In vivo studies of cysteine metabolism. Use of D-cysteinesulfinate, a novel cysteinesulfinate decarboxylase inhibitor, to probe taurine and pyruvate synthesis.

Weinstein, Catherine L.; Haschemeyer, Rudy H.

doi:10.1016/s0021-9258(18)37428-3

Cited by 35 publications

(7 citation statements)

References 43 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Increased synthesis of GSH in the liver is likely to be a main contributor to increased Cys uptake in this tissue (Melchior et al, 2004;Schalinske, 2009). Previous work by others has shown that Tau and SO 4 can be transferred between tissues (Weinstein et al, 1988;Malmezat et al, 1998). In the current study, the presence of 35 S-Tau in tissues that are unable to synthesize Tau confirmed that Tau exchange between the tissues is occurring during the 5-h isotope infusion period.…”

Section: Discussionsupporting

confidence: 85%

“…These results also suggest that ISS modifies the catabolism of Cys in several tissues, specifically increasing the production of Tau and SO 4 in the visceral tissues while decreasing the catabolism of Cys to SO 4 in skeletal muscle and the small intestine. In addition, these results indicate that growing pigs fed a SAA limiting diet, like mice and unlike rats, catabolize Cys primarily to Tau and not to SO 4 (Weinstein et al, 1988).…”

Section: Discussionmentioning

confidence: 77%

“…In previous studies, administration of 13 C-Cys and the appearance of 13 C in expired CO 2 have been used to generate estimates of irreversible Cys loss (Lyons et al, 2001). However, this approach tends to underestimate the irreversible loss of Cys, since it does not account for the accumulation of 13 C in pyruvate and the incomplete recovery of generated 13 CO 2 (Weinstein et al, 1988) . When using 35 S-Cys as the tracer, the rate of catabolism of Cys to Tau and SO 4 is measured directly, providing an alternative and more accurate estimate of irreversible Cys loss.…”

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

Immune system stimulation increases the irreversible loss of cysteine to taurine, but not sulfate, in starter pigs

Rakhshandeh

Lange

Htoo

2020

Journal of Animal Science

View full text Add to dashboard Cite

An isotope tracer study was conducted to evaluate the effects of immune system stimulation (ISS) on the irreversible loss of cysteine (Cys) to taurine (Tau) and sulfate (SO4), as well as glutathione (GSH) synthesis, during the fed state in pigs. We previously have reported that ISS increases plasma Cys flux and the GSH synthesis rate at the tissue and whole-body levels in growing pigs. Thus, the current article presents the data on the irreversible loss of Cys during ISS in pigs. Ten gilts (BW: 7.0 ± 0.12 kg) were feed restricted a sulfur amino acids (SAA) limiting diet and injected twice with either saline (n = 4) or increasing amounts of E. coli lipopolysaccharide (n = 6). The day after the second injection, a 5-h primed continuous intravenous infusion of 35S-Cys was conducted. ISS reduced plasma Cys and total SAA concentrations (16% and 21%, respectively; P < 0.05). However, ISS had no effect on the plasma concentrations of Tau and SO4, nor did it affect the appearance of 35S in plasma Tau, plasma SO4, urinary Tau, or urinary SO4 (P > 0.19). On a whole-body basis and including urinary excretion, ISS increased the appearance of 35S in Tau by 67% (P < 0.05), but tended to decrease the appearance of 35S in SO4 by 22% (P < 0.09). Overall, the current findings indicate that during ISS, decreased plasma SAA concentrations and increased plasma Cys flux are attributed in part to increased rates of Cys conversion to Tau, but not Cys catabolism to SO4. Thus, increased utilization of Cys for the synthesis of immune system metabolites, such as GSH and Tau, is likely the main contributor to increased Cys flux during ISS in pigs. In addition, the irreversible loss of Cys during ISS is small and has a minimal impact on the daily SAA requirements of starter pigs.

show abstract

Section: Discussionsupporting

confidence: 85%

Section: Discussionmentioning

confidence: 77%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Immune system stimulation increases the irreversible loss of cysteine to taurine, but not sulfate, in starter pigs

Rakhshandeh

Lange

Htoo

2020

Journal of Animal Science

View full text Add to dashboard Cite

show abstract

“…The promiscuity of GCLC toward amino acids other than cysteine is not a unique feature of this enzyme and has been shown for many other metabolic enzymes. For example, serine palmitoyl transferase will also metabolize alanine or glycine when serine is limiting (Penno et al, 2010) and glutamate-aspartate aminotransferase will also metabolize cysteine sulfinic acid (Weinstein et al, 1988). In the case of GCLC, this feature may have been selected for during evolution, as the S. cerevisiae homolog (Gsh1p) also has the ability to at least use valine (Sofyanovich et al, 2019).…”

Section: Discussionmentioning

confidence: 99%

Non-canonical Glutamate-Cysteine Ligase Activity Protects against Ferroptosis

et al. 2021

View full text Add to dashboard Cite

show abstract

“…The substrate of CDO, cysteine, is both toxic (1-2 g kg 21 ) and readily oxidizes to form the poorly soluble disulfide, cystine (depending on the pH, concentrations above 250 mg L 21 will cause it to precipitate forming cystine stones). 25 It has been noted that cysteine elicits excitotoxin behavior, acting on the N-methyl-D-aspartate (NMDA) subtype of glutamate receptor. 26 Other researchers postulate that this amino acid contributes to the formation of reactive oxygen species, oxidizing essential molecules, such as the catecholaminergic neurotransmitter dopamine.…”

Section: Biological Significancementioning

confidence: 99%

Cysteine dioxygenase: structure and mechanism

2007

View full text Add to dashboard Cite

Cysteine dioxygenase (CDO) catalyzes the oxidation of cysteine to cysteine sulfinic acid, which is the first major step in cysteine catabolism in mammalian tissues. Crystal structures of mouse, rat, human and bacterial CDO have recently become available and provide significant mechanistic insights. Unlike most non-heme Fe(II) dioxygenases, coordination of the Fe in CDO deviates from the 2-His-1-carboxylate facial triad archetype and instead adopts a His3 facial triad. This change is expected to have an influence on oxygen activation by the catalytic site. The structures also reveal the presence of a cysteinyltyrosine (Tyr157-Cys93) post-translational modification near the active site. Kinetic studies of mutant CDOs reveal that the cysteine residue is less critical than the tyrosine for enzyme activity. Inconsistencies about the details of the active site and the nature of substrate binding exist and are discussed. Herein we review the structural biology along with relevant kinetics studies that have been conducted on CDO for insights into the reaction mechanism of this novel non-heme iron dioxygenase.

show abstract

In vivo studies of cysteine metabolism. Use of D-cysteinesulfinate, a novel cysteinesulfinate decarboxylase inhibitor, to probe taurine and pyruvate synthesis.

Cited by 35 publications

References 43 publications

Immune system stimulation increases the irreversible loss of cysteine to taurine, but not sulfate, in starter pigs

Immune system stimulation increases the irreversible loss of cysteine to taurine, but not sulfate, in starter pigs

Non-canonical Glutamate-Cysteine Ligase Activity Protects against Ferroptosis

Cysteine dioxygenase: structure and mechanism

Contact Info

Product

Resources

About