The oxidation of L- and D-cysteine to inorganic sulfate and taurine in the rat

Krijgsheld, Klaas R.; Glazenburg, Eltjo J.; Scholtens, Egbert; Mulder, Gerard J.

doi:10.1016/0304-4165(81)90139-2

Cited by 57 publications

(24 citation statements)

References 9 publications

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“…3). These observations with the previous finding that D-cysteine is easily absorbed through the gastrointestinal tract and enters the blood stream 30 suggest that D-cysteine may be immediately metabolized to produce bound sulfane sulphur in tissues. Both D-cysteine and L-cysteine protect cerebellar neurons from oxidative stress, and further increase cell viability at the higher concentrations (Fig.…”

Section: Article Nature Communications | Doi: 101038/ncomms2371supporting

confidence: 76%

A novel pathway for the production of hydrogen sulfide from D-cysteine in mammalian cells

et al. 2013

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In eukaryotes, hydrogen sulphide acts as a signalling molecule and cytoprotectant. Hydrogen sulphide is known to be produced from L-cysteine by cystathionine b-synthase, cystathionine g-lyase and 3-mercaptopyruvate sulfurtransferase coupled with cysteine aminotransferase. Here we report an additional biosynthetic pathway for the production of hydrogen sulphide from D-cysteine involving 3-mercaptopyruvate sulfurtransferase and D-amino acid oxidase. Unlike the L-cysteine pathway, this D-cysteine-dependent pathway operates predominantly in the cerebellum and the kidney. Our study reveals that administration of D-cysteine protects primary cultures of cerebellar neurons from oxidative stress induced by hydrogen peroxide and attenuates ischaemia-reperfusion injury in the kidney more than L-cysteine. This study presents a novel pathway of hydrogen sulphide production and provides a new therapeutic approach to deliver hydrogen sulphide to specific tissues.

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Section: Article Nature Communications | Doi: 101038/ncomms2371supporting

confidence: 76%

A novel pathway for the production of hydrogen sulfide from D-cysteine in mammalian cells

et al. 2013

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“…Moreover, the addition of sodium sulfate or cysteine to the diet did not result in a rise in the plasma sulfate concentration in the rat (19), although it may restore the sulfate levels to normal in acetaminophen-pretreated rats.…”

Section: Acetaminophen Pretreatment To Decrease Sulfate Availabilitymentioning

confidence: 99%

Sulfation and Glucuronidation as Competing Pathways in the Metabolism of Hydroxamic Acids: The Role of N,O-Sulfonation in Chemical Carcinogenesis of Aromatic Amines

Mulder¹,

Meerman²

1983

Environmental Health Perspectives

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Aromatic amines can be metabolized by N-acetylation and N-hydroxylation to hydroxamic acids; these subsequently are conjugated to form the N,O-sulfonate and N,O-glucuronide conjugates. The N,O-sulfonates are highly labile metabolites that generate reactive intermediates involved in the covalent binding of the parent compound to protein, RNA and DNA, as well as to low molecular compounds like glutathione. This paper discusses methods used to decrease sulfation in vivo, and thereby to enhance the formation of the more stable N,O-glucuronides from N-hydroxy-2-acetylaminofluorene and N-hydroxy-4-acetylamino-4'-fluorobiphenyl. Acetaminophen pretreatment decreases the sulfate availability, but results in many side effects that complicate the analysis of the results. An 8% casein diet reduces the sulfate availability in the rat to approximately 20% of control and thus offers an effective approach to decrease sulfation.The most effective selective inhibition of sulfation is by pentachlorophenol, which very strongly reduces N,O-sulfonation of both hydroxamic acids, and selectively inhibits the formation of DNA adducts that have retained the N-acetyl group. This inhibitor and the related 2,6-dichloro-4-nitrophenol can be employed to study the role of sulfation of hydroxamic acids in initiation and promotion of tumor formation by aromatic amines.

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“…Inorganic sulfate was measured by a turbidimetric method that has been described and modified by Krijgsheld et al (16,17). To 500 PI of (diluted) serum or urine containing 0.1-1.3 mM inorganic sulfate, 2 ml of trichloroacetic acid solution (5% weight/volume) was added, and the mixture was allowed to stand at room temperature for 10 minutes.…”

Section: Methodsmentioning

confidence: 99%

Salicylate‐induced depletion of endogenous inorganic sulfate. Potential role in the suppression of sulfated glycosaminoglycan synthesis in murine articular cartilage

Vries¹,

Berg²,

Putte³

1985

Arthritis & Rheumatism

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Sodium salicylate has been shown to suppress glycosaminoglycan (GAG) synthesis by articular hyaline cartilage in vitro. We investigated the in vivo effect of sodium salicylate on murine patellar cartilage, using incorporation of intraperitoneally administered 35S-sulfate as a measure of sulfated GAG synthesis. Our results indicated that a single dose of sodium salicylate (200 mg/ kg) inhibited in vivo sulfated GAG synthesis by 56%, compared with controls, and had no effect on sulfated GAG breakdown. A striking finding was that sodium sulfate treatment reduced the serum concentration of inorganic sulfate from 1.1 mM to approximately 0.3 mM, and that this serum reduction was associated with a twofold increase in urinary excretion of sulfate. Using anatomically intact patellar cartilage, in vitro studies clearly showed that, in concentrations reached in vivo (21 mM), salicylate suppressed murine chondrocyte GAG synthesis. However, in the presence of serum, the effects of 1 mM salicylate were abolished. We also found that sulfated GAG synthesis was clearly inhibited at low concentrations of sulfate (<0.5 mM). Our data indicate that sodium salicylate can suppress articular chondrocyte sulfated GAG synthesis in vivo, and that this effect may particularly be due to a drug-induced reduction of endogenous sulfate. Several nonsteroidal antiinflammatory drugs (NSAIDs) commonly used in the treatment of arthritis have been shown to provoke suppression of glycosaminoglycan (GAG) synthesis in organ cultures of normal articular cartilage (1-3). Studies have clearly shown that salicylate administration suppresses in vitro GAG synthesis in normal human articular cartilage and that degenerated cartilage is affected even more by this drug (43). In experiments on canine osteoarthritic cartilage (6), an almost complete suppression was observed at salicylate concentrations of 10-3M (14 mg%), a level which is readily achieved in human serum. ~~Because patients with rheumatic diseases often receive long-term treatment with NSAIDs, it is relevant to know whether the suppressive effect of these drugs, as observed in vitro, also occurs in vivo. A deleterious effect of salicylates on articular cartilage after long-term treatment has been shown in studies of animals (7,8). However, the chondrocyte synthetic function of salicylate-treated animals has only been tested ex vivo (7,9), and a direct action of salicylates on in vivo articular GAG synthesis has not been established.Originally, the present study was aimed at investigations of the short-term effect of sodium salicylate on in vivo sulfated GAG synthesis in normal articular cartilage. A preliminary experiment showed that sodium salicylate indeed inhibited 35S-sulfate incorporation in articular cartilage, but the most striking observation was a decrease in the serum content of 35S-sulfate, which paralleled a decrease in the endogenous serum sulfate level (10). With these observations and those of others (ll), who found that the lowering of environmental inorganic sulfate per se may SALI...

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The oxidation of L- and D-cysteine to inorganic sulfate and taurine in the rat

Cited by 57 publications

References 9 publications

A novel pathway for the production of hydrogen sulfide from D-cysteine in mammalian cells

A novel pathway for the production of hydrogen sulfide from D-cysteine in mammalian cells

Sulfation and Glucuronidation as Competing Pathways in the Metabolism of Hydroxamic Acids: The Role of N,O-Sulfonation in Chemical Carcinogenesis of Aromatic Amines

Salicylate‐induced depletion of endogenous inorganic sulfate. Potential role in the suppression of sulfated glycosaminoglycan synthesis in murine articular cartilage

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