Effect of bathocuproine disulfonate, a copper chelator, on cyst(e)ine metabolism by freshly isolated rat hepatocytes.

Coloso, Relicardo M.; Drake, Marie R.; Stipanuk, Martha H.

doi:10.1152/ajpendo.1990.259.3.e443

Cited by 14 publications

(10 citation statements)

References 27 publications

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“…Treatment of rat enterocytes, renal cortical tubules, or hepatocytes with propargylglycine to inhibit CSE resulted in inhibition of sulfur anion production or overall catabolism of Cys by about 50% (Drake et al 1987; Stipanuk et al 1990; Coloso and Stipanuk 1989). In addition, manipulation of the Cys to cystine ratio in the medium appeared to alter the relative catabolism of Cys by desulfuration versus oxidative, cysteinesulfinate-dependent pathways, with cystine formation favoring desulfuration (Coloso et al 1990). Because rat liver CSE prefers cystine as substrate, this finding can be considered consistent with desulfuration of cyst(e)ine by CSE.…”

Section: Cysteine Undergoes Desulfuration To Hydrogen Sulfide (H2s) Omentioning

confidence: 99%

Dealing with methionine/homocysteine sulfur: cysteine metabolism to taurine and inorganic sulfur

Stipanuk

Ueki

2010

J of Inher Metab Disea

402

294

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Synthesis of cysteine as a product of the transsulfuration pathway can be viewed as part of methionine or homocysteine degradation, with cysteine being the vehicle for sulfur conversion to end products (sulfate, taurine) that can be excreted in the urine. Transsulfuration is regulated by stimulation of cystathionine β-synthase and inhibition of methylene tetrahydrofolate reductase in response to changes in the level of S-adenosylmethionine, and this promotes homocysteine degradation when methionine availability is high. Cysteine is catabolized by several desulfuration reactions that release sulfur in a reduced oxidation state, generating sulfane sulfur or hydrogen sulfide (H2S), which can be further oxidized to sulfate. Cysteine desulfuration is accomplished by alternate reactions catalyzed by cystathionine β-synthase and cystathionine γ-lyase. Cysteine is also catabolized by pathways that require the initial oxidation of the cysteine thiol by cysteine dioxygenase to form cysteinesulfinate. The oxidative pathway leads to production of taurine and sulfate in a ratio of approximately 2:1. Relative metabolism of cysteine by desulfuration versus oxidative pathways is influenced by cysteine dioxygenase activity, which is low in animals fed low-protein diets and high in animals fed excess sulfur amino acids. Thus, desulfuration reactions dominate when cysteine is deficient, whereas oxidative catabolism dominates when cysteine is in excess. In rats consuming a diet with an adequate level of sulfur amino acids, about two thirds of cysteine catabolism occurs by oxidative pathways and one third by desulfuration pathways. Cysteine dioxygenase is robustly regulated in response to cysteine availability and may function to provide a pathway to siphon cysteine to less toxic metabolites than those produced by cysteine desulfuration reactions.

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Section: Cysteine Undergoes Desulfuration To Hydrogen Sulfide (H2s) Omentioning

confidence: 99%

Dealing with methionine/homocysteine sulfur: cysteine metabolism to taurine and inorganic sulfur

Stipanuk

Ueki

2010

J of Inher Metab Disea

402

294

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“…Bathocuproine is used as a metal chelator and displays a relative preference for copper (Coloso et al, 1990). In the presence of 6 through 10 mM bathocuproine, fluorescence was significantly reduced compared with cells incubated with PAP in the absence of bathocuproine (Figure 8).…”

Section: Effects Of Metal Chelatorsmentioning

confidence: 99%

“…Metal chelators phenanthroline (for iron ;Millar et al, 2000) and bathocuproine (for copper; Coloso et al, 1990) were used to determine if Fenton chemistry accounted for production of hydroxyl radicals when cells were incubated with PAP. ROS-associated fluorescence was significantly decreased with either chelator (Figures 7 and 8).…”

Section: Intracellular Events In Pap Toxicitymentioning

confidence: 99%

Contribution of reactive oxygen species to para-aminophenol toxicity in LLC-PK1 cells

Foreman¹,

Tarloff²

2008

Toxicology and Applied Pharmacology

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Para-aminophenol (PAP) causes nephrotoxicity by biochemical mechanisms that have not been fully elucidated. PAP can undergo enzymatic or non-enzymatic oxidation to form reactive intermediates. Using modulators of reactive oxygen species (ROS), the role of ROS in PAP toxicity in LLC-PK 1 cells was investigated. ROS formation was determined using a fluorescein derivative and viability using alamarBlue. Following treatment of cells with PAP, ROS formation occurred prior to loss of cell viability. Several modulators of ROS were used to identify the pathways involved in PAP toxicity. Viability was improved with catalase treatment, while viability was decreased when cells were treated with superoxide dismutase (SOD). Both catalase and SOD exert their effects outside of cells in the incubation medium, since there was no evidence of uptake of these enzymes in LLC-PK 1 cells. In cell-free incubations, hydrogen peroxide (H 2 O 2 ) was produced when 0.5 mM PAP was included in the incubation medium. Further, SOD greatly increased and catalase greatly decreased H 2 O 2 production in these cell-free incubations. These data suggest that H 2 O 2 formed in the incubation medium contributes to loss of viability following PAP treatment. When cells were coincubated with 0.5 mM PAP and tiron, pyruvate, bathocuproine, 1, 10-phenanthroline, or dimethylthiourea (DMTU), ROS formation was decreased. However, there was minimal improvement in cell viability. Paradoxically, DMTU exacerbated PAP-induced loss of viability. These data suggest ROS are generated in cells exposed to PAP but these species are not the predominant cause of cellular injury.

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“…99) Bathocuproine Sulfonate (BCS): BCS is a water-soluble and Cu(I)-specific chelator. 100,101) Although BCS is not used for Cu toxicosis in the clinical setting, it can induce to the Cu deficiency in cultured cells. 35) The effect of BCS on Alzheimer's disease was evaluated.…”

Section: Cu Chelatorsmentioning

confidence: 99%

Research Tools and Techniques for Copper Metabolism in Mammals

Ogra

2011

JOURNAL OF HEALTH SCIENCE

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Copper (Cu) is an essential component of biological redox reactions and its deficiency is fatal to the body. At the same time, Cu is extremely toxic when present in excess. In this regard, several groups of Cu-regulating proteins in the body act to regulate the concentration of Cu within a certain range. However, the overall mechanism underlying the maintenance of Cu homeostasis in the body and cells remains poorly understood. In this review, recent research tools, such as animal models and gene-modified animals, and techniques, such as speciation and imaging of Cu, are highlighted.

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Effect of bathocuproine disulfonate, a copper chelator, on cyst(e)ine metabolism by freshly isolated rat hepatocytes.

Cited by 14 publications

References 27 publications

Dealing with methionine/homocysteine sulfur: cysteine metabolism to taurine and inorganic sulfur

Dealing with methionine/homocysteine sulfur: cysteine metabolism to taurine and inorganic sulfur

Contribution of reactive oxygen species to para-aminophenol toxicity in LLC-PK1 cells

Research Tools and Techniques for Copper Metabolism in Mammals

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