Disease relevance of cysteate

• On the other hand, L-cysteic acid, L-alanosine, and N-phosphonacetyl-L-aspartic acid were shown to be effective inhibitors of sodium-dependent uptake in Hepatoma 5123C cells [1].
• Cysteic acid did not support weight gain [2].
• Growth with cysteate also restores bead movement and phage sensitivity [3].
• Desulfitobacterium hafniense, however, grew with both isethionate and cysteate in the presence of molybdate [4].
• The effects of a series of gliotoxic amino acids (L-alpha-aminoadipate, L-serine-O-sulphate, D-aspartate and L-cysteate) on metabolism of [1-13C]glucose were examined in C6 glioma cells using 13C nuclear magnetic resonance (NMR) spectroscopy [5].

High impact information on cysteate

• Therefore, cell-free exposure to pervanadate causes cysteine to cysteic acid oxidation of Ran and several other proteins and Ran-K8/K18 association [6].
• After acid hydrolysis, the proportions of labeled serine and alanine (or cysteic acid) were determined by high performance liquid chromatography, and the results were compared with those obtained for the completed proteoglycan molecules isolated from the same cultures [7].
• By amino acid analysis, sickle protein 4.1 was found to contain less methionine and tyrosine than did the normal protein and contained approximately 1 mol% cysteic acid, whereas the normal protein did not contain any cysteic acid [8].
• We conclude that protonation of the mediating ASC system, possibly substrate-assisted, rather than od the free anionic amino acid, converts the system from function for various short chained amino acids to function for aspartate, cysteine sulfinate, and cysteate [9].
• Titration of elongation factor G (EF-G) with the thiol reagents 5,5'-dithiobis(2-nitrobenzoate) (DNTB), p-hydroxymercuribenzoate (HMB), and N-ethylmaleimide and analysis of cysteic acid after performic acid oxidation revealed a total of four sulfhydryl groups per EF-G molecule [10].

Chemical compound and disease context of cysteate

• Compared to a suboptimal (25% of maximum) level of L-methionine alone, supplements to this level L-methionine by N-acetyl-L-cysteine produced a weight gain of 214%; L-cysteine, 178%; L-cysteic acid, 154%; DL- + meso-lanthionine, 127%; L-cysteine sulfinic acid, 113%; D-cysteine, 76%; and S-methyl-L-cysteine, 13% [11].
• Cysteine is not an obligatory intermediate in the biosynthesis of cysteate by Cytophaga johnsonae [12].
• The enhancing effect of cystine on oxidative injury of E. coli cells appears to be directly mediated by the amino acid and in fact cysteic acid, the most likely oxidation product, had no effect on the killing of bacterial cells elicited by hydrogen peroxide [13].
• Paracoccus pantotrophus NKNCYSA utilizes (R)-cysteate (2-amino-3-sulfopropionate) as a sole source of carbon and energy for growth, with either nitrate or molecular oxygen as terminal electron acceptor, and the specific utilization rate of cysteate is about 2 mkat (kg protein)(-1) [14].
• Dissimilation of cysteate via 3-sulfolactate sulfo-lyase and a sulfate exporter in Paracoccus pantotrophus NKNCYSA [14].

Biological context of cysteate

• These results indicate the existence of an Na+-independent specific binding site for cysteic acid in the synaptic membrane of rat cerebral cortex, which may be different from that for glutamate [15].
• For 39 wk, six groups of four specific-pathogen-free cats each were fed purified diets that provided either 1.25 g taurine or 0, 1.0, 2.0, 10 or 20 g cysteic acid/kg diet [16].
• The stimulation of release by external amino acids followed Michaelis-Menten kinetics; the apparent Km values (in microM) were: 14.65 +/- 0.98 for D-aspartate; 8.00 +/- 1.5 for L-aspartate; 22.31 +/- 1.62 for L-glutamate; 6.76 +/- 0.3 for L-cysteate and 7.89 +/- 1.23 for L-cysteinesulphinate [17].
• The rat hippocampal slice preparation and its electrophysiology were used to assess the toxicity of two sulfur-containing amino acids, L-cysteate (CA) and L-cysteine (CYS) [18].
• The beta-elimination and sulfite addition reaction of these peptidoglycans yielded cysteic acid-containing peptides, and the amino acid sequences of some of them were determined [19].

Anatomical context of cysteate

• Synaptosomes isolated from rat brain accumulated cysteic acid by a high-affinity transport system (Km = 12.3 +/- 2.1 microM; Vmax = 2.5 nmol mg protein-1 min-1) [20].
• Depolarization, with either high [K+] or veratridine, of the plasma membranes of synaptosomes loaded with cysteate caused parallel release of cysteate, aspartate, and glutamate [20].
• No adverse gross clinical signs were observed in cats fed any diets containing cysteic acid; minor histopathologic changes of the pancreas and thyroid were found in three of four cats fed 20 g cysteic acid/kg diet [16].
• Quisqualate, L-aspartate, DL-homocysteate, and L-cysteate increased both astrocytic 3H-OMG space and 3H-taurine release from cultured astrocytes, while kainate (1 mM) stimulated 3H-taurine release without affecting astrocytic volume [21].
• We now report a positive modulatory action of the sulphur-containing amino acids (SCAAs), L-cysteic acid (CA) and L-cysteine sulphinic acid (CSA), at presynaptic group I mGlu receptors, specifically of the mGlu5 subtype, acting to enhance synaptic glutamate release from the rat forebrain in vitro [22].

Associations of cysteate with other chemical compounds

• Addition of extrasynaptosomal cysteate, aspartate, or cysteine sulfinate to synaptosomes loaded with [35S]cysteate induced rapid efflux of the cysteate [20].
• Transport of cysteate by synaptosomes isolated from rat brain: evidence that it utilizes the same transporter as aspartate, glutamate, and cysteine sulfinate [20].
• The suitability of micellar electrokinetic chromatography (MEKC) coupled with diode array or laser-induced fluorescence (LIF) detection to analyze the four sulfur-containing excitatory amino acids (SEAA), homocysteine sulfinic acid (HCSA), homocysteic acid (HCA), cysteine sulfinic acid (CSA), and cysteic acid (CA) was investigated [23].
• After an overnight hydrolysis, urine samples dried and reconstituted with the internal standard cysteic acid (in sodium hydrogen carbonate, pH 9.3) were derivatized with N,N-diethyl-2,4-dinitro-5-fluoroaniline (FDNDEA) at 100 degrees C for 20 min [24].
• Molecular modeling showed that the heparin-binding domain of FGF-1 includes cysteine-131 and that cysteine-131, upon oxidation to cysteic acid during the iodination procedures, would interact with lysine-126 and lysine-132 [25].

Gene context of cysteate

• Surprisingly, cysteic acid was the most potent stimulant of SRIF release, with a minimal effective dose of 0.1 microM [26].
• 5. However, lowering the assay pH to 5.5 significantly enhanced the interaction of the ASCT1 carrier with anionic amino acids such as cysteate, in a pH-dependent manner [27].
• Amino acid analysis of performic acid-oxidized MSA revealed 2--3 cysteic acid residues, and reduction and alkylation resulted in loss of biologic residues, and reduction and alkylation resulted in loss of biologic activity [28].
• Amino acid composition analysis revealed that cysteic acid was generated upon Fe2+/ascorbate addition to PEPCK [29].
• In fact, direct incubation of bovine serum albumin (BSA) with peroxodisulfate and periodate barely alters the isoelectric point (pI) and does not produce any cysteic acid [30].

Analytical, diagnostic and therapeutic context of cysteate

• The dipeptide was recovered as cysteic acid or cysteic acid oxime and detected by HPLC and MALDI-TOF mass spectrometry [31].
• A sensitive and rapid assay method method for cysteic acid decarboxylase was develped which combined the selectivity of ion exchange resin (a complete retention of the substrate, cysteic acid, and exclusion of the product, taurine) with the speed of a vacuum filtration [32].

References