bims-medica Biomed News
on Metabolism and diet in cancer
Issue of 2026–01–25
eleven papers selected by
Brett Chrest, Wake Forest University
  1. The 2025 Sir David Cuthbertson Lecture: Energy metabolism: Beyond calories, feeding the mitochondria.
  2. The Antiseizure Medication Stiripentol Inhibits Mitochondrial Complex I by Blocking Early-Stage Electron Transfer.
  3. Vitamin B12 supports skeletal muscle oxidative phosphorylation capacity in male mice.
  4. Renal Ketogenesis Protects Against Ischemic Kidney Injury.
  5. BCOR mutations define a therapeutic vulnerability to DHODH Inhibition in acute myeloid leukemia.
  6. Dietary duration and composition differentially influence mitochondrial activity and gene expression in a tissue-specific manner in aged rats.
  7. Glucose-6-phosphate dehydrogenase deficiency is associated with improved survival in patients with acute myeloid leukemia treated with venetoclax and azacitidine.
  8. Glioma chemotherapeutic resistance is tied to membrane electrophysiological properties and glycosylation.
  9. NDUFS4, a mitochondrial complex I subunit, is essential for T-cell metabolic fitness and immune function.
  10. NAD+ and Sirt5 restore mitochondrial bioenergetics failure and improve locomotor defects caused by sucla2 mutations.
  11. BDH1 Protects against Diabetic Cardiomyopathy by Improving Mitochondrial Function and Suppressing Cardiomyocyte Apoptosis Via Activation of the AKT/GSK3β Pathway.
  1. Clin Nutr. 2026 Jan 09. pii: S0261-5614(26)00002-6. [Epub ahead of print]57 106575
    The 2025 Sir David Cuthbertson Lecture: Energy metabolism: Beyond calories, feeding the mitochondria.
    Eric Fontaine.
      In this article, I explore how energy metabolism depends on proper mitochondrial function. Adenosine triphosphate (ATP), the main source of energy for cells, is mainly produced in the mitochondria as a result of the fusion of hydrogen produced by the breakdown of nutrients with oxygen. This reaction allows protons to be pumped across the inner mitochondrial membrane, creating a gradient that powers ATP synthesis. However, ATP production is not perfectly efficient. Some oxygen is consumed without generating ATP due to proton leaks or other processes that utilize the gradient. Diet, hormones, and cellular signals can alter mitochondrial efficiency: for example, hyperthyroidism and polyunsaturated fatty acid deficiency cause uncoupling, while hypothyroidism and nitric oxide increase coupling but reduce maximum ATP production. I also point out that the use of ATP depends on its thermodynamic value, which is reflected in the Adenosine triphosphate/Adenosine diphosphate ratio ([ATP]/[ADP] ratio). A decrease in this ratio can selectively reduce certain ATP-consuming processes, as shown in studies on metformin and imeglimin. In cases of stress or nutritional deficiency, cells can consume ATP without performing useful work, leading to inefficiency or even cell death when the [ATP]/[ADP] ratio collapses. Knowing that these concepts are quite complex, I have simplified them to make clear that mitochondria are more than just passive "powerhouses of cells".
    Keywords:  Efficiency; Energy metabolism; Flux–force relationship; Kinetics; Mitochondria; Thermodynamics
    DOI:  https://doi.org/10.1016/j.clnu.2026.106575
  2. J Biol Chem. 2026 Jan 20. pii: S0021-9258(26)00049-9. [Epub ahead of print] 111179
    The Antiseizure Medication Stiripentol Inhibits Mitochondrial Complex I by Blocking Early-Stage Electron Transfer.
    Cyrielle L Bouchez, Thibaut Molinié, Guillaume Duranthon, Sebastian Lillo, Corinne Pellon, Nadia El Mammeri, Benjamin Dartigues, Philippe Pasdois, Benoit Pinson, Macha Nikolski, Anne Devin, Arnaud Mourier, Roland T Ullrich, Thomas Daubon.
      The oxidation of NADH is essential for maintaining cellular redox balance and supporting cell metabolism. Mitochondrial complex I (NADH:ubiquinone oxidoreductase) plays a central role in this process by coupling NADH oxidation to electron transfer and proton translocation across the inner mitochondrial membrane. We previously reported that the antiseizure medication stiripentol decreases lactate production and mitochondrial respiration, suggesting an impact on NADH turnover beyond its known inhibition of lactate dehydrogenase. In this study, we identify complex I as a target of stiripentol across multiple species and cell types. Biochemical and spectroscopic analyses demonstrate that stiripentol inhibits NADH oxidation and electron transfer through a mechanism distinct from that of classical ubiquinone pocket inhibitors such as rotenone or piericidin A. Remarkably, stiripentol acts upstream of the ubiquinone reduction site, representing the first example of a complex I inhibitor with a binding site within the N-module. These findings uncover a previously unrecognized mode of complex I inhibition and link stiripentol's metabolic effects to direct modulation of mitochondrial NADH oxidation. This work broadens the understanding of stiripentol's mechanism of action and highlights its potential to modulate redox metabolism in cancer cells.
    DOI:  https://doi.org/10.1016/j.jbc.2026.111179
  3. J Nutr. 2026 Jan 20. pii: S0022-3166(26)00016-7. [Epub ahead of print] 101367
    Vitamin B12 supports skeletal muscle oxidative phosphorylation capacity in male mice.
    Luisa F Castillo, Katarina E Heyden, Abigail R Williamson, Wenxia Ma, Olga V Malysheva, Nathaniel M Vacanti, Anna E Thalacker-Mercer, Martha S Field.
       BACKGROUND: Vitamin B12 is a cofactor in folate-mediated one-carbon metabolism (FOCM), which generates nucleotides (thymidylate (dTMP) and purines) and methionine. Depressed de novo thymidylate (dTMP) synthesis leads to uracil accumulation in DNA.
    OBJECTIVE: The purpose of this study was to determine how B12 availability affects mitochondrial DNA (mtDNA) integrity and mitochondrial function in skeletal muscle. B12 deficiency was modeled in young-adult mice. Intramuscular B12 injection in aged mice assessed the role of B12 supplementation in age-related changes in skeletal muscle.
    METHODS: Male methionine synthase knockdown (Mtr+/-) and wild-type littermates (Mtr+/+) were weaned to either an AIN93G-based control (C) diet containing 25 μg/kg vitamin B12 (Mtr+/+, n=8; Mtr+/-, n=9) or a B12-deficient (-B12) diet containing 0 μg/kg vitamin B12 (n=9 per genotype) for seven weeks. Aged (20-22mo) male C57BL/6N mice were acclimated to an AIN93G control diet four weeks, then received either weekly injections of saline (vehicle control [30 uL 0.9% NaCl], n=5) or B12 (0.65 μg per 30uL 0.9% NaCl; n=6) in each of two hindleg muscles [1.25 μg B12 total]) for eight weeks. Outcomes measured included maximal oxygen consumption rate (OCR), uracil in mtDNA (a biomarker of mtDNA integrity), mtDNA copy number, and mitochondrial mass. Data were analyzed using a two-way ANOVA in the Mtr+/- mouse model exposed to B12-deficient diets and by a student's t-test for B12 supplementation in aged mice.
    RESULTS: The tibialis anterior (TA) muscle from Mtr+/- mice exhibited 50% lower (p=0.01) maximal respiratory capacity of the electron transport chain than did TA from Mtr+/+ mice. Exposure to the -B12 diet lowered maximal capacity of complex I in mitochondrially rich muscle (soleus and mitochondria-rich portions of quadriceps and gastrocnemius) by 25% (p=0.02). Uracil in mitochondrial DNA (mtDNA) in red muscle and gastrocnemius was elevated ∼10 fold with exposure to -B12 diet (p=0.04 and p<0.001, respectively). In aged mice, gastrocnemius complex IV activity was increased 2-fold with intramuscular B12 supplementation (p=0.04).
    CONCLUSIONS: Exposure to a B12-deficient diet led to uracil accumulation in mtDNA and impaired maximal oxidative capacity in skeletal muscle. B12 supplementation improved complex IV maximal capacity in gastrocnemius from aged mice, a model of age-related skeletal muscle decline.
    Keywords:  Vitamin B12; mitochondrial DNA; oxidative phosphorylation; skeletal muscle; thymidylate; uracil
    DOI:  https://doi.org/10.1016/j.tjnut.2026.101367
  4. J Am Soc Nephrol. 2026 Jan 21.
    Renal Ketogenesis Protects Against Ischemic Kidney Injury.
    Kyle Feola, Andrea H Venable, Mina Rasouli, Emma-Grace Haley, Chetana Jadhav, Ricardo Monroy, Tatyana McCoy, Sarah C Huen.
       BACKGROUND: Abnormal renal fatty acid oxidation in kidney disease suggests that dysregulated metabolism is a key component of kidney disease pathogenesis. While the liver is the main ketogenic organ, the rate-limiting enzyme for ketogenesis, mitochondrial Hydroxymethylglutaryl-CoA synthase 2 (HMGCS2), is induced in the proximal tubule of the kidney during fasting. We previously demonstrated that HMGCS2 induced in the kidney does not contribute to the circulating pool of ketones during fasting and cannot compensate for hepatic ketogenic deficiency. We hypothesized that kidney HMGCS2 may be acting locally within the kidney to maintain normal function during metabolic stress or injury.
    METHODS: Mice with kidney or liver specific deletion of Hmgcs2 were subjected to ischemia/reperfusion injury (IRI). Kidney histology, metabolomics and lipidomics were analyzed. Mice were placed on a ketogenic diet for four days to increase plasma and kidney ketone content. Using novel mouse models with proximal tubular hemagglutinin-tagged mitochondria with or without Hmgcs2 deletion, proximal tubular-specific mitochondria were isolated and fatty acid oxidation capacity was measured after IRI.
    RESULTS: Mice with kidney specific Hmgcs2 deletion had significantly more kidney injury after IRI compared to wild-type controls. Kidneys lacking HMGCS2 exhibited a decrease in ketone content and an increase in lipid droplet accumulation after IRI. Proximal tubular-specific mitochondria lacking HMGCS2 had significantly lower fatty acid oxidation capacity both at baseline and after ischemic injury. Administration of a ketogenic diet for four days prior to IRI was sufficient to decrease kidney injury and augment mitochondrial fatty acid oxidation in kidney Hmgcs2 knockout mice. Kidney tissue lipidomics revealed that the loss of kidney HMGCS2 was associated with a decrease in both arachidonic acid containing phospholipids and prostaglandin levels.
    CONCLUSIONS: Loss of renal HMGCS2 and resultant ketogenesis increased ischemia-induced injury and decreased mitochondrial fatty acid oxidation capacity, suggesting a role in renal ketogenesis in limiting acute kidney injury.
    DOI:  https://doi.org/10.1681/ASN.0000001014
  5. Ann Hematol. 2026 Jan 19. 105(1): 32
    BCOR mutations define a therapeutic vulnerability to DHODH Inhibition in acute myeloid leukemia.
    Florian Robert, Cherif Badja, Soraya Boushaki, Andrea Degasperi, Yasin Memari, Sophie Momen, Theodoros I Roumeliotis, Zuza Kozik, Malgorzata Gozdecka, Jyoti Choudhary, George Vassiliou, Gene Cc Koh, Serena Nik-Zainal.
      Acute Myeloid Leukemia (AML) remains challenging to treat, especially in cases with mutations in the BCL-6 co-repressor (BCOR), which are associated with poor prognosis and chemo-resistance. In this study, we reveal a synthetic lethal interaction between BCOR and dihydroorotate dehydrogenase (DHODH). We demonstrate that BCOR-deficient cells have a heightened sensitivity to DHODH inhibitors such as brequinar and leflunomide, that are already in clinical use. We confirm that DHODH inhibition selectively induces cell death in BCOR-mutant cells in multiple cellular models, in malignant and non-malignant cells, through chemical and genetic manipulation. Interestingly, we find that the dependency on DHODH does not stem from its role in de novo pyrimidine biosynthesis disruption. Rather, DHODH's role in the electron transport chain, essential for mitigating reactive oxygen species, may be the physiological vulnerability that pushes BCOR-mutant cells toward cell death when DHODH is inhibited. DHODH inhibitors could be repurposed as targeted therapies for BCOR-mutant tumors, offering a promising strategy for precision medicine in AML and other cancers.
    Keywords:  Acute myeloid leukemia; BCOR; DHODH; DHODH inhibition; Leukemia; Synthetic lethality; Targeted therapy 
    DOI:  https://doi.org/10.1007/s00277-026-06773-z
  6. Transl Med Aging. 2025 ;9 100-107
    Dietary duration and composition differentially influence mitochondrial activity and gene expression in a tissue-specific manner in aged rats.
    Brea J Ford, Anisha Banerjee, Sarah Ding, Anna A Caton, Ashley Grothaus, Sara N Burke, Abbi R Hernandez.
      Mitochondrial dysfunction is a hallmark of aging, affecting multiple systems and tissues, contributing to impairments in function. The resultant decreases in energy availability, along with increased oxidative stress, may be attenuated through diet. Fasting paradigms (including time restricted feeding (TRF)) and ketogenic diets (keto) both influence mitochondrial function, potentially mitigating these effects. However, the duration and modality of dietary intervention required for ameliorating age-related mitochondrial impairments remain unknown. Therefore, this study investigated the effects of a chronically (8-24 months; cTRFc) and acutely (22-24 months; aTRFc) administered TRF diet with standard macronutrients, as well as a chronically (8-24 months) administered TRF with ketogenic macronutrients (cTRFk), on mitochondrial activity and gene expression in aged male rats across tissues (brain, liver, muscle). Despite some synergy across the chronic diet groups, keto and TRF duration influenced mitochondrial function in a tissue- and diet-specific manner. Mitochondrial complex II activity was higher in cTRFk rats within the liver. Mitochondrial complex IV activity was lower in muscle and hippocampal tissue in both chronic TRF-fed groups. Relatedly, expression of the complex IV-related gene Cox2 increased within the CA3 subregion of the hippocampus of cTRFk. In this same region, expression of the mitochondrial biogenesis related gene Pgc1a was increased in cTRFc diet rats only. Within the liver, Cox5b expression increased in both groups of chronic TRF rats. Together, these findings highlight complex, tissue-specific responses to long-term dietary interventions, emphasizing the need for further research to develop targeted nutritional strategies for enhancing mitochondrial function and metabolic health in aging populations.
    Keywords:  Fasting; Hippocampus; Ketogenic diet; Liver; Muscle
    DOI:  https://doi.org/10.1016/j.tma.2025.11.001
  7. Cancer. 2026 Feb 01. 132(3): e70265
    Glucose-6-phosphate dehydrogenase deficiency is associated with improved survival in patients with acute myeloid leukemia treated with venetoclax and azacitidine.
    Shira Buchrits, Alon Rozental, Noa Korngold, Ofer Algor, Shirly Partouche, Galit Granot, Pia Raanani, Ofir Wolach.
       BACKGROUND: Glucose-6-phosphate dehydrogenase (G6PD) deficiency impairs cellular redox balance through reduced NADPH production and is the most common enzymatic disorder-causing anemia. Venetoclax combined with azacitidine (Ven-Aza) targets leukemic stem cells by disrupting oxidative phosphorylation and inducing mitochondrial stress. This study hypothesized that G6PD deficiency may enhance the efficacy of Ven-Aza in acute myeloid leukemia (AML) by reducing leukemic cell metabolic resilience.
    METHODS: The authors studied 73 consecutive patients with newly diagnosed (ND) AML treated with Ven-Aza. G6PD activity was systematically assessed at diagnosis in all patients and categorized as normal (n = 47), borderline (n = 11), or deficient (n = 15).
    RESULTS: Composite complete remission rates were 93% in the G6PD deficient group versus 69% in the normal/borderline group (p = .03). Patients with G6PD deficiency had a significantly longer median overall survival (23.8 months; 95% confidence interval [CI], 8.9-38.7), as compared to 8.96 months (95% CI, 2.9-15.0) in the normal/borderline group (p = .034). In multivariate analysis, G6PD-deficiency was associated with improved survival as compared to patients with normal G6PD activity (hazard ratio, 0.417; 95% CI, 0.181-0.965, p = .043). No significant differences were observed across groups in rates of febrile neutropenia, pneumonia, sepsis, or grade 3-4 cytopenia.
    CONCLUSION: G6PD deficiency is associated with higher response rates and improved survival in patients with ND-AML treated with Ven-Aza. These findings support G6PD deficiency as a potential biomarker of therapeutic sensitivity to Ven-AZA and may uncover metabolic vulnerabilities in AML with potential therapeutic implications.
    Keywords:  acute myeloid leukemia; azacitidine; biomarkers; glucose‐6‐phosphate dehydrogenase deficiency; survival analysis; venetoclax
    DOI:  https://doi.org/10.1002/cncr.70265
  8. Bioeng Transl Med. 2026 Jan;11(1): e70069
    Glioma chemotherapeutic resistance is tied to membrane electrophysiological properties and glycosylation.
    Alan Y L Jiang, Andrew R Yale, J Nicole Hanamoto, Nicole S Lav, Vi Phuong Dang, Clarissa C Ro, Christopher R Douglas, Kaijun Di, Jacob Deyell, Daniela A Bota, Lisa A Flanagan.
      Diffuse gliomas are brain tumors that include oligodendroglioma, astrocytoma, and glioblastoma (GBM), the most common and deadly primary brain tumor. A major challenge in glioma treatment is resistance to the first-line chemotherapeutic, temozolomide (TMZ). Plasma membrane properties of cells with increased chemotherapeutic resistance are not well understood, despite the fact that the membrane is the first point of contact with the environment and greatly shapes cell behavior. Plasma membrane glycosylation impacts cell function, and we found significant differences in glycosylation of TMZ-resistant cells. We further identified plasma membrane electrophysiological properties predicting glioma cell TMZ resistance. We enriched cells with higher TMZ resistance by sorting glioma cells based on electrophysiological properties, indicating the relevance of membrane properties to chemotherapeutic resistance. These findings could lead to rapid separation methods for patient tumor cells, a better understanding of the molecular profiles of resistant cells, and novel treatment options for gliomas.
    Keywords:  cell sorting; chemoresistance; dielectrophoresis; glioblastoma; temozolomide
    DOI:  https://doi.org/10.1002/btm2.70069
  9. Front Immunol. 2025 ;16 1734203
    NDUFS4, a mitochondrial complex I subunit, is essential for T-cell metabolic fitness and immune function.
    Oded Shamriz, Zahala Bar-On, Omri Yosef, Leonor Cohen-Daniel, Ayelet Sheer, Or Reuven, Wajeeh Salaymeh, Amijai Saragovi, Raz Somech, Atar Lev, Hagar Mor-Shaked, Yuval Tal, Aviva Fattal-Valevski, Simon Edvardson, Michael Berger.
       Introduction: Mitochondrial metabolism is essential for T-cell function, but the roles of individual electron transport chain (ETC) components are unclear. Here, we aimed to explore the role of mitochondrial complex I (CI) subunit NADH:ubiquinone oxidoreductase iron-sulfur protein 4 (NDUFS4) in T-cell metabolic fitness and immunity.
    Methods: We used a T cell-specific Ndufs4 knockout mouse model to find that NDUFS4 deficiency disrupts CI function, leading to metabolic and redox imbalances. Additionally, T cells from a patient with Leigh syndrome induced by NDUFS4 loss-of-function were analyzed.
    Results: Ndufs4-deficient T cells exhibit impaired OXPHOS, reduced respiratory capacity, and increased glycolysis, accompanied by reactive oxygen species (ROS) accumulation and defective TCR-driven activation, including reduced proliferation and cytokine production. In vivo, Ndufs4(-/-) mice show T-cell lymphopenia and impaired humoral and cytotoxic immunity. Importantly, T cells from a single Leigh syndrome patient with an NDUFS4 loss-of-function variant showed similar defects, including impaired activation and proliferation.
    Discussion: These findings highlight the importance of NDUFS4 for human immunity and establish a mechanistic link between complex I dysfunction and T-cell immunodeficiency. Our results identify NDUFS4 as a key regulator connecting mitochondrial integrity to adaptive immune function.
    Keywords:  NDUFS4; NDUFS4 knockout mice; T cells; leigh syndrome (LS); mitochondria
    DOI:  https://doi.org/10.3389/fimmu.2025.1734203
  10. JCI Insight. 2026 Jan 23. pii: e181812. [Epub ahead of print]11(2):
    NAD+ and Sirt5 restore mitochondrial bioenergetics failure and improve locomotor defects caused by sucla2 mutations.
    Joy Richard, Giulia Lizzo, Noélie Rochat, Adrien Jouary, Pedro Tm Silva, Alice Parisi, Stefan Christen, Sofia Moco, Michael B Orger, Philipp Gut.
      Mitochondria-derived acyl-coenzyme A (acyl-CoA) species chemically modify proteins, causing damage when acylation reactions are not adequately detoxified by enzymatic removal or protein turnover. Defects in genes encoding the mitochondrial respiratory complex and TCA cycle enzymes have been shown to increase acyl-CoA levels due to reduced enzymatic flux and result in proteome-wide hyperacylation. How pathologically elevated acyl-CoA levels contribute to bioenergetics failure in mitochondrial diseases is not well understood. Here, we demonstrate that bulk succinylation from succinyl-CoA excess consumes the enzymatic cofactor NAD+ and propagates mitochondrial respiratory defects in a zebrafish model of succinyl-CoA ligase deficiency, a childhood-onset encephalomyopathy. To explore this mechanism as a therapeutic target, we developed a workflow to monitor behavioral defects in sucla2-/- zebrafish and show that hypersuccinylation is associated with reduced locomotor behavior and impaired ability to execute food hunting patterns. Postembryonic NAD+ precursor supplementation restores NAD+ levels and improves locomotion and survival of sucla2-/- zebrafish. Mechanistically, nicotinamide and nicotinamide riboside require the NAD+-dependent desuccinylase Sirt5 to enhance oxidative metabolism and nitrogen elimination through the urea cycle. Collectively, NAD+ supplementation activates Sirt5 to protect against damage to mitochondria and locomotor circuits caused by protein succinylation.
    Keywords:  Cell biology; Genetic diseases; Metabolism; Mitochondria
    DOI:  https://doi.org/10.1172/jci.insight.181812
  11. Diabetes Metab J. 2026 Jan 19.
    BDH1 Protects against Diabetic Cardiomyopathy by Improving Mitochondrial Function and Suppressing Cardiomyocyte Apoptosis Via Activation of the AKT/GSK3β Pathway.
    Yan Wang, Yanan Cheng, Jianbo Wu, Yu Zhao, Di Wang, Longyan Yang, Dong Zhao.
       Background: Diabetic cardiomyopathy (DCM) is the main cause of heart failure in diabetes patients with no effective therapies currently available. A deeper understanding of the mechanisms underlying DCM is essential for identifying novel therapeutic targets.
    Methods: DCM model was established in C57BL/6J mice by administering multiple low-dose intraperitoneal injections of streptozotocin (STZ) in combination with a high-fat diet (HFD). Proteomic profiling was conducted on cardiac tissues from control and DCM mice to identify differentially expressed proteins. The expression of β-hydroxybutyrate dehydrogenase 1 (BDH1, also known as 3-hydroxybutyrate dehydrogenase) in cardiac tissues and cardiomyocyte were determined by immunoblot and quantitative polymerase chain reaction. The function and mechanism of BDH1 in DCM were investigated using a cardiac-specific BDH1-overexpressing mouse model, combined with cardiomyocyte cell lines with either BDH1 overexpression or knockdown.
    Results: BDH1 was markedly downregulated in cardiac tissues of DCM mice, as well as in cardiomyocytes treated with high glucose and palmitic acid (HGPA). Cardiac-specific overexpression of BDH1 markedly improved cardiac dysfunction and myocardial fibrosis in DCM mice. In vitro, BDH1 overexpression attenuated mitochondrial damage and inhibited apoptosis in cardiomyocytes induced by HGPA. Conversely, BDH1 knockdown exacerbated these pathological changes under HGPA conditions. Transcriptome analysis linked BDH1 expression to the phosphatidylinositol 3-kinase (PI3K)-protein kinase B (AKT) pathway, and we confirmed that BDH1 overexpression reversed diabetes-induced inhibition of the AKT/glycogen synthase kinase 3β (GSK3β) pathway. The protective effects of BDH1 on mitochondrial function and cardiomyocytes apoptosis were abolished following treatment with AKT inhibitor (AKTi). Cardiac-specific overexpression of BDH1 markedly decreased β-hydroxybutyric acid (BHB, the predominant ketone body) levels in cardiac tissues of DCM mice. Elevated BHB levels suppressed AKT activation in cardiomyocytes, while BDH1 overexpression effectively restored AKT/GSK3β pathway activity and ameliorated BHB-induced mitochondrial dysfunction and cardiomyocytes apoptosis.
    Conclusion: Our study demonstrates that BDH1 plays a protective role in DCM by regulating BHB level and activating the AKT/GSK3β pathway, thereby mitigating mitochondrial damage and cardiomyocyte apoptosis. BDH1 may be a promising therapeutic target for DCM.
    Keywords:  Diabetic cardiomyopathies; Glycogen synthase kinase 3 beta; Hydroxybutyrate dehydrogenase; Ketone bodies; Mitochondria
    DOI:  https://doi.org/10.4093/dmj.2025.0257
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