Hydrogen sulfide in the endocrine and reproductive systems

Zhu, Xiaoyan; Gu, Hang; Ni, Xin

doi:10.1586/ecp.10.125

Cited by 34 publications

(30 citation statements)

References 74 publications

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“…It has various effects such as antioxidant, anti-inflammatory and anti-apoptotic in different parts of body (Yonezawa et al, 2007). In addition, it has the main role in corpus cavernosum as a mediator of smooth muscle relaxation and can be found in vas deferens and prostate tissues (Zhu, Gu, & Ni, 2011). It was reported that CSE is expressed in sertoli cells, spermatogonia and epididymis of rats.…”

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confidence: 99%

“…H 2 S can be produced by different enzymes including cystathionine β-synthase (CBS), cystathionine γ-lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (3MST) (Kimura, 2013). Several studies have demonstrated the protective effects of H 2 S on disorders such as renal and reproductive system diseases (Lobb et al, 2014;Zhu et al, 2011). In addition, it has the main role in corpus cavernosum as a mediator of smooth muscle relaxation and can be found in vas deferens and prostate tissues (Zhu, Gu, & Ni, 2011).…”

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confidence: 99%

“…It was reported that CSE is expressed in sertoli cells, spermatogonia and epididymis of rats. For instance, the therapeutic effects of H 2 S are reported in erectile dysfunction, heat-induced injury in testicular germ cells and diabetes-induced testicular dysfunction (Li, Xie, Chua, Wong, & Bian, 2015;Wang et al, 2018;Zhu et al, 2011). D,L-propargylglycine (PAG) is a well-known CSE enzyme inhibitor, which is used in this study to explore the exact role of CSE in this model of rat varicocele.…”

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Long‐term NaHS administration reduces oxidative stress and apoptosis in a rat model of left‐side varicocele

et al. 2019

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The main aim of this study was to assay the testicular H2S levels in the varicocele rat model and then to investigate the protective effects of NaHS on morphometric changes, sperm parameters, oxidative stress and apoptosis markers in rat's testis. D,L‐propargylglycine (PAG) was administrated to show the effects of cystathionine γ‐lyase enzyme (CSE) inhibition in the varicocele. Rats were assigned to four groups: (a) Sham, (b) varicocele, (c) varicocele + PAG and (d) varicocele + NaHS. Animals in varicocele + NaHS group received 30 µmol/L NaHS in drinking water for 56 days. In the varicocele + PAG group, animals received PAG 19 mg/kg twice a week. Morphometric assessment, oxidative stress markers, testicular H2S levels, sperm parameters, TUNEL assay and expression of Bax/Bcl2 were evaluated at the end of experiment. Testicular H2S levels were significantly decreased in varicocele group. NaHS significantly improved sperm parameters, morphometric characteristics and oxidative stress compared to varicocele group. Oxidative stress status deteriorated in the PAG group compared to the varicocele group. This study showed that a low testicular H2S level might play a critical role in male infertility. Thus, NaHS administration may be a promising treatment strategy for male infertility in varicocele. In addition, CSE may not be the only important enzyme in testicular H2S production.

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Long‐term NaHS administration reduces oxidative stress and apoptosis in a rat model of left‐side varicocele

et al. 2019

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“…H 2 S, a colorless, flammable, and foul odored gas, has been considered poisonous for a long time1022. Recently, it has been found to be a signaling molecule regulating insulin secretion/sensitivity and vascular homeostasis to control blood pressure and penile tone102223. Furthermore, it is a mediator of dietary restriction24.…”

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Hydrogen Sulfide and/or Ammonia Reduces Spermatozoa Motility through AMPK/AKT Related Pathways

Zhao

Zhang

Liu

et al. 2016

Sci Rep

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A number of emerging studies suggest that air pollutants such as hydrogen sulfide (H2S) and ammonia (NH3) may cause a decline in spermatozoa motility. The impact and underlying mechanisms are currently unknown. Boar spermatozoa (in vitro) and peripubertal male mice (in vivo) were exposed to H2S and/or NH3 to evaluate the impact on spermatozoa motility. Na2S and/or NH4Cl reduced the motility of boar spermatozoa in vitro. Na2S and/or NH4Cl disrupted multiple signaling pathways including decreasing Na+/K+ ATPase activity and protein kinase B (AKT) levels, activating Adenosine 5′-monophosphate (AMP)-activated protein kinase (AMPK) and phosphatase and tensin homolog deleted on chromosome ten (PTEN), and increasing reactive oxygen species (ROS) to diminish boar spermatozoa motility. The increase in ROS might have activated PTEN, which in turn diminished AKT activation. The ATP deficiency (indicated by reduction in Na+/K+ ATPase activity), transforming growth factor (TGFβ) activated kinase-1 (TAK1) activation, and AKT deactivation stimulated AMPK, which caused a decline in boar spermatozoa motility. Simultaneously, the deactivation of AKT might play some role in the reduction of boar spermatozoa motility. Furthermore, Na2S and/or NH4Cl declined the motility of mouse spermatozoa without affecting mouse body weight gain in vivo. Findings of the present study suggest that H2S and/or NH3 are adversely associated with spermatozoa motility.

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“…H 2 S biosynthesis in mammals is catalyzed by cystathionine β-synthase, cystathionine γ-lyase, and 3-mercaptopyruvate sulfurtransferase. 3,4 H 2 S signaling is implicated in numerous cellular processes 5−7 and plays an especially important role in the cardiovascular system where the gasotransmitter protects against ischemia/reperfusion injury, regulates blood pressure, promotes angiogenesis, and inhibits plaque formation. 8−11 H 2 S also acts as a neuromodulator/neuroprotectant and an oxygen sensor and can induce hibernation-like states in mice.…”

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Biosynthesis of a Central Intermediate in Hydrogen Sulfide Metabolism by a Novel Human Sulfurtransferase and Its Yeast Ortholog

2014

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Human sulfide:quinone oxidoreductase (SQOR) catalyzes the conversion of H2S to thiosulfate, the first step in mammalian H2S metabolism. SQOR’s inability to produce the glutathione persulfide (GSS–) substrate for sulfur dioxygenase (SDO) suggested that a thiosulfate:glutathione sulfurtransferase (TST) was required to provide the missing link between the SQOR and SDO reactions. Although TST could be purified from yeast, attempts to isolate the mammalian enzyme were not successful. We used bioinformatic approaches to identify genes likely to encode human TST (TSTD1) and its yeast ortholog (RDL1). Recombinant TSTD1 and RDL1 catalyze a predicted thiosulfate-dependent conversion of glutathione to GSS–. Both enzymes contain a rhodanese homology domain and a single catalytically essential cysteine, which is converted to cysteine persulfide upon reaction with thiosulfate. GSS– is a potent inhibitor of TSTD1 and RDL1, as judged by initial rate accelerations and ≥25-fold lower Km values for glutathione observed in the presence of SDO. The combined action of GSS– and SDO is likely to regulate the biosynthesis of the reactive metabolite. SDO drives to completion p-toluenethiosulfonate:glutathione sulfurtransferase reactions catalyzed by TSTD1 and RDL1. The thermodynamic coupling of the irreversible SDO and reversible TST reactions provides a model for the physiologically relevant reaction with thiosulfate as the sulfane donor. The discovery of bacterial Rosetta Stone proteins that comprise fusions of SDO and TSTD1 provides phylogenetic evidence of the association of these enzymes. The presence of adjacent bacterial genes encoding SDO–TSTD1 fusion proteins and human-like SQORs suggests these prokaryotes and mammals exhibit strikingly similar pathways for H2S metabolism.

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Hydrogen sulfide in the endocrine and reproductive systems

Cited by 34 publications

References 74 publications

Long‐term NaHS administration reduces oxidative stress and apoptosis in a rat model of left‐side varicocele

Long‐term NaHS administration reduces oxidative stress and apoptosis in a rat model of left‐side varicocele

Hydrogen Sulfide and/or Ammonia Reduces Spermatozoa Motility through AMPK/AKT Related Pathways

Biosynthesis of a Central Intermediate in Hydrogen Sulfide Metabolism by a Novel Human Sulfurtransferase and Its Yeast Ortholog

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