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Review
. 2022 Oct 19:9:928287.
doi: 10.3389/fmolb.2022.928287. eCollection 2022.

The role of sulfur compounds in chronic obstructive pulmonary disease

Simin Jiang  1 , Yahong Chen  1
Affiliations
Review

The role of sulfur compounds in chronic obstructive pulmonary disease

Simin Jiang et al. Front Mol Biosci. .

Abstract

Chronic obstructive pulmonary disease (COPD) is a common respiratory disease that brings about great social and economic burden, with oxidative stress and inflammation affecting the whole disease progress. Sulfur compounds such as hydrogen sulfide (H2S), thiols, and persulfides/polysulfides have intrinsic antioxidant and anti-inflammatory ability, which is engaged in the pathophysiological process of COPD. Hydrogen sulfide mainly exhibits its function by S-sulfidation of the cysteine residue of the targeted proteins. It also interacts with nitric oxide and acts as a potential biomarker for the COPD phenotype. Thiols' redox buffer such as the glutathione redox couple is a major non-enzymatic redox buffer reflecting the oxidative stress in the organism. The disturbance of redox buffers was often detected in patients with COPD, and redressing the balance could delay COPD exacerbation. Sulfane sulfur refers to a divalent sulfur atom bonded with another sulfur atom. Among them, persulfides and polysulfides have an evolutionarily conserved modification with antiaging effects. Sulfur compounds and their relative signaling pathways are also associated with the development of comorbidities in COPD. Synthetic compounds which can release H2S and persulfides in the organism have gradually been developed. Naturally extracted sulfur compounds with pharmacological effects also aroused great interest. This study discussed the biological functions and mechanisms of sulfur compounds in regulating COPD and its comorbidities.

Keywords: chronic obstructive pulmonary disease; hydrogen sulfide; sulfane sulfur; sulfur compound; thiols.

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Conflict of interest statement

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

Figures

FIGURE 1
FIGURE 1
Enzymatic biosynthesis and oxidative pathway of hydrogen sulfide (H2S). The biosynthesis of H2S was mediated by CBS, CSE, and 3-MST. The major substrates are homocysteine and L-cysteine. Persulfide and polysulfides reduced in mitochondria also generate H2S. H2S can be oxidized by SQR, SD, and ST, which are mitochondrial inner membrane-anchored enzymes, to form sulfate and deprived from the organism. CBS: cystathionine β-synthase; CSE, cystathionine γ-lyase; CAT, cysteine aminotransferase; CoQ, coenzyme Q; CARS, cysteinyl-tRNA synthetases; 3-MST, 3-mercaptopyruvate; MST, 3-mercaptopyruvate sulfurtransferase; α-KG, α-ketoglutarate; SQR, sulfide quinone reductase; SD, sulfur dioxygenase; ST, sulfur transferase.
FIGURE 2
FIGURE 2
Mechanism of hydrogen sulfide alleviating chronic obstructive pulmonary disease. EMT, epithelial–mesenchymal transition; ERS, endoplasmic reticulum stress; SOD, superoxide dismutase.
FIGURE 3
FIGURE 3
Dynamic interchange between protein persulfides, protein thiols, and H2S. H2S can react with an oxidized cysteine residue in protein (e.g., -SOH, -SNO, and -SSG) to generate protein persulfides. The protein persulfides can be oxidized by ROS and subsequently reduced by Trx to form thiols. The protein thiols can also transform into protein persulfides via trans-sulfidation. Trx, thioredoxin; ROS, reactive oxygen species.
FIGURE 4
FIGURE 4
Interaction between hydrogen sulfide and nitric oxide. H2S can directly react with NO to form HSNO. HSNO is unstable, which can be reduced by H2S to form HNO and H2S2. Chemical interplay of the H2S donor Na2S with the NO donor (DEA/NO or RSNOs) produces nitrosopersulfide (SSNO-), polysulfides, and SULFI/NO. H2S has both activation and inhibition ability toward the synthesis of NO and vice versa. SULFI, N-nitrosohydroxylamine-N-sulfonate.
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