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PubMed1971

Structural studies on bovine -crystallin.

The amino acid sequences around the cysteine residues in the lens protein, gamma-crystallin, were studied. Fraction II of the gamma-crystallin from calf lens (Björk, 1964) was used. The protein was oxidized with performic acid and then hydrolysed with trypsin. Six peptides containing cysteic acid were isolated. One of the peptides contained three residues of cysteic acid and the others contained one residue of cysteic acid. We conclude that there are eight unique residues of cysteic acid in the oxidized protein. Amino acid analysis suggests that there are also eight residues of cysteic acid in the molecule, which thus contains only one polypeptide chain.

Amino Acid Sequence↗
PubMed1997

Penicillin biosynthesis: intermediates of biosynthesis of delta-L-alpha-aminoadipyl-L-cysteinyl-D-valine formed by ACV synthetase from Acremonium chrysogenum.

The tripeptide delta-L-alpha-aminoadipyl-L-cysteinyl-D-valine (LLD-ACV) is synthesised by the multifunctional enzyme ACV synthetase integrating four steps of the penicillin and cephalosporin biosynthetic pathway. Peptide synthesis follows the thiotemplate mechanism from intermediates bound as thioesters to the enzyme. The formation of delta-(L-alpha-aminoadipyl)-L-cysteinyl-thioester in the absence of L-valine was shown by isolation of the enzyme-substrate complex and cleavage of the covalently bound intermediate with performic acid. The dipeptide was recovered as cysteic acid or cysteic acid oxime and detected by HPLC and MALDI-TOF mass spectrometry. We conclude that the first peptide bond is formed between delta-carboxyl of L-aminoadipic acid and L-cysteine, followed by addition of the dipeptidyl intermediate to L-valine.

Acremonium↗
PubMed1982

Sagittal cerebellar microbands of taurine neurons: immunocytochemical demonstration by using antibodies against the taurine-synthesizing enzyme cysteine sulfinic acid decarboxylase.

Taurine neurons in the cerebellum of rabbit, rat, and mouse were localized at the light microscope level by using polyclonal antibodies against cysteine sulfinic acid decarboxylase (CSADCase; EC 4.1.1.29), the enzyme responsible for the conversion of cysteine sulfinic acid to hypotaurine and of cysteic acid to taurine. The indirect peroxidase-antiperoxidase method was used on Vibratome sections and on serial sections of paraffin-embedded tissue. Intensification of CSADCase immunoreactivity was achieved by pretreatment of the animal with L-cysteine or L-cysteic acid intravenously 1-2 hr prior to perfusion. A combination of L-cysteic acid and demecolcine, which retards axoplasmic flow, was most effective in maximizing CSADCase immunoreactivity. Although these treatments intensified immunoreactivity in neurons, no more cells were reactive than in untreated controls. L-Glutamic acid did not increase CSADCase immunoreactivity but did increase immunoreactivity with antibodies against L-glutamic acid decarboxylase (GAD; EC 4.1.1.15), the synthetic enzyme for gamma-aminobutyric acid. Specificity was established by negative results obtained with various control incubations including the use of CSADCase antiserum preabsorbed with the antigen. Taurine neurons of the cerebellar cortex are arranged in sagittal microbands, defined by intensely CSADCase-reactive Purkinje neurons and their axons and dendrites, together with stellate, basket, and Golgi cells and their processes. In the vermis there is a narrow midline band, flanked laterally by three wider bands on either side, each separated from the next by an unreactive zone. Although the zonal borders are sharp, the interzonal areas contain some CSADCase-immunoreactive axons but no cell bodies. The seven vermal bands are best observed in the anterior lobe. Others exist in the lateral hemispheres. The paraflocculus and flocculus contain numerous intensely immunoreactive neurons, and banding is difficult to discern. Lobule X of the vermis is also heavily endowed with taurine neurons. Numerous large and medium-sized deep cerebellar and vestibular nuclei are also immunoreactive. These observations indicate that cerebellar neurons are chemically heterogeneous but that neurons of similar chemical signature in the cerebellar cortex are organized into sagittal microbands. This corroborates our earlier evidence that Purkinje cells containing motilin and those containing both motilin and gamma-aminobutyric acid are also arranged in vermal sagittal microbands. The midline vermal band contains Purkinje neurons with multiple neuroactive substances-taurine, gamma-aminobutyric acid, and motilin. It remains to be determined how this chemical zonation in the cerebellar cortex relates to the banded afferent innervation from spinal, vestibular, reticular, and olivary sources.

Animals↗
PubMed1966

Location of disulphide bridges by diagonal paper electrophoresis. The disulphide bridges of bovine chymotrypsinogen A.

1. A new method is described for ;fingerprinting' cysteic acid peptides derived from the disulphide bridges of proteins. Cystine peptides are separated by paper electrophoresis and oxidized on paper by performic acid vapour. Electrophoresis at right angles to the first direction produces parallel groups of cysteic acid peptides lying off a diagonal. This ;fingerprint' reveals the way in which the cysteic acid peptides were originally joined in the protein. 2. The method allows a very easy selective purification of cysteic acid peptides. 3. By applying this method to bovine chymotrypsinogen A, we found that the half-cystine residues were linked 1-122, 42-58, 136-201, 168-182 and 191-220.

Amino Acid Sequence↗
PubMed2005

Human Ran cysteine 112 oxidation by pervanadate regulates its binding to keratins.

We used a proteomic approach to identify proteins that associate with keratins 8 or 18 (K8/K18) in a pervanadate-dependent manner. Pervanadate triggers Ran-K8/K18 binding and a gel-migration-shift of Ran from 25 to 27 kDa, which does not occur upon exposure to H2O2 or vanadate or if pervanadate is excluded during cell solubilization. Generation of 27-kDa Ran is not related to hyperphosphorylation, is heat-insensitive, but occurs upon conversion of Ran cysteines to cysteic acid. The pervanadate-mediated Ran cysteine --> cysteic acid oxidation and its related gel migration shift affects other proteins including actin. Mutation of the three Ran cysteines (Cys-85, -112, and -120) showed that Ran Cys-112 oxidation generates 27-kDa Ran and accounts for its keratin binding. Proteasome inhibition accentuates Ran-keratin binding after cell exposure to pervanadate. Therefore, cell-free exposure to pervanadate causes cysteine to cysteic acid oxidation of Ran and several other proteins and Ran-K8/K18 association. In cells, stabilization of oxidized Ran by proteasome inhibition promotes Ran-keratin interaction. Keratin sequestration of oxidized Ran may provide a back-up protective mechanism in some cases of oxidative injury.

Actins↗
PubMedDate not supplied

Taurine, analogues and ethanol elicited responses.

The effect of taurine, of some of its precursors and major metabolic products on spontaneous locomotor activity were studied in mice. The effect of taurine and some analogues on certain ethanol-mediated responses were observed. Administration of taurine, 50 mg/kg, IP, did not significantly alter motility in experimental animals compared to controls. Behavioral depression was evident subsequent to injection of cysteine hydrochloride or taurocholic acid (50 mg/kg). Administration of taurocholic acid, 50 mg/kg, IP, 30 min prior to a narcotic dose of ethanol, 5 g/kg, IP, reduced the time required for the onset of ethanol-narcosis. Pretreatment with cysteic acid, 50 mg/kg, IP, prolonged ethanol-produced narcosis. Treatment with cysteic acid 30 min prior to ethanol, 2.5 g/kg, IP, was found to decrease whole blood ethanol concentration as compared to the respective controls without a concomitant changes in brain ethanol levels. Administration of taurocholic acid, 100 mg/kg, IP, decreased the intake of an ethanol solution in rats preferring 5% ethanol solution over water as the drinking fluid of choice. None of the compounds tested altered endogenous specific activity of mouse liver alcohol dehydrogenase when given once daily (50 mg/kg, IP) for 10 consecutive days. The results suggest that both taurocholic acid and cysteic acid exert additive action to some ethanol-elicited responses studied.

Alcohol Drinking↗
PubMed1981

Effect of bile acid derivatives on taurine biosynthesis and extracellular slime production in encapsulated Staphylococcus aureus S-7.

Various bile acids were added to cultures of encapsulated strains of Staphylococcus aureus growing in serum-soft agar medium of brain heart infusion broth. We examined effects of these compounds on cellular characteristics such as growth type, cell volume index, clumping factor reaction, slime yield, taurine content, and L-(--)-cysteic acid decarboxylase activity. Upon addition to the medium of either taurochenodeoxycholic acid, taurocholic acid (25 to 50 microgram/ml), or cholic acid (10 to 25 microgram/ml), the colonial morphology of taurine-positive cells (strain S-7) was altered from the diffuse to the compact type in serum-soft agar. Also, the titer of the clumping factor reaction increased, while the cell volume index and slime yield were markedly decreased. Tauro-bile acids, including taurocholic acid, taurochenodeoxycholic acid, taurodehydrocholic acid, and taurodeoxycholic acid (50 microgram/ml) inhibited the synthesis of taurine and resulted in decreased L-(--)-cysteic acid decarboxylase activity. Among all of the derivatives cholic acid itself was found to inhibit slime production and L-(--)-cysteic acid decarboxylase activity to the greatest extent. Glyco-bile acid derivatives and taurolicholic acid (50 to 100 microgram/ml) had no effect on L-(--)-cysteic acid decarboxylase activity. Compounds such as glycodeoxycholic acid (50 to 100 microgram/ml) had no effect upon any of the cellular characteristics tested. No effect was observed upon addition of any of these compounds to cultures of the taurine-negative strain (T-26-B). We did find a correlation between the inhibition of taurine biosynthesis and decreased slime production. Electron micrographs indicated that this encapsulated strain was converted to an unencapsulated state in the presence of bile acids.

Bile Acids and Salts↗
PubMed1993

Cytotoxic actions and effects on intracellular Ca2+ and cGMP concentrations of sulphur-containing excitatory amino acids in cultured cerebral cortical neurons.

Effects of the sulphur-containing acidic amino acids (SAAs) cysteic acid (CA), homocysteic acid (HCA), cysteine sulphinic acid (CSA), homocysteine sulphinic acid (HCSA), and S-sulphocysteine (SC) on intracellular concentrations of Ca2+ ([Ca2+]i) and cGMP ([cGMP]i) as well as their cytotoxic actions were investigated in cultured cerebral cortical neurons. The glutamate receptor subtype selective antagonists APV (D-(-)-2-amino-5-phosphonopentanoate) acting on N-methyl-D-aspartate (NMDA) receptors and DNQX (6,7-dinitroquinoxaline-2,3-dione) acting on non-NMDA receptors were employed to obtain information about the involvement of glutamate receptor subtypes in these actions of the SAAs. It was found that all SAAs exerted a cytotoxic action on the neurons. The ED50 values for CSA, CA, HCSA, and HCA were around 30 to 50 microM and that for SC was about 150 microM. The glutamate transport blocker L-aspartate-beta-hydroxamate increased the efficacy of CSA and CA but had no effect on the cytotoxic actions of the remaining SAAs. In case of CA, HCA, and SC the cytotoxicity could be prevented by APV alone and for HCSA, DNQX could block the toxic action. DNQX reduced the toxicity of HCA somewhat but the presence of APV was required for complete protection. CSA toxicity could only be blocked by the combination of APV and DNQX. All SAAs induced an increase in [cGMP]i and [Ca2+]i and with regard to [Ca2+]i SC was the most potent and CA the least potent SAA. The effect of all SAAs on [cGMP]i could be blocked by APV alone whereas DNQX had no effect except in the case of HCSA where the response was blocked completely and HCA where the response was inhibited by 75%.(ABSTRACT TRUNCATED AT 250 WORDS)

2-Amino-5-phosphonovalerate↗
PubMed1994

High-performance liquid chromatography method for the determination of protein-glutathione mixed disulfide.

We have developed an efficient and sensitive method for the quantification of picomole quantities of protein-glutathione and protein-cysteine mixed disulfides in ocular lens. Performic acid oxidation releases glutathione and cysteine from the protein-mixed disulfides as glutathione sulfonic acid and cysteic acid, respectively. The sulfonic acids are derivatized with phenylisothiocyanate, and the phenylthiocarbamyl derivatives are separated by HPLC using a reversed-phase ODS column, equilibrated with 0.14 M sodium acetate, containing 0.1% triethylamine and 6% acetonitrile.

Animals↗
PubMed1992

Taurine receptor: kinetic analysis and pharmacological studies.

A new procedure for the preparation of the taurine receptor from mammalian brain is described. The taurine receptor thus prepared shows a Kd of 92 nM, Bmax of 6.0 pmol/mg protein and Hill coefficient of 0.90 suggesting a single site model for the binding of 3H-taurine to the receptor. The binding of 3H-taurine to the receptor is highly specific and is not affected by agonists and antagonists of other receptors such as glutamate, quisqualic acid, kainate and NMDA for the glutamate receptor; glycine and strychnine for the glycine receptor; FNZP for the benzodiazepine receptor; picrotoxin and bicuculline for the GABAB receptor. However, analogues of taurine (e.g., homotaurine and hypotaurine) are potent inhibitors inhibiting more than 50% of 3H-taurine binding at 0.1 microM. Taurine receptor binding is not significantly affected by monovalent cations (e.g., Na+, K+, Li+ and NH4+) at 1 mM or divalent cations (e.g., Mg2+, Ca2+, Ba2+ and Mn2+) at 0.1 mM. However, the binding was completely abolished by Co2+, Zn2+ and Hg2+ at 0.1 mM, suggesting the presence of free sulfhydryl groups near or at the ligand binding site. Among the amino acids tested, cysteic acid was the most potent inhibitor, followed by beta-alanine, valine, tyrosine and cysteine inhibiting 3H-taurine to an extent of 84, 66, 63, 62, and 58% of 1 mM, respectively. Nucleotides and second messengers (e.g., ATP, ADP, cAMP, GTP, cGMP and diacyl glycerol) do not inhibit 3H-taurine binding significantly at 0.1 mM. From above studies, it seems that the taurine receptor is not up- or down-regulated by ions or second messengers at the taurine binding site. Whether the taurine receptor is coupled to a G-protein mediated second messenger system is currently under investigation.

Amino Acids↗
PubMedDate not supplied

Irreversible thiol oxidation in carbonic anhydrase III: protection by S-glutathiolation and detection in aging rats.

Proteins with reactive sulfhydryls are central to many important metabolic reactions and also contribute to a variety of signal transduction systems. In this report, we examine the mechanisms of oxidative damage to the two reactive sulfhydryls of carbonic anhydrase III. Hydrogen peroxide (H2O2), peroxy radicals, or hypochlorous acid (HOCl) produced irreversibly oxidized forms, primarily cysteine sulfinic acid or cysteic acid, of carbonic anhydrase III if glutathione (GSH) was not present. When GSH was approximately equimolar to protein thiols, irreversible oxidation was prevented. H202 and peroxyl radicals both generated S-glutathiolated carbonic anhydrase III via partially oxidized protein sulfhydryl intermediates, while HOCl did not cause S-glutathiolation. Thus, oxidative damage from H202 or AAPH was prevented by protein S-glutathiolation, while a direct reaction between GSH and oxidant likely prevents HOCl-mediated protein damage. In cultured rat hepatocytes, carbonic anhydrase III was rapidly S-glutathiolated by menadione. When hepatocyte glutathione was depleted, menadione instead caused irreversible oxidation. We hypothesized that normal depletion of glutathione in aged animals might also lead to an increase in irreversible oxidation. Indeed, both total protein extracts and carbonic anhydrase III contained significantly more cysteine sulfinic acid in older rats compared to young animals. These experiments show that, in the absence of sufficient GSH, oxidation reactions lead to irreversible protein sulfhydryl damage in purified proteins, cellular systems, and whole animals.

Aging↗
PubMed1988

A new antifungal antibiotic, cystargin: fermentation, isolation, and characterization.

A new sulfur-containing peptide antifungal antibiotic, cystargin, was isolated from the fermentation broth of a new species of genus Kitasatosporia, designated as Kitasatosporia cystarginea. On acid hydrolysis, cystargin (C60H77N19O17S6) gave equimolar glycine, proline, aspartic acid and arginine. By performic acid oxidation, cysteic acid was detected after hydrolysis. It showed a growth inhibitory activity against various phytopathogenic fungi and inhibition of beta-1,3-glucan synthetase from Saccharomyces cerevisiae.

Actinomycetales↗
PubMed1998

[Effects of excitatory sulfur amino acids on glutamate transport in synaptosomes isolated from the rat cerebral cortex].

Transport of glutamate, the disturbance of which has been implicated in amyotrophic lateral sclerosis (ALS), may be influenced by various substances. Excitatory sulfur amino acids (SAAs) could be increased in ALS, because the elevation of taurine, the final product of the metabolic pathway of SAAs, has been reported in this intractable disease. I examined effects of excitatory SAAs on the transport of glutamate in synaptosomes. Synaptosome fractions were prepared by discontinuous density-gradient centrifugation from the rat cerebral cortex, and were incubated at 35 degrees C with varying concentrations of L-[3H] glutamate in the absence or presence of excitatory SAAs; cysteine sulfinic acid (CSA), cysteic acid (CA), homocysteine sulfinic acid (HCSA), homocysteic acid (HCA) and S-sulfocysteine (SC). Kinetic characterization of uptake confirmed the high-affinity nature of the transport system, the Michaelis constant (Km) for glutamate uptake being 10 microM. The nature of inhibition was competitive. Potent inhibition of transport was exhibited by CSA and CA, whereas substantially weaker inhibitory effects were exhibited by HCSA, and almost no effects by HCA or SC. Inhibition by excitatory SAAs, especially CSA and CA of the high-affinity glutamate transporter may be involved in the pathogenesis of ALS.

ATP-Binding Cassette Transporters↗
PubMed1989

Cysteine-induced changes of low molecular sulfhydryl/disulfide ratio in rat lymphoid cells.

Changes in total protein and nonprotein sulfhydryl content, cell membrane sulfhydryls and mitogen response were examined after incubation of rat lymphoid cells with L-cysteine. Distribution of 35S L-cysteine within the metabolic pool of low molecular thiols and protein thiols was determined by quantitative analysis of metabolites of the oxidative taurine pathway, glutathione, mixed disulfides and protein-associated radioactivity. Significant, incubation time-dependent increase of [3H] thymidine, [3H] uridine and [14C] leucine incorporation was observed in cysteine-preincubated, PHA-stimulated lymph node cells. Subsequent inhibition of PHA-response of lymphocytes and a marked increase of intracellular content of free (reduced form) cysteine was observed as a result of constant supply of cysteine into cells from the incubation medium. Maintenance of [35S] L-cysteine, transported into thymocytes within 3 hours, mainly in -SH form, was dependent on the constant presence of cysteine in the medium and slightly dependent on its concentration (0.01-10 mM). Cysteine catabolites of the oxidative taurine pathway, i.e. taurine, cysteinesulfinic acid and cysteic acid, as well as glutathione, low molecular mixed disulfides, protein cysteine mixed disulfides and proteinincorporated cysteine increased proportionally to the time of cysteine uptake but not to the increasing amounts of intracellular free cysteine. These results support the hypothesis of changed-SH/SS equilibrium of low molecular thiols due to the presence of high amounts of free cysteine, reflecting cell metabolism and functions.

Animals↗
PubMed1988

[Gas chromatographic determination of amino acids with nitrogen-selective detection].

Heptafluorobutyryl isobutyl ester derivatives of amino acids were determined, using the thermionic nitrogen-phosphorus detector. The linearity of the detector (more than 5 decades), allows determinations above 0.3 pMol and 110 nMol, without the need for further dilution. Due to the specificity of the detector, no fractionation or other pretreatment of the samples prior to hydrolysis were necessary. The separation of the amino acid derivatives ranges from fair to excellent when comparing separations on packed columns with those on capillary columns. On the capillary analyser, however, only a few runs could be performed, since it was not available for a long enough period of time. The reproducibility of the determination was high in the monobasic amino acids, with a coefficient of variation (c.v.) of less than 3, but somewhat worse in arginine, histidine, cystine and minor components. Histidine needs an on-column acylation by the co-injection of the hydrolysate with acetic anhydride. The amino acids tryptophan, cysteic acid and methionine sulphone have not been investigated until now. A disadvantage of the procedure compared with other analytical methods is the rather complicated derivatisation, which until now, has not been easily automated. Finally, the practicability of the method is demonstrated by the results of eightfold determinations in 13 heat-treated (canned) food samples.

Amino Acids↗
PubMed1980

Substrate specificity of a proteolytic enzyme isolated from a mutant of Pseudomonas fragi.

Previous studies have described the isolation of mutationally altered proteases in Pseudomonas fragi (Noreau, J., and Drapeau, G.R. (1979) J. Bacteriol, 140, 911-916. In the present study, it is shown that one of these proteases cleaves specifically the peptide bonds on the NH2-terminal side of either aspartic acid or cysteic acid residues in oxidized ribonuclease. With myoglobin as the substrate, a similar specificity was observed except that only four out of the six aspartyl bonds present were hydrolyzed.

Amino Acids↗
PubMed1978

Purification and characterization of mitochondrial cysteine aminotransferase from rat liver.

Cysteine aminotransferase has been purified over 300-fold from rat liver mitochondria. Transamination between L-cysteine and 2-oxoglutarate, and the reverse reaction, were observed to be catalyzed by the purified enzyme but inhibited by L-aspartate. The enzyme also catalyzed transamination of alanine, 3-sulfinic acid, aspartic acid, and cysteic acid. A new reaction assay method was devised, contributing an indication that mitochondrial cysteine aminotransferase is identical to mitochondrial aspartate aminotransferase. The latter apparently catalyzed 3 transamination reactions in the cysteine degradation process within mitochondria.

Animals↗
PubMed1995

[Cytotoxicity of excitatory sulfur amino acids in primary cultured rat cerebral neurons].

The elevation of taurine level in the central nervous system of patients with amyotrophic lateral sclerosis (ALS) indicates the presence of derangement in sulfur amino acid metabolism in this disease. In the metabolic pathway from methionine to taurine and in its branch pathways, excitatory sulfur amino acids are formed. These are cysteine (Cys), cysteine sulfinic acid (CSA), cysteic acid (CA), homocysteine sulfinic acid (HCSA), homocysteic acid (HCA) and S-sulfo cysteine (SC). This study was undertaken to investigate whether these excitatory sulfur amino acids have any cytotoxicity, since excitotoxicity has recently been implicated in the pathogenesis of ALS. Primary cultures of cerebral neurons were prepared from fetal rats, using an established method. Neuronal cell injury was assessed by examination of cultures with phase-contrast microscopy and with bright-field examination of trypan blue staining, a dye staining non-viable cells. The morphological estimate of cell injury was confirmed by the measurement of the activity of lactate dehydrogenase, released from damaged or destroyed cells, in the extracellular fluid. This convenient and quantitative index invariably correlated with the morphological estimates. Among the 6 sulfur amino acids, CSA and HCSA showed cytotoxicity, while Cys, CA, HCA and SC did not. K0.5 of CSA was 80 microM, and that of HCSA was 300 microM. The cytotoxicity of CSA was stronger than that of glutamate, K0.5 of which was 100 microM. Relevance of these excitotoxic sulfur amino acids, especially CSA to the pathogenesis of ALS has not been studied. This possibility will be a subject for future study.

Amino Acids, Sulfur↗