Thiazolidine-2-carboxylate derivatives formed from glyoxylate and L-cysteine or L-cysteinylglycine as possible physiological substrates for D-aspartate oxidase

Burns, C. L.; Main, D. E.; Buckthal, David J.; Hamilton, Gordon A.

doi:10.1016/0006-291x(84)91388-3

Cited by 37 publications

(8 citation statements)

References 13 publications

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“…Ddo enzymatic activity was first identified before D-enantiomer amino acids were believed to be endogenously synthesized in mammals (Still et al, 1949). Therefore, the D-amino acid oxidizing property of Ddo was considered nonphysiologic, and unsuccessful efforts were made to find possible endogenous functions (Burns et al, 1984). With orders of magnitude D-aspartate elevation in Ddo Ϫ/Ϫ mice, this study clearly demonstrates that Ddo is the endogenous enzyme responsible for metabolizing D-aspartate. Reciprocally high and low tissue concentrations occur for Ddo and D-aspartate, resembling Dao and D-serine (Snyder and Kim, 2000).…”

Section: Discussionmentioning

confidence: 86%

d-Aspartate Regulates Melanocortin Formation and Function: Behavioral Alterations in d-Aspartate Oxidase-Deficient Mice

et al. 2006

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Section: Discussionmentioning

confidence: 86%

d-Aspartate Regulates Melanocortin Formation and Function: Behavioral Alterations in d-Aspartate Oxidase-Deficient Mice

et al. 2006

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“…For example, 2‐oxothiazolidine‐4‐carboxylate was shown to be transported intracellularly and metabolized by 5‐oxo‐ l ‐prolinase, yielding ADP and S‐carboxycysteine, which was then decarboxylated non‐enzymatically to generate cysteine . Similarly, thiazolidine‐2 carboxylate derivatives were identified as substrate for aspartate oxidase . Very recently, Su et al published data on the chemical interaction of thiazolidine structures and reduced glutathione thus providing evidence for a non‐enzymatic mechanism of intracellular cysteine release.…”

Section: Discussionmentioning

confidence: 99%

“…49 Similarly, thiazolidine-2 carboxylate derivatives were identified as substrate for aspartate oxidase. 50 Very recently, Su et al 51 published data on the chemical interaction of thiazolidine structures and reduced glutathione thus providing evidence for a non-enzymatic mechanism of intracellular cysteine release. If we extrapolate to the thiazolidines tested in this study, as supported in Ref.…”

Section: Discussionmentioning

confidence: 99%

Antioxidant effect of thiazolidine molecules in cell culture media improves stability and performance

Kuschelewski

Schnellbaecher

Pering

et al. 2017

Biotechnology Progress

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The ability of cell culture media components to generate reactive species as well as their sensitivity to oxidative degradation, affects the overall stability of media and the behavior of cells cultured in vitro. This study investigates the influence of thiazolidine molecules, formed from the condensation between cysteine and alpha-ketoacids, on the stability of these complex mixtures and on the performance of cell culture processes aiming to produce therapeutically relevant monoclonal antibodies. Results presented in this study indicate that 2-methyl-1,3-thiazolidine-2,4-dicarboxylic acid and 2-(2-carboxyethyl)-1,3-thiazolidine-2,4-dicarboxylic acid, obtained by condensation of cysteine with pyruvate or alpha-ketoglutarate, respectively, are able to stabilize cell culture media formulations, in particular redox sensitive molecules like folic acid, thiamine, l-methionine (met) and l-tryptophan (trp). The use of thiazolidine containing feeds in Chinese hamster ovary fed-batch processes showed prolonged culture duration and increased productivity. This enhanced performance was correlated with lower reactive species generation, extracellularly and intracellularly. Moreover, an anti-oxidative response was triggered via the induction of superoxide dismutase and an increase in the total glutathione pool, the major intracellular antioxidant. In total, the results confirm that cells in vitro are not cultured in an oxidant-free environment, a concept that has to be considered when studying the influence of reactive species in human diseases. Furthermore, this study indicates that thiazolidines are an interesting class of antioxidant molecules, capable of increasing cell culture media stability and process performance. © 2017 American Institute of Chemical Engineers Biotechnol. Prog., 33:759-770, 2017.

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“…D-ASPOX is quite similar to the well-known D-amino acid oxidase (D-AAOX), but both proteins can be separated by differential purification and exhibit major differences in substrate specificity and their response to inhibition (Negri et al, 1987;Hamilton, 1985). Whereas D-AAOX oxidizes neutral or basic D-amino acids, D-ASPOX specifically catalyzes the oxidation of the D-stereoisomers of the acidic amino acids aspartate and glutamate (D'Aniello et al, I993b;Negri et al, 1987;Hamilton, 1985) and also of stereoisomers of certain other acidic amino or heterocyclic iminoacids (Solinas et al, 1986;Hamilton, 1985;Burns et al, 1984). D-ASPOX transfers electrons either to oxygen, producing hydrogen peroxide, or to other terminal electron acceptors (Negri et al, 1987;Dixon and Kenworthy, 1967).…”

Section: Introductionmentioning

confidence: 99%

Light and electron microscopic localization of D-aspartate oxidase in peroxisomes of bovine kidney and liver: an immunocytochemical study.

Zaar

1996

J Histochem Cytochem.

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D-Aspartate oxidase (EC 1.4.3.1; D-ASPOX) specifically oxidizes the D-isomers of dicarboxylic amino acids such as aspartic or glutamic acid. Subcellular fractionation experiments in the past showed its association with peroxisome preparations in kidney cortex and liver. However, no information exists on the in situ localization and distribution of the enzyme in different cell types. We have purified the enzyme from the bovine kidney and raised an antibody against it in rabbits. The monospecificity of the antibody has been confirmed by Western blotting and it does not crossreact with D-amino, acid oxidase. Immunohistochemical localization of the antigen in bovine kidney and liver with the streptavidin-biotin-peroxidase technique revealed a punctate localization in the epithelial cells of proximal nephron tubules, particularly in the straight P-3 segment, as well as in hepatocytes. This is consistent with a localization in peroxisomes. Best results have been obtained with Carnoy-fixed material after paraffin embedding or after fixation with formaldehyde-glutaraldehyde in cryostat sections. Immunoelectron microscopy with protein A-gold confirms the peroxisomal localization of D-ASPOX. Gold particles are distributed over the matrix, suggestive of a peroxisomal matrix enzyme. This is the first report on the localization of D-ASPOX, a little-known peroxisomal enzyme. The techniques described and the antibody prepared will now allow systematic investigation of its tissue distribution.

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Thiazolidine-2-carboxylate derivatives formed from glyoxylate and L-cysteine or L-cysteinylglycine as possible physiological substrates for D-aspartate oxidase

Cited by 37 publications

References 13 publications

d-Aspartate Regulates Melanocortin Formation and Function: Behavioral Alterations in d-Aspartate Oxidase-Deficient Mice

d-Aspartate Regulates Melanocortin Formation and Function: Behavioral Alterations in d-Aspartate Oxidase-Deficient Mice

Antioxidant effect of thiazolidine molecules in cell culture media improves stability and performance

Light and electron microscopic localization of D-aspartate oxidase in peroxisomes of bovine kidney and liver: an immunocytochemical study.

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