Role of 3-Mercaptopyruvate Sulfurtransferase (3-MST) in Physiology and Disease [PDF]
Antioxidants, 2023 3-mercaptopyruvate sulfurtransferase (3-MST) plays the important role of producing hydrogen sulfide. Conserved from bacteria to Mammalia, this enzyme is localized in mitochondria as well as the cytoplasm. 3-MST mediates the reaction of 3-mercaptopyruvate
Swetha Pavani Rao +3 more
doaj +6 more sources
Regulation of CyR61 expression and release by 3-mercaptopyruvate sulfurtransferase in colon cancer cells [PDF]
Redox Biology, 2022 Cysteine-rich angiogenic inducer 61 (CYR61, also termed CCN family member 1 or CCN1), is a matricellular protein encoded by the CYR61 gene. This protein has been implicated in the regulation of various cancer-associated processes including tumor growth ...
Kelly Ascenção +2 more
doaj +5 more sources
Expression of 3-Mercaptopyruvate Sulfurtransferase in the Mouse [PDF]
Molecules, 2016 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.
Masahiro Tomita +2 more
doaj +7 more sources
Cysteine Aminotransferase (CAT): A Pivotal Sponsor in Metabolic Remodeling and an Ally of 3-Mercaptopyruvate Sulfurtransferase (MST) in Cancer [PDF]
Molecules, 2020 Metabolic remodeling is a critical skill of malignant cells, allowing their survival and spread. The metabolic dynamics and adaptation capacity of cancer cells allow them to escape from damaging stimuli, including breakage or cross-links in DNA strands ...
Ana Hipólito +3 more
doaj +7 more sources
Brain 3-Mercaptopyruvate Sulfurtransferase (3MST): Cellular Localization and Downregulation after Acute Stroke. [PDF]
PLoS ONE, 2013 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
Heng Zhao +3 more
doaj +6 more sources
Role of 3-mercaptopyruvate sulfurtransferase in cancer: Molecular mechanisms and therapeutic perspectives [PDF]
Translational OncologyThe occurrence and development of tumor is mediated by a wide range of complex mechanisms. Subsequent to nitric oxide and carbon monoxide, hydrogen sulfide (H2S) holds the distinction of being the third identified gasotransmitter.
Ka Zhang +12 more
doaj +4 more sources
Hydrogen Sulfide From Cysteine Desulfurase, Not 3-Mercaptopyruvate Sulfurtransferase, Contributes to Sustaining Cell Growth and Bioenergetics in E. coli Under Anaerobic Conditions [PDF]
Frontiers in Microbiology, 2019 Endogenous hydrogen sulfide (H2S), which is primarily generated by 3-mercaptopyruvate sulfurtransferase (3-MST) in Escherichia coli (E. coli) under aerobic conditions, renders bacteria highly resistant to oxidative stress.
Jun Wang +7 more
doaj +3 more sources
Novel Characterization of Antioxidant Enzyme, 3-Mercaptopyruvate Sulfurtransferase-Knockout Mice: Overexpression of the Evolutionarily-Related Enzyme Rhodanese [PDF]
Antioxidants, 2019 The antioxidant enzyme, 3-mercaptopyruvate sulfurtransferase (MST, EC 2.8.1.2) is localized in the cytosol and mitochondria, while the evolutionarily-related enzyme, rhodanese (thiosulfate sulfurtransferase, TST, EC 2.8.1.1) is localized in the ...
Noriyuki Nagahara +3 more
doaj +4 more sources
Role of 3-Mercaptopyruvate Sulfurtransferase in the Regulation of Proliferation, Migration, and Bioenergetics in Murine Colon Cancer Cells [PDF]
Biomolecules, 2020 3-mercaptopyruvate sulfurtransferase (3-MST) has emerged as one of the significant sources of biologically active sulfur species in various mammalian cells.
Fiona Augsburger +5 more
doaj +4 more sources
Effect of S-Allyl -L-Cysteine on MCF-7 Cell Line 3-Mercaptopyruvate Sulfurtransferase/Sulfane Sulfur System, Viability and Apoptosis. [PDF]
Int J Mol Sci, 2020 The S-Allyl-L-cysteine (SAC) component of aged garlic extract (AGE) is proven to have anticancer, antihepatotoxic, neuroprotective and neurotrophic properties.
Bronowicka-Adamska P +3 more
europepmc +5 more sources