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Dynamic Thiol/Disulphide Homeostasis in Patients With Fibromyalgia.

ABSTRACT: Objectives:This study aims to investigate dynamic thiol/disulphide homeostasis in patients with fibromyalgia syndrome (FMS). Patients and methods:Fifty female patients with FMS (mean age 40.5±7.2 years; range 21 to 55 years) and 40 healthy female controls (mean age 39±9.4 years, range 22 to 55 years) were included in the study. Pain visual analog scale, tender points, Fibromyalgia Impact Questionnaire, and Beck Depression Inventory were evaluated. Age, body mass index (BMI), and symptom durations were also recorded. Native thiol, disulphide and total thiol levels were measured with a novel automated method. Results:Serum disulphide levels were 14.7±3.4 ?mol/L and 22.2±3.6 ?mol/L in the FMS and control groups, respectively (p<0.001). Native thiol levels were 452.1±33.8 ?mol/L and 433.5±37.6 ?mol/L in the FMS and control groups, (p=0.015), while total thiol levels were 481.7±35.6 ?mol/L and 477.5±38.9 ?mol/L in the FMS and control groups, respectively (p=0.593). In the FMS group, disulphide/native thiol percent ratios and disulphide/ total thiol percent ratios were statistically significantly lower and native/total thiol percent ratios were statistically significantly higher than those of the control group. There were no correlations between serum thiol/disulphide profiles and pain scores & clinical variables in patients with FMS. Conclusion:Because of the decreased disulphide and increased native thiol levels, the thiol/disulphide balance has shifted to the reductive side. This metabolic disturbance may have a role in the pathogenesis of FMS.

SUBMITTER: Fidan F

PROVIDER: S-EPMC6190990 | biostudies-other | 2017 Jun

REPOSITORIES: biostudies-other

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Dynamic Thiol/Disulphide Homeostasis in Patients With Fibromyalgia.

Fidan Fatma F Alkan Berat Meryem BM Uğurlu Fatma Gülçin FG Bozkurt Sinem S Sezer Nebahat N Biçer Cemile C Erel Özcan Ö Ardiçoğlu Özge Ö Akkuş Selami S

Archives of rheumatology 20170118 2

<h4>Objectives</h4>This study aims to investigate dynamic thiol/disulphide homeostasis in patients with fibromyalgia syndrome (FMS).<h4>Patients and methods</h4>Fifty female patients with FMS (mean age 40.5±7.2 years; range 21 to 55 years) and 40 healthy female controls (mean age 39±9.4 years, range 22 to 55 years) were included in the study. Pain visual analog scale, tender points, Fibromyalgia Impact Questionnaire, and Beck Depression Inventory were evaluated. Age, body mass index (BMI), and s ...[more]

PMID: 30375563

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Project description:The protein disulphide-bond isomerization activity of highly active homogeneous protein disulphide-isomerase (measured by re-activation of 'scrambled' ribonuclease) is enhanced by EDTA and by phosphate buffers. As shown for previous less-active preparations, the enzyme has a narrow pH optimum around pH 7.8 and requires the presence of either a dithiol or a thiol. The dithiol dithiothreitol is effective at concentrations 100-fold lower than the monothiols reduced glutathione and cysteamine. The enzyme follows Michaelis-Menten kinetics with respect to these substrates; Km values are 4,620 and 380 microM respectively. The enzyme shows apparent inhibition by high concentrations of thiol or dithiol compounds (greater than 10 X Km), but the effect is mainly on the extent of reaction, not the initial rate. This is interpreted as indicating the formation of significant amounts of reduced ribonuclease in these more reducing conditions. The purified enzyme will also catalyse net reduction of insulin disulphide bonds by reduced glutathione (i.e. it has thiol:protein-disulphide oxidoreductase or glutathione:insulin transhydrogenase activity), but this requires considerably higher concentrations of enzyme and reduced glutathione than does the disulphide-isomerization activity. The Km for reduced glutathione in this reaction is an order of magnitude greater than that for the disulphide-isomerization activity, and the turnover number is considerably lower than that of other enzymes that can catalyse thiol-disulphide oxidoreduction. Conventional two-substrate steady-state analysis of the thiol:protein-disulphide oxidoreductase activity indicates that it follows a ternary-complex mechanism. The protein disulphide-isomerase and thiol:protein-disulphide oxidoreductase activities co-purify quantitatively through the final stages of purification, implying that a single protein species is responsible for both activities. It is concluded that previous preparations, from various sources, that have been referred to as protein disulphide-isomerase, disulphide-interchange enzyme, thiol:protein-disulphide oxidoreductase or glutathione:insulin transhydrogenase are identical or homologous proteins. The assay, nomenclature and physiological role of this enzyme are discussed.

Project description:Cysteine occupies a central position in plant metabolism due to its biochemical functions. Arabidopsis thaliana cells contain different O-acetylserine(thiol)lyase (OASTL) enzymes that catalyze the biosynthesis of cysteine. Because they are localized in the cytosol, plastids and mitochondria, this results in multiple subcellular cysteine pools. Much progress has been made on the most abundant OASTL enzymes; however, information on the less abundant OASTL-like proteins has been scarce. To unequivocally establish the enzymatic reaction catalyzed by the minor cytosolic OASTL isoform CS-LIKE (AT5G28030), we expressed this enzyme in bacteria and characterized the purified recombinant protein. Our results demonstrate that CS-LIKE catalyzes the desulfuration of L-cysteine to sulfide plus ammonia and pyruvate. Thus, CS-LIKE is a novel L-cysteine desulfhydrase (EC 4.4.1.1), and we propose to designate it DES1. The impact and functionality of DES1 in cysteine metabolism was revealed by the phenotype of the T-DNA insertion mutants des1-1 and des1-2. Mutation of the DES1 gene leads to premature leaf senescence, as demonstrated by the increased expression of senescence-associated genes and transcription factors. Also, the absence of DES1 significantly reduces the total cysteine desulfuration activity in leaves, and there is a concomitant increase in the total cysteine content. As a consequence, the expression levels of sulfur-responsive genes are de-regulated, and the mutant plants show enhanced antioxidant defenses and tolerance to conditions that promote oxidative stress. Our results suggest that DES1 from Arabidopsis is an L-cysteine desulfhydrase involved in maintaining cysteine homeostasis, mainly at late developmental stages or under environmental perturbations. Using the Affymetrix ATH1 GeneChips, we performed a comparative transcriptomic analysis on leaves of the des1-1 and wild type plants grown on soil for three weeks. Three biological replicates were performed for each sample and hybridized to the chips. We made the comparison of des1-1 leaves versus wild-type leaves to classify the differently expressed genes in the mutant plant.

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Dynamic Thiol/Disulphide Homeostasis in Patients With Fibromyalgia.

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Dynamic Thiol/Disulphide Homeostasis in Patients With Fibromyalgia.

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