bims-smemid Biomed News
on Stress metabolism in mitochondrial dysfunction
Issue of 2025–03–23
three papers selected by
Deepti Mudartha, The International Institute of Molecular Mechanisms and Machines



  1. J Physiol Biochem. 2025 Mar 21.
      Pyruvate dehydrogenase kinases (PDKs) can regulate the conversion of pyruvate to acetyl coenzyme A through the mitochondrial pyruvate dehydrogenase complex (PDHC). As the rate-limiting enzymes of PDHC, PDKs link glycolysis to the tricarboxylic acid cycle. Pathological changes in many diseases involve alterations in cellular metabolism, which are partly reflected in changes in mitochondrial function. The intermediate role of PDKs in metabolic processes allows for the influence of both glycolysis and oxidative phosphorylation. Recent studies have shown that PDKs play a crucial role in regulating metabolic reprogramming, mitochondrial function and cellular activities in both oncological studies and various non-oncological diseases. This paper aims to clarify the molecular regulatory mechanisms of PDKs; review the relationship of PDKs with cellular metabolic reprogramming, regulation of ROS, and apoptosis; and the present status of research on PDKs in osteoporosis, diabetes mellitus, and vascular diseases. With this review, we have increased our understanding and insight at the molecular level, providing new insights into targeting PDKs to reverse metabolism-related diseases.
    Keywords:  Apoptosis; Metabolic diseases; Metabolic reprogramming; Pyruvate dehydrogenase kinase; ROS
    DOI:  https://doi.org/10.1007/s13105-025-01068-9
  2. Free Radic Biol Med. 2025 Mar 17. pii: S0891-5849(25)00175-3. [Epub ahead of print]
      Coenzyme A (CoA) is an essential cofactor present in all living cells, which plays critical roles in diverse biochemical processes, including cellular metabolism, signal transduction, regulation of gene expression, and the antioxidant response. This review summarizes current knowledge on the role of CoA and its metabolically active thioesters in promoting cellular growth and proliferation (pro-growth) and discusses emerging research on CoA's antioxidant properties that enhance cell survival (pro-survival).
    Keywords:  Antioxidant function; Cellular metabolism; Coenzyme A; Protein CoAlation; Signal transduction
    DOI:  https://doi.org/10.1016/j.freeradbiomed.2025.03.025
  3. Redox Biol. 2025 Mar 14. pii: S2213-2317(25)00108-9. [Epub ahead of print]82 103595
      Mitochondria are central to eukaryotic cell function, driving energy production, intermediary metabolism, and cellular homeostasis. Dysregulation of mitochondrial function often results in oxidative stress, a hallmark of numerous diseases, underscoring the critical need for maintaining mitochondrial integrity. Among mitochondrial enzymes, thiosulfate sulfurtransferase (TST) has emerged as a key regulator of sulfur metabolism, redox balance, and Fe-S protein maintenance. Beyond its well-known role in cyanide detoxification, TST facilitates hydrogen sulfide (H2S) metabolism by catalyzing the transfer of sulfur from persulfides (R-SSH) to thiosulfate (S2O32-), promoting H2S oxidation and preventing its toxic accumulation. Additionally, TST contributes to the thiol-dependent antioxidant system by regulating reactive sulfur species and sustaining mitochondrial functionality through its role in sulfide-driven bioenergetics. This review highlights the biochemical and therapeutic significance of TST in mitochondrial and cellular health, emphasizing its protective roles in diseases associated with oxidative stress and mitochondrial dysfunction. Dysregulation of TST has been implicated in diverse pathologies, including specific metabolic disorders, neurological diseases, cardiovascular conditions, kidney dysfunction, inflammatory bowel disease, and cancer. These associations underline TST's potential as a biomarker and therapeutic target. Therapeutic strategies to activate the TST pathway are explored, with a focus on sodium thiosulfate (STS), novel small molecule (Hit 2), and recombinant hTST protein. STS, an FDA-approved compound, has demonstrated antioxidant and anti-inflammatory effects across multiple preclinical models, mitigating oxidative damage and improving mitochondrial integrity. A slow-release oral formulation of STS is under development, offering promise for expanding its clinical applications. Small molecule activators like Hit 2 and hTST protein have shown efficacy in enhancing mitochondrial respiration and reducing oxidative stress, though both reagents need further in vitro and in vivo investigations. Despite promising advancements, TST-based therapies remain underexplored. Future research should focus on leveraging TST's interplay with pathways like NRF2 signaling, investigating its broader protective roles in cellular health, and developing targeted interventions. Enhancing TST activity represents an innovative therapeutic approach for addressing mitochondrial dysfunction, oxidative stress, and their associated pathologies, offering new hope for the treatment of diseases associated with mitochondrial dysfunction.
    Keywords:  Mitochondrial dysfunction; Oxidative stress; Redox signaling; Thiosulfate sulfurtransferase (TST)
    DOI:  https://doi.org/10.1016/j.redox.2025.103595