Role of 3-Mercaptopyruvate Sulfurtransferase (3-MST) in Physiology and Disease [PDF]
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 +4 more sources
Activation of 3-Mercaptopyruvate Sulfurtransferase by Glutaredoxin Reducing System [PDF]
Glutaredoxin (EC 1.15–1.21) is known as an oxidoreductase that protects cysteine residues within proteins against oxidative stress. Glutaredoxin catalyzes an electron transfer reaction that donates an electron to substrate proteins in the reducing system
Noriyuki Nagahara
doaj +5 more sources
Expression of 3-Mercaptopyruvate Sulfurtransferase in the Mouse [PDF]
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 +5 more sources
Regulation of CyR61 expression and release by 3-mercaptopyruvate sulfurtransferase in colon cancer cells [PDF]
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 +4 more sources
Role of 3-mercaptopyruvate sulfurtransferase in cancer: Molecular mechanisms and therapeutic perspectives [PDF]
The 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 +3 more sources
Cysteine Aminotransferase (CAT): A Pivotal Sponsor in Metabolic Remodeling and an Ally of 3-Mercaptopyruvate Sulfurtransferase (MST) in Cancer [PDF]
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 +5 more sources
Brain 3-Mercaptopyruvate Sulfurtransferase (3MST): Cellular Localization and Downregulation after Acute Stroke. [PDF]
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 +5 more sources
Cardiovascular phenotype of mice lacking 3-mercaptopyruvate sulfurtransferase. [PDF]
Hydrogen sulfide (H2S) is a physiological mediator that regulates cardiovascular homeostasis. Three major enzymes contribute to the generation of endogenously produced H2S, namely cystathionine γ-lyase (CSE), cystathionine β-synthase (CBS) and 3-mercaptopyruvate sulfurtransferase (3-MST).
Peleli M +14 more
europepmc +5 more sources
3-Mercaptopyruvate sulfurtransferase supports endothelial cell angiogenesis and bioenergetics. [PDF]
Background and PurposeDuring angiogenesis, quiescent endothelial cells (ECs) are activated by various stimuli to form new blood vessels from pre‐existing ones in physiological and pathological conditions. Many research groups have shown that hydrogen sulfide (H2S), the newest member of the gasotransmitter family, acts as a proangiogenic factor. To date,
Abdollahi Govar A +11 more
europepmc +6 more sources
Inhibition of the 3-mercaptopyruvate sulfurtransferase-hydrogen sulfide system promotes cellular lipid accumulation. [PDF]
Abstract H2S is generated in the adipose tissue by cystathionine γ-lyase, cystathionine β-synthase, and 3-mercaptopyruvate sulfurtransferase (3-MST). H2S plays multiple roles in the regulation of various metabolic processes, including insulin resistance. H2S biosynthesis also occurs in adipocytes.
Casili G +5 more
europepmc +3 more sources

