Brain 3-Mercaptopyruvate Sulfurtransferase (3MST): Cellular Localization and Downregulation after Acute Stroke

3-Mercaptopyruvate sulfurtransferase (3MST) is an important enzyme for the synthesis of hydrogen sulfide (H2S) in the brain. We present here data that indicate an exclusively localization of 3MST in astrocytes. Regional distribution of 3MST activities is even and unremarkable. Following permanent mi...

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Published in:PloS one 2013-06, Vol.8 (6), p.e67322
Main Authors: Zhao, Heng, Chan, Su-Jing, Ng, Yee-Kong, Wong, Peter T-H
Format: Article
Language:English
Subjects:
3-Mercaptopyruvate sulfurtransferase
Animals
Astrocytes
Astrocytes - enzymology
Astrocytes - pathology
Brain
Cardiovascular system
Cell adhesion & migration
Central nervous system
Cerebral blood flow
Cerebral Cortex - enzymology
Cerebral Cortex - pathology
Corpus Callosum - enzymology
Corpus Callosum - pathology
Corpus Striatum - enzymology
Corpus Striatum - pathology
Down-Regulation
Enzymes
Gene Expression Regulation, Enzymologic
Gliosis
Homocysteine
Hydrogen
Hydrogen sulfide
Hydrogen Sulfide - metabolism
Ischemia
Localization
Male
Medicine
Neostriatum
Nervous system
Neurosciences
Occlusion
Pharmacology
Rats
Rats, Sprague-Dawley
Rodents
Stroke
Stroke - enzymology
Stroke - pathology
Sulfide
Sulfurtransferase
Sulfurtransferases - biosynthesis
Tumor necrosis factor-TNF
Veins & arteries
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description 3-Mercaptopyruvate sulfurtransferase (3MST) is an important enzyme for the synthesis of hydrogen sulfide (H2S) in the brain. We present here data that indicate an exclusively localization of 3MST in astrocytes. Regional distribution of 3MST activities is even and unremarkable. Following permanent middle cerebral artery occlusion (pMCAO), 3MST was down-regulated in both the cortex and striatum, but not in the corpus collosum. It appears that the down-regulation of astrocytic 3MST persisted in the presence of astrocytic proliferation due to gliosis. Our observations indicate that 3MST is probably not responsible for the increased production of H2S following pMCAO. Therefore, cystathionine β-synthase (CBS), the alternative H2S producing enzyme in the CNS, remains as a more likely potential therapeutic target than 3MST in the treatment of acute stroke through inhibition of H2S production.
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We present here data that indicate an exclusively localization of 3MST in astrocytes. Regional distribution of 3MST activities is even and unremarkable. Following permanent middle cerebral artery occlusion (pMCAO), 3MST was down-regulated in both the cortex and striatum, but not in the corpus collosum. It appears that the down-regulation of astrocytic 3MST persisted in the presence of astrocytic proliferation due to gliosis. Our observations indicate that 3MST is probably not responsible for the increased production of H2S following pMCAO. 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subjects 3-Mercaptopyruvate sulfurtransferase
Animals
Astrocytes
Astrocytes - enzymology
Astrocytes - pathology
Brain
Cardiovascular system
Cell adhesion & migration
Central nervous system
Cerebral blood flow
Cerebral Cortex - enzymology
Cerebral Cortex - pathology
Corpus Callosum - enzymology
Corpus Callosum - pathology
Corpus Striatum - enzymology
Corpus Striatum - pathology
Down-Regulation
Enzymes
Gene Expression Regulation, Enzymologic
Gliosis
Homocysteine
Hydrogen
Hydrogen sulfide
Hydrogen Sulfide - metabolism
Ischemia
Localization
Male
Medicine
Neostriatum
Nervous system
Neurosciences
Occlusion
Pharmacology
Rats
Rats, Sprague-Dawley
Rodents
Stroke
Stroke - enzymology
Stroke - pathology
Sulfide
Sulfurtransferase
Sulfurtransferases - biosynthesis
Tumor necrosis factor-TNF
Veins & arteries
title Brain 3-Mercaptopyruvate Sulfurtransferase (3MST): Cellular Localization and Downregulation after Acute Stroke
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