bims-cytox1 Biomed News
on Cytochrome oxidase subunit 1
Issue of 2026–10–18
two papers selected by
Gavin McStay, Liverpool John Moores University
  1. Reversible Dimerization of Cytochrome Oxidase in Detergent Solution as Detected by Dynamic Light Scattering.
  2. Mitochondrially Encoded Cytochrome C Oxidase 1, a Hypoxia- and Lactylation-Related Gene, Acts as a Tumor Suppressor and Therapeutic Target in Oral Squamous Cell Carcinoma.
  1. Int J Mol Sci. 2026 Sep 30. pii: 8744. [Epub ahead of print]27(19):
    Reversible Dimerization of Cytochrome Oxidase in Detergent Solution as Detected by Dynamic Light Scattering.
    Natalia V Azarkina, Victor N Orlov, Maria S Muntyan, Yury M Chesnokov, Semen V Nesterov, Ilya P Oleynikov, Tatiana V Vygodina.
      Reversible changes in the quaternary structure of eukaryotic cytochrome c oxidase (CcO) are presumably involved in the enzyme activity regulation. Conventional methods for determining quaternary states are relatively complex. We applied dynamic light scattering (DLS) to estimate the size of CcO in micelles and identified different oligomeric forms in dynamic equilibrium. Thin-layer gel filtration and non-denaturing gel electrophoresis revealed CcO forms with different molecular masses. CcO quaternary structure was analyzed by cryo-electron microscopy. Prokaryotic cytochrome oxidase served as a control. Increasing protein concentration, cholate treatment, and acidification shifted the equilibrium toward larger micellar structures, suggesting CcO oligomerization. Protein dilution, dodecyl maltoside at high concentrations, alkalinization, and treatment with Triton X-100 reversed this process. The apparent size of prokaryotic cytochrome oxidase micelles remained constant regardless of enzyme concentration and presence of cholate. The apparent molecular masses of CcO in diluted and concentrated preparations corresponded to monomers and dimers, respectively. The amphipol-stabilized CcO forms, both monomeric and the cholate-containing dimeric, retained their characteristic sizes across various enzyme concentrations. Given that the DLS-based identification of the CcO oligomeric states was confirmed by three independent methods mentioned above, DLS appears to be a convenient tool for characterizing CcO quaternary structures in solution and monitoring their interconversion.
    Keywords:  amphipol; cytochrome c oxidase; dimerization; dynamic light scattering; monomerization
    DOI:  https://doi.org/10.3390/ijms27198744
  2. Head Neck. 2026 Oct 13.
    Mitochondrially Encoded Cytochrome C Oxidase 1, a Hypoxia- and Lactylation-Related Gene, Acts as a Tumor Suppressor and Therapeutic Target in Oral Squamous Cell Carcinoma.
    Yuan-Dong Zuo, Si-Da Dong, Jian-Hao Li, Ji-Chen Li.
       BACKGROUND: Aberrant expression of mitochondrially encoded Cytochrome c Oxidase Subunit 1 (MT-CO1) has increasingly been associated with tumor invasiveness and adverse clinical outcomes across multiple malignancies. However, its functional role and regulatory mechanisms in oral squamous cell carcinoma (OSCC) remain poorly understood.
    METHODS: Transcriptomic data from The Cancer Genome Atlas (TCGA) and the Gene Expression Omnibus (GEO) were integrated to identify genes consistently dysregulated across datasets. Candidate prognostic genes were subsequently prioritized using Cox proportional hazards regression in combination with least absolute shrinkage and selection operator (LASSO) regression. A multi-omics validation framework was then applied, encompassing analysis of MT-CO1 expression in OSCC, protein-level validation using the Human Protein Atlas, and evaluation of associations with clinicopathological characteristics. The functional effects of MT-CO1 were evaluated in OSCC cell lines using gain-of-function assays. To assess the feasibility of pharmacologically targeting MT-CO1, molecular docking and subsequent molecular dynamics simulations were performed to characterize the interaction between amorolfine and MT-CO1; mechanistic rescue experiments were then conducted to determine whether the drug's effects were MT-CO1-dependent.
    RESULTS: MT-CO1 was associated with hypoxia and lactylation and was downregulated in OSCC, with lower expression correlating with poorer survival. MT-CO1 overexpression reduced cell viability, proliferation, and invasion while enhancing apoptotic signaling in vitro. Computational analyses further predicted a stable, high-affinity interaction between amorolfine and MT-CO1. Importantly, MT-CO1 suppression attenuated the antineoplastic effects of amorolfine in OSCC cells, supporting an MT-CO1-dependent mechanism of action.
    CONCLUSIONS: MT-CO1 as an underappreciated tumor-suppressive factor in OSCC and support further evaluation of amorolfine for therapeutic repurposing. MT-CO1 may serve as a biomarker of treatment response and that the MT-CO1-amorolfine axis may represent an actionable therapeutic vulnerability in OSCC.
    Keywords:  hypoxia; lactylation; mitochondrially encoded cytochrome C oxidase 1; oral squamous cell carcinoma
    DOI:  https://doi.org/10.1002/hed.70475
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