Boyao Tan’s research while affiliated with Anhui University of Traditional Chinese Medicine and other places

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Publications (1)

Physiological function of sulfur. Sulfur mainly exists in the form of compounds in the human body and participates in various biological processes. First of all, sulfur also participates in antioxidant defense and detoxification processes. Cysteine is an important antioxidant that can neutralize reactive oxygen species, thereby reducing the damage of oxidative stress to cells iron–sulfur proteins are minimally functional proteins of mitochondria; Secondly, Cystine and cysteine, two sulfur-containing amino acids, participate in the formation of disulfide bonds in proteins, stabilizing their three-dimensional structure and function. The formation of disulfide bonds can maintain the normal conformation of proteins, thereby ensuring their normal function; Finally, sulfur also participates in the synthesis of iron sulfur proteins and is an essential component of the electron transport chain. It plays a critical role in biological processes such as cellular respiration and photosynthesis.
The similarities and differences between disulfidptosis and ferroptosis in CNS. SLC7A11 is the catalytic subunit of the XcT system, which absorbs cysteine from the extracellular environment and converts it into cysteine to synthesize GSH. GPX4 uses GSH to reduce LOOH to LOH, preventing lipid peroxidation and inhibiting ferroptosis. Meanwhile, GSH is oxidized to GSSG. Then GSSG is converted back to GSH through GR mediated reduction reaction, consuming NADPH in the process. Under conditions of glucose starvation and high SLC7A11, the pentose phosphate pathway is blocked, resulting in reduced NADPH production, hindered conversion of cysteine to cysteine, accumulation of cysteine and other disulfides, triggering the formation of abnormal disulfide bonds in redox sensitive proteins, ultimately leading to the rupture of the cytoskeleton and cell disulfidptosis. On the other hand, due to NADPH depletion, cystine cannot be converted into cysteine, resulting in reduced synthesis of GSH and generation of lipid peroxides, leading to ferroptosis. Abbreviations: NADP+: nicotinamide adenine dinucleotide phosphate, reduced form; NADPH: nicotinamide adenine dinucleotide phosphate; GSH: glutathione; GPX4: Glutathione peroxidase 4; LOOH: lipid hydroperoxides; LOH: lipid alcohols; GSSG: glutathione disulfide; GR: glutathione disulfide reductase.
Mechanisms of disulfidptosis. By analyzing the relationships among the expression level of SL7A11, NADPH metabolism, and glucose levels, the factors necessary for cell death were explored. When SLC7A11 and glucose are overexpressed or decreased simultaneously, cell survival occurs. However, only when high SLC7A11, low glucose, and NADPH depletion are present simultaneously can they lead to cystine/cysteine conversion disorders, the accumulation of disulfides, and ultimately disulfidptosis. When glucose starvation blocks the production of NADPH through the pentose phosphate pathway, a large amount of intracellular cysteine input through high expression of SLC7A11 depletes NADPH. Owing to the insolubility of cystine, NADPH is needed as a reducing force to decompose it into cysteine. The low supply of NADPH also blocks the process of cystine conversion to cysteine, leading to a large accumulation of cystine and activating the Rac1-WRC-Arp2/3 pathway. Abnormal disulfide bonds are formed in actin cytoskeleton proteins, and F-actin is broken down, ultimately leading to disulfidptosis. Moreover, depletion of NADPH can also hinder GSH/GSSG conversion and Trx-(SH) 2/Trx-S2 conversion, ultimately leading to an imbalance in the intracellular glutathione and thioredoxin antioxidant systems. Abbreviations: GLUT: glucose transporter; Trx-(SH) 2: thioredoxin reduced; Trx-S2 thioredoxin oxidized; NADP+: nicotinamide adenine dinucleotide phosphate, reduced form; NADPH: nicotinamide adenine dinucleotide phosphate; G6P: glucose-6-phosphate dehydrogenase; 6PG: 6-phosphogluconate; R5P: ribose-5-phosphate dehydrogenase; GSH: glutathione; GSSG: glutathione oxidized.
Disulfidptosis-related genes in the CNS.
Disulfidptosis: a new target for central nervous system disease therapy
  • Literature Review
  • Full-text available

March 2025

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64 Reads

Jing Chang

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Danhong Liu

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Yuqi Xiao

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Jun Liao

Disulfidptosis is a pathologic process that occurs under conditions of NADPH deficiency and excess disulfide bonds in cells that express high levels of SLC7A11. This process is caused by glucose deprivation-induced disulfide stress and was first described by cancer researchers. Oxidative stress is a hypothesized mechanism underlying diseases of the central nervous system (CNS), and disulfide stress is a specific type of oxidative stress. Proteins linked to disulfidptosis and metabolic pathways involved in disulfidptosis are significantly associated with diseases of the CNS (neurodegenerative disease, neurogliomas and ischemic stroke). However, the specific mechanism responsible for this correlation remains unknown. This review provides a comprehensive overview of the current knowledge regarding the origin elements, genetic factors, and signaling proteins involved in the pathogenesis of disulfidptosis. It demonstrates that the disruption of thiometabolism and disulfide stress play critical roles in CNS diseases, which are associated with the potential role of disulfidptosis. We also summarize disulfidptosis-related drugs and highlight potential therapeutic strategies for treating CNS diseases. Additionally, this paper suggests a testable hypothesis that might be a promising target for treating CNS diseases.

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