Modification of liver cytosol enzyme activities promoted in vitro by reduced sulfur species generated from cystine with γ-cystathionase

Ogasawara, Yuki; Suzuki, Toshihiro; Ishii, Kazuyuki; Tanabe, Shinzo

doi:10.1016/s0304-4165(96)00072-4

Cited by 14 publications

(6 citation statements)

References 35 publications

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“…1. Moreover, we found that rat liver cytosolic CSE catalyzed the generation of bound sulfur in the presence of cystine or cysteine [9]. In addition, in vitro modification of sulfhydryl-dependent enzymes was found to occur as a result of their interaction with bound sulfur, which had high reactivity and relative specificity for thiol residues [9].…”

Section: Introductionmentioning

confidence: 90%

“…Moreover, we found that rat liver cytosolic CSE catalyzed the generation of bound sulfur in the presence of cystine or cysteine [9]. In addition, in vitro modification of sulfhydryl-dependent enzymes was found to occur as a result of their interaction with bound sulfur, which had high reactivity and relative specificity for thiol residues [9]. Although physiologically active sulfur species (bound sulfur) have long been recognized in living organisms [8,10,11], their biological function remains poorly understood so far.…”

Section: Introductionmentioning

confidence: 99%

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Polysulfide exerts a protective effect against cytotoxicity caused by t‐buthylhydroperoxide through Nrf2 signaling in neuroblastoma cells

et al. 2013

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a b s t r a c tPolysulfide is a bound sulfur species derived from endogenous H 2 S. When mouse neuroblastoma, Neuro2A cells were exposed to tert-butyl hydroperoxide after treatment with polysulfide, a significant decline in cell toxicity was observed. Rapid uptake of polysulfides induced translocation of Nrf2 into the nucleus, resulting in acceleration of GSH synthesis and HO-1 expression. We demonstrated that polysulfide reversibly modified Keap1 to form oxidized dimers and induced the translocation of Nrf2. Moreover, polysulfide treatment accelerated Akt phosphorylation, which is a known pathway of Nrf2 phosphorylation. Thus, polysulfide may mediate the activation of Nrf2 signaling, thereby exerting protective effects against oxidative damage in Neuro2A cells.

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Section: Introductionmentioning

confidence: 90%

Section: Introductionmentioning

confidence: 99%

Polysulfide exerts a protective effect against cytotoxicity caused by t‐buthylhydroperoxide through Nrf2 signaling in neuroblastoma cells

et al. 2013

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“…Sulfuration of erythrocyte enzymes via exposure to a hydropersulfide generating system led to the inhibition of numerous enzymes [54]. Similarly, liver enzymes treated with CSE/cystine (a system that generates Cys-SSH) were also found to be either inhibited or unaffected [55]. However, hydropersulfide formation in the protein parkin has been reported to enhance its catalytic activity, possibly leading to a protection against the development of Parkinson's disease [56].…”

Section: What Cellular Conditions Are Conducive To Hydropersulfide Fomentioning

confidence: 99%

Biological hydropersulfides and related polysulfides – a new concept and perspective in redox biology

et al. 2018

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The chemical biology of thiols (RSH, e.g., cysteine and cysteine‐containing proteins/peptides) has been a topic of extreme interest for many decades due to their reported roles in protein structure/folding, redox signaling, metal ligation, cellular protection, and enzymology. While many of the studies on thiol/sulfur biochemistry have focused on thiols, relatively ignored have been hydropersulfides (RSSH) and higher order polysulfur species (RSSnH, RSSnR, n > 1). Recent and provocative work has alluded to the prevalence and likely physiological importance of RSSH and related RSSnH. RSSH of cysteine (Cys‐SSH) has been found to be prevalent in mammalian systems along with Cys‐SSH‐containing proteins. The RSSH functionality has not been examined to the extent of other biologically relevant sulfur derivatives (e.g., sulfenic acids, disulfides, etc.), whose roles in cell signaling are strongly indicated. The recent finding of Cys‐SSH biosynthesis and translational incorporation into proteins is an unequivocal indication of its fundamental importance and necessitates a more profound look into the physiology of RSSH. In this Review, we discuss the currently reported chemical biology of RSSH (and related species) as a prelude to discussing their possible physiological roles.

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“…We have now examined this possibility in an animal model of pancreatitis. To this end, we have identified H 2 S synthesizing enzyme activity and CSE (mRNA signal) in rat pancreatic homogenates and examined the effect of DL-propargylglycine (PAG), an irreversible inhibitor of CSE (1,(13)(14)(15)(16)(17)(18) on the development of pancreatitis and the subsequent lung injury in this model.…”

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confidence: 99%

Role of hydrogen sulfide in acute pancreatitis and associated lung injury

et al. 2005

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Hydrogen sulfide (H2S) is a naturally occurring gas with potent vasodilator activity. Cystathionine-gamma-lyase (CSE) and cystathionine-beta-synthase (CBS) utilize L-cysteine as substrate to form H2S. Of these two enzymes, cystathionine-gamma-lyase (CSE) is believed to be the key enzyme that forms H2S in the cardiovascular system. Whilst H2S has been reported to relax precontracted rat arteries in vitro and to lower blood pressure in the rat, its effect in an inflammatory condition such as acute pancreatitis has not previously been reported. In this paper, we report the presence of H2S synthesizing enzyme activity and CSE (as determined by mRNA signal) in the pancreas. Also, prophylactic, as well as therapeutic, treatment with the CSE inhibitor, DL-propargylglycine (PAG), significantly reduced the severity of caerulein-induced pancreatitis and associated lung injury, as determined by 1) hyperamylasemia [plasma amylase (U/L) (control, 1204+/-59); prophylactic treatment: placebo, 10635+/-305; PAG, 7904+/-495; therapeutic treatment: placebo, 10427+/-470; PAG, 7811+/-428; P<0.05 PAG c.f. placebo; n=24 animals in each group]; 2) neutrophil sequestration in the pancreas [pancreatic myeloperoxidase oxidase (MPO) activity (fold increase over control) (prophylactic treatment: placebo, 5.78+/-0.63; PAG, 2.97+/-0.39; therapeutic treatment: placebo, 5.48+/-0.52; PAG, 3.03+/-0.47; P<0.05 PAG c.f. placebo; n=24 animals in each group)]; 3) pancreatic acinar cell injury/necrosis; 4) lung MPO activity (fold increase over control) [prophylactic treatment: placebo, 1.99+/-0.16; PAG, 1.34+/-0.14; therapeutic treatment: placebo, 2.03+/-0.12; PAG, 1.41+/-0.97; P<0.05 PAG c.f. placebo; n=24 animals in each group]; and 5) histological evidence of lung injury. These effects of CSE blockade suggest an important proinflammatory role of H2S in regulating the severity of pancreatitis and associated lung injury and raise the possibility that H2S may exert similar activity in other forms of inflammation.

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Modification of liver cytosol enzyme activities promoted in vitro by reduced sulfur species generated from cystine with γ-cystathionase

Cited by 14 publications

References 35 publications

Polysulfide exerts a protective effect against cytotoxicity caused by t‐buthylhydroperoxide through Nrf2 signaling in neuroblastoma cells

Polysulfide exerts a protective effect against cytotoxicity caused by t‐buthylhydroperoxide through Nrf2 signaling in neuroblastoma cells

Biological hydropersulfides and related polysulfides – a new concept and perspective in redox biology

Role of hydrogen sulfide in acute pancreatitis and associated lung injury

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