Thiol/disulfide homeostasis in untreated schizophrenia patients

Topçuoğlu, Canan; Bakirhan, Abdurrahim; Yılmaz, Fatma Meriç; Neşeli̇oğlu, Salim; Erel, Özcan; Sahiner, Safak Yalcin

doi:10.1016/j.psychres.2017.02.016

Cited by 30 publications

(30 citation statements)

References 35 publications

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“…It has been demonstrated that NT, TT levels were significantly lower in schizophrenia and heroin addiction patients. Furthermore, authors have demonstrated a negative correlation between NT, TT levels and Positive and Negative Syndrome Scale [45,46].…”

Section: Psychiatric Diseasesmentioning

confidence: 99%

Thiol-disulfide homeostasis: an integrated approach with biochemical and clinical aspects

Erel

Erdoğan

2020

Turk J Med Sci

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Dynamic thiol-disulfide homeostasis (TDH) is a new area has begun to attract more scrutiny. Dynamic TDH is reversal of thiol oxidation in proteins and represents the status of thiols (-SH) and disulfides (-S-S-). Organic compounds containing the sulfhydryl group is called thiol, composed of sulfur and hydrogen atoms. Disulfides are the most important class of dynamic, redox responsive covalent bonds build in between two thiol groups. For many years, thiol levels were analyzed by several methods. During last years, measurements of disulfide levels have been analyzed by a novel automated method, developed by Erel and Neselioglu. In this method, addition to thiol-termed as native thiol-levels, disulfide levels were also measured and sum of native thiol and disulfide levels were termed as total thiol. Therefore, TDH was begun to be understood in organism. In healthy humans, TDH is maintained within a certain range. Dysregulated dynamic TDH has been implicated several disorders with unknown etiology. A growing body of evidence has demonstrated that the thiol-disulfide homeostasis is involved in variety diseases, such as diabetes mellitus, hypertension, non-small cell lung cancer, Familial Mediterranean fever, inflammatory bowel diseases, occupational diseases, gestational diabetes mellitus and preeclampsia. These results may elucidate some pathogenic mechanism or may be a predictor indicating diagnostic clue, prognostic marker or therapeutic sign. In conclusion, protection of the thiol disulfide homeostasis is of great importance for the human being. Evidence achieved so far has proposed that thiol-disulfide homeostasis is an important issue needs to elucidate wholly.

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Section: Psychiatric Diseasesmentioning

confidence: 99%

Thiol-disulfide homeostasis: an integrated approach with biochemical and clinical aspects

Erel

Erdoğan

2020

Turk J Med Sci

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“…In contrast, the lack of H 2 S production may cause the pathology of Parkinson's disease, Huntington's disease and Alzheimer's disease (Cao et al, 2018;Chung et al, 2004;He et al, 2016;Paul et al, 2014;Sbodio et al, 2016Sbodio et al, , 2018Vandiver et al, 2013;Wright et al, 2016;Xie et al, 2013). The detrimental effects caused by the excess production of H 2 S and H 2 S n (Ide et al, 2019) as well as those by lacking in the neuroprotective effect of these molecules (Topcuoglu et al, 2017;Ünal et al, 2018;Xiong et al, 2018) have been reported for the pathogenesis of schizophrenia. (Taub et al, 1999).…”

Section: Pathophysiological Role Of H 2 S H 2 S N and Nomentioning

confidence: 99%

Hydrogen sulfide signalling in the CNS ‐ Comparison with NO

Kimura

2020

British J Pharmacology

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Hydrogen sulfide (H 2 S) together with polysulfides (H 2 S n , n > 2) are signalling molecules like NO with various physiological roles including regulation of neuronal transmission, vascular tone, inflammation and oxygen sensing. H 2 S and H 2 S n diffuse to the target proteins for S-sulfurating their cysteine residues that induces the conformational changes to alter the activity. On the other hand, 3-mercaptopyruvate sulfurtransferase transfers sulfur from a substrate 3-mercaptopyruvate to the cysteine residues of acceptor proteins. A similar mechanism has also been identified in S-nitrosylation. S-sulfuration and S-nitrosylation by enzymes proceed only inside the cell, while reactions induced by H 2 S, H 2 S n and NO even extend to the surrounding cells. Disturbance of signalling by these molecules as well as S-sulfuration and S-nitrosylation causes many nervous system diseases. This review focuses on the signalling by H 2 S and H 2 S n with S-sulfuration comparing to that of NO with S-nitrosylation and discusses on their roles in physiology and pathophysiology.

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“…In contrast, the lack of H 2 S production may cause the pathology of Parkinson's, Huntington's, and Alzheimer's diseases (Chung et al, 2004;Vandiver et al, 2013;Xie et al, 2013;Paul et al, 2014;Sbodio et al, 2016;Wright et al, 2016;He et al, 2016;Cao et al, 2018;Sbodio et al, 2018). The detrimental effects caused by the excess production of H 2 S and H 2 S n (Ide et al, 2019) as well as those by lacking in the neuroprotective effect of these molecules (Xiong et al, 2018;Topcuoglu et al, 2017;Unal et al, 2018;Koike et al, 2016) have been reported for the pathogenesis of schizophrenia.…”

Section: Pathophysiological Role Of H 2 S H 2 S N and Nomentioning

confidence: 99%

“…For these diseases a supplementation of H 2 S may have a benefit. In schizophrenia both beneficial and toxic effects of H 2 S and H 2 S n have been reported (Koike et al, 2016;Topcuoglu et al, 2017;Unal et al, 2018;Xiong et al, 2018;Ide et al, 2019). The balance of H 2 S, H 2 S n and NO as well as S-sulfuration together with S-nitrosylation plays an important role for the pathogenesis of these neuronal diseases.…”

Section: Introductionmentioning

confidence: 99%

Hydrogen sulfide signaling in the central nervous system -Comparison with nitric oxide-

Kimura¹

2020

Preprint

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Hydrogen sulfide (H2S) together with polysulfides (H2Sn, n>2) are signaling molecules like nitric oxide (NO) with various physiological roles including regulation of neuronal transmission, vascular tone, inflammation, oxygen sensing etc. H2S and H2Sn diffuse to the target proteins to S-sulfurate their cysteine residues to induce the conformational changes to alter the activity. On the other hand, 3-mercaptopyruvate sulfurtransferase transfers sulfur from a substrate 3-mercaptopyruvate to the cysteine residues of acceptor proteins. A similar mechanism has also been identified in S-nitrosylation. S-sulfuration and S-nitrosylation by enzymes proceed only inside the cell, while reactions induced by H2S, H2Sn and NO even extend to the surrounding cells. Disturbance of signaling by these molecules as well as S-sulfuration and S-nitrosylation causes many neuronal diseases. This review focuses on the signaling by H2S and H2Sn with S-sulfuration compared with those of NO and S-nitrosynation, and discuss on their roles in physiology and pathophysiology.

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Thiol/disulfide homeostasis in untreated schizophrenia patients

Cited by 30 publications

References 35 publications

Thiol-disulfide homeostasis: an integrated approach with biochemical and clinical aspects

Thiol-disulfide homeostasis: an integrated approach with biochemical and clinical aspects

Hydrogen sulfide signalling in the CNS ‐ Comparison with NO

Hydrogen sulfide signaling in the central nervous system -Comparison with nitric oxide-

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