc.R110.128363","article-title":"Redox biochemistry of hydrogen sulfide","volume":"285","author":"Kabul","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"1913","DOI":"10.1093\/oxfordjournals.jbchem.a133393","article-title":"The mechanism of the l-cystine cleavage reaction catalyzed by rat liver gamma-cystathionase","volume":"89","author":"Yamanishi","year":"1981","journal-title":"J. Biochem."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"813","DOI":"10.1089\/ars.2005.7.813","article-title":"The role of cystathionine beta-synthase in homocysteine metabolism","volume":"7","author":"Jhee","year":"2005","journal-title":"Antioxid. Redox Signal."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1093\/jb\/mvp111","article-title":"Vascular endothelium expresses 3-mercaptopyruvate sulfurtransferase and produces hydrogen sulfide","volume":"146","author":"Shibuya","year":"2009","journal-title":"J. Biochem."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1089\/ars.2011.4468","article-title":"Is novel signal transducer sulfur oxide involved in the redox cycle of persulfide at the catalytic site cysteine in a stable reaction intermediate of mercaptopyruvate sulfurtransferase?","volume":"16","author":"Nagahara","year":"2012","journal-title":"Antioxid. Redox Signal."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"277","DOI":"10.1007\/s10620-007-9854-9","article-title":"Differentiation of the roles of sulfide oxidase and rhodanese in the detoxification of sulfide by the colonic mucosa","volume":"53","author":"Wilson","year":"2008","journal-title":"Dig. Dis. Sci."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"14774","DOI":"10.1038\/srep14774","article-title":"Identification of H2S3 and H2S produced by 3-mercaptopyruvate sulfurtransferase in the brain","volume":"5","author":"Kimura","year":"2015","journal-title":"Sci. Rep."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"29","DOI":"10.1111\/jnc.12698","article-title":"Contribution of cysteine aminotransferase and mercaptopyruvate sulfurtransferase to hydrogen sulfide production in peripheral neurons","volume":"130","author":"Minamoto","year":"2014","journal-title":"J. Neurochem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1007\/s004180050286","article-title":"Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: Confocal laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis","volume":"110","author":"Nagahara","year":"1998","journal-title":"Histochem. Cell Biol."},{"key":"ref_19","first-page":"1277","article-title":"Mercaptopyruvate sulfurtransferase as a defense against cyanide toxication: Molecular properties and mode of detoxification","volume":"14","author":"Nagahara","year":"1999","journal-title":"Histol. Histopathol."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"34569","DOI":"10.1074\/jbc.M505643200","article-title":"Post-translational regulation of mercaptopyruvate sulfurtransferase via a low redox potential cysteine-sulfenate in the maintenance of redox homeostasis","volume":"280","author":"Nagahara","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1561","DOI":"10.1074\/jbc.M605931200","article-title":"Thioredoxin-dependent enzymatic activation of mercaptopyruvate sulfurtransferase. An intersubunit disulfide bond serves as a redox switch for activation","volume":"282","author":"Nagahara","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"1986","DOI":"10.1038\/srep01986","article-title":"Antioxidant enzyme, 3-mercaptopyruvate sulfurtransferase-knockout mice exhibit increased anxiety-like behaviors: A model for human mercaptolactate-cysteine disulfiduria","volume":"3","author":"Nagahara","year":"2013","journal-title":"Sci. Rep."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"21350","DOI":"10.3390\/molecules191221350","article-title":"Is development of high-grade gliomas sulfur-dependent?","volume":"19","author":"Czubak","year":"2014","journal-title":"Molecules"},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Zhao, H., Chan, S.J., Ng, Y.K., and Wong, P.T.H. (2013). Brain 3-Mercaptopyruvate Sulfurtransferase (3MST): Cellular Localization and Downregulation after Acute Stroke. PLoS ONE, 8.","DOI":"10.1371\/journal.pone.0067322"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"703","DOI":"10.1089\/ars.2008.2253","article-title":"3-Mercaptopyruvate Sulfurtransferase Produces Hydrogen Sulfide and Bound Sulfane Sulfur in the Brain","volume":"11","author":"Shibuya","year":"2009","journal-title":"Antioxid. Redox Signal."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1016\/j.autneu.2013.08.066","article-title":"Chronic intermittent hypoxia promotes expression of 3-mercaptopyruvate sulfurtransferase in adult rat medulla oblongata","volume":"179","author":"Li","year":"2013","journal-title":"Auton. Neurosci."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1","DOI":"10.2119\/molmed.2015.00035","article-title":"Regulation of Vascular Tone, Angiogenesis and Cellular Bioenergetics by the 3-Mercaptopyruvate Sulfurtransferase\/H2S Pathway: Functional Impairment by Hyperglycemia and Restoration by DL-\u03b1-Lipoic Acid","volume":"21","author":"Coletta","year":"2015","journal-title":"Mol. Med."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"4008","DOI":"10.1002\/pmic.200700341","article-title":"HUPO BPP pilot study: A proteomics analysis of the mouse brain of different developmental stages","volume":"7","author":"Wang","year":"2007","journal-title":"Proteomics"}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/21\/12\/1707\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T19:28:23Z","timestamp":1760210903000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/21\/12\/1707"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,12,11]]},"references-count":28,"journal-issue":{"issue":"12","published-online":{"date-parts":[[2016,12]]}},"alternative-id":["molecules21121707"],"URL":"https:\/\/doi.org\/10.3390\/molecules21121707","relation":{},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,12,11]]}}}