Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: confocal laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis

@article{Nagahara1998TissueAS,
  title={Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: confocal laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis},
  author={Noriyuki Nagahara and Takaaki Ito and Hitoshi Kitamura and Takeshi Nishino},
  journal={Histochemistry and Cell Biology},
  year={1998},
  volume={110},
  pages={243-250}
}
Abstract In our previous study, we found that mercaptopyruvate sulfurtransferase (MST) was evolutionarily related to mitochondrial rhodanese. To elucidate the difference between MST and rhodanese, the tissue, cellular, and subcellular distribution of rat MST was determined biochemically and immunohistochemically by using anti-MST antibody raised in rabbit. In an immunohistochemical study, tetramethyl rhodamine isothiocyanate-conjugated phalloidin against F-actin and fluorescein isothiocyanate… 
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Expression of 3-Mercaptopyruvate Sulfurtransferase in the Mouse
TLDR
Fundamental information is revealed regarding the MST expression of various organs in adult and fetal mice, and the morphological phenotype of MST gene–deficient mice.
Plant mercaptopyruvate sulfurtransferases: molecular cloning, subcellular localization and enzymatic activities.
TLDR
Recombinant proteins, expressed in Escherichia coli, exhibited MST/TST activity ratios determined from kcat/Km values of 11 and 26 for MST1 and MST2, respectively, which indicates that the proteins encoded by both AtM ST1 and AtMST2 are MST rather than TST type.
Novel Characterization of Antioxidant Enzyme, 3-Mercaptopyruvate Sulfurtransferase-Knockout Mice: Overexpression of the Evolutionarily-Related Enzyme Rhodanese
TLDR
It is concluded that TST is overexpressed in MST-KO mice and detected only in wild-type mice, as expected.
Characterization and Interaction Studies of Two Isoforms of the Dual Localized 3-Mercaptopyruvate Sulfurtransferase TUM1 from Humans*
TLDR
The studies showed that TUM1 interacts with the l-cysteine desulfurase NFS1 and the rhodanese-like protein MOCS3, suggesting a dual function of Tum1 both in sulfur transfer for the biosynthesis of the molybdenum cofactor, and for the thiolation of tRNA.
Structure and Kinetic Analysis of H2S Production by Human Mercaptopyruvate Sulfurtransferase*
TLDR
The crystal structure analysis allows us to propose a detailed mechanism for MST in which an Asp-His-Ser catalytic triad is positioned to activate the nucleophilic cysteine residue and participate in general acid-base chemistry, whereas the kinetic analysis indicates that thioredoxin is likely to be the major physiological persulfide acceptor from MST.
Sulfurtransferases and Cyanide Detoxification in Mouse Liver, Kidney, and Brain
TLDR
The activity of rhodanese, 3-mercaptopyruvate sulfurtransferase (MPST) and cystathionase in mouse liver, kidney, and four brain regions was studied and it seemed that in the telencephalon, where the total sulfur content, but not the sulfane sulfur level, was significantly increased, some sulfur-containing compounds appeared in response to cyanide.
Arabidopsis thaliana 3-mercaptopyruvate sulfurtransferases interact with and are protected by reducing systems
Evidence for a functional genetic polymorphism of the human thiosulfate sulfurtransferase (Rhodanese), a cyanide and H2S detoxification enzyme.
Potential role of the 3-mercaptopyruvate sulfurtransferase (3-MST)-hydrogen sulfide (H2S) pathway in cancer cells.
Thioredoxin regulates human mercaptopyruvate sulfurtransferase at physiologically-relevant concentrations
TLDR
The poorly-studied MPST1 variant is characterized and it is demonstrated that substitutions in its Ser–His–Asp triad, proposed to serve a general acid–base role, minimally affect catalytic activity, revealing MPST's potential to generate low-molecular-weight persulfides.
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