Role of sulfiredoxin in systemic diseases influenced by oxidative stress

Abstract

Sulfiredoxin is a recently discovered member of the oxidoreductases family which plays a crucial role in thiol homoeostasis when under oxidative stress. A myriad of systemic disorders have oxidative stress and reactive oxygen species as the key components in their etiopathogenesis. Recent studies have evaluated the role of this enzyme in oxidative stress mediated diseases such as atherosclerosis, chronic obstructive pulmonary disease and a wide array of carcinomas. Its action is responsible for the normal functioning of cells under oxidative stress and the promotion of cell survival in cancerous cells. This review will highlight the cumulative effects of sulfiredoxin in various systemic disorders with a strong emphasis on its target activity and the factors influencing its expression in such conditions.

Chemical proteomics reveals new targets of cysteine sulfinic acid reductase

“…The observation that PRDX6 and GAPDH S -sulfinylation is not repaired by SRX is consistent with earlier biochemical findings 16 and independently validate our method. The overall level of S -sulfinylation was also increased in Srx −/− MEFs during the recovery period ( Supplementary Dataset 3 ), affirming the susceptibility of Srx -deficient cells to acute oxidative stress 21,35 . As tryptic peptides bearing the catalytic cysteines of established SRX substrates PRDX 1–4 were too long and hydrophobic for robust chemoproteomic analysis, we next examined whether DiaAlk could detect changes in S -sulfinylation in one of these sentinel peroxidases, PRDX1, by immunoblot.…”

“…18,19 ). Despite its regulatory potential 20 and association with diseases 21 linked to reactive oxygen species (ROS) 22 generation, including cancer 23–25 , the scope, dynamics, and function of sulfinic acid is essentially unknown, owing to major challenges of detection.…”

Comparative estimation of sulfiredoxin levels between chronic periodontitis and healthy patients – A case‐control study

“…Induction of sulfiredoxin expression through the transcription factor Nrf2 (nuclear factor‐erythroid2‐related factor 2) was observed in various cell types . Literature review has elucidated the role of sulfiredoxin in various oxidative stress‐induced conditions and thereby ascertained the pivotal role of sulfiredoxin in the redox balance …”

“…The Srx enzyme is solely responsible for Prx activation by the reduction of the cysteine sulfinic acid of the Prx to its stable thiol state . The Srx enzyme exerts its action on Prx to efficiently remove the hydrogen peroxide moieties and attenuate intracellular oxidative stress …”

Targeting the Redox Landscape in Cancer Therapy

“…Overoxidation of the peroxidatic cysteine yields sulfinic or irreversible sulfonic acid, rendering PRDX inactive [206] ( Figure 2). Sulfinic acid in PRDX can be reduced to sulfenic acid by sulfiredoxin, an antioxidative enzyme that is explored as a potential drug target in cancer therapy [207][208][209]. Reversible sulfenic acid in PRDXs is reduced by the thiol-containing thioredoxin, which exists as a cytosolic (TXN1) and a mitochondrial version (TXN2).…”