bims-lypmec Biomed News
on Lysosomal positioning and metabolism in cardiomyocytes
Issue of 2026–02–08
four papers selected by
Satoru Kobayashi, New York Institute of Technology



  1. J Neurochem. 2026 Feb;170(2): e70363
      Dysregulation of autophagy and lysosomal function is central to Parkinson's disease (PD), yet the upstream mechanisms leading to lysosomal failure remain unclear. Across primary mouse cortical neurons, MT-3 deficient primary mouse astrocytes, human iPSC-derived midbrain dopaminergic neurons, and Rho0 CHO cells lacking mitochondrial respiration, we investigated how mitochondrial stress perturbs zinc (Zn2+) homeostasis and lysosomal integrity. We identify intracellular zinc as a critical mediator linking mitochondrial dysfunction to lysosomal membrane permeabilization (LMP) and neuronal death. Inhibition of mitochondrial complex I by 1-methyl-4-phenylpyridinium (MPP+) elevated reactive oxygen species (ROS) and intracellular zinc, jointly driving LMP. Blocking either ROS or zinc markedly attenuated lysosomal damage and cell death, demonstrating that both act upstream of LMP. To define zinc regulation, we examined metallothionein-3 (MT-3), a brain-enriched zinc-binding protein. MT-3-deficient astrocytes were more vulnerable to MPP+ and zinc overload (ZnCl2) but paradoxically resistant to hydrogen peroxide (H2O2), suggesting that MT-3 buffers cytosolic zinc during mitochondrial injury or extracellular zinc influx yet can release bound zinc under oxidative conditions. Using Rho0 cells, we show that MPP+ toxicity depends on mitochondrial ROS, as loss of mitochondrial function nearly abolished cell death. However, Rho0 cells were highly sensitive to ZnCl2 and H2O2 and exhibited markedly reduced lysosomal abundance, indicating limited capacity to sequester zinc and increased susceptibility to zinc-mediated injury. These findings support a coordinated system in which lysosomes and zinc-binding proteins maintain zinc homeostasis. When cytosolic zinc rises, its accumulation within lysosomes induces LMP and accelerates cell death. Collectively, our results identify intracellular zinc as an upstream trigger of lysosomal dysfunction and neurodegeneration. Zinc-mediated LMP provides a mechanistic link between mitochondrial injury, impaired autophagic flux, and α-synuclein pathology in PD. Enhancing zinc homeostasis and lysosomal resilience may offer promising therapeutic strategies.
    Keywords:  Parkinson's disease; lysosomal membrane permeabilization (LMP); mitochondria; reactive oxygen species (ROS); zinc
    DOI:  https://doi.org/10.1111/jnc.70363
  2. FASEB J. 2026 Feb 15. 40(3): e71540
      Although extensive clinical and basic research has been conducted on diabetic cardiomyopathy (DbCM), the therapeutic efficacy for this condition remains significantly limited. Ubiquitin-specific peptidase 20 (USP20), a deubiquitinating enzyme, plays an essential role in regulating protein ubiquitination and modulating various cellular processes. In this study, we aimed to investigate the effect of USP20 on the pathogenesis of DbCM, which may provide a novel therapeutic target for its treatment. The cardiomyocyte-specific USP20 conditional knockout (USP20CKO) mice were employed in this study. The type 2 diabetes mouse model was established using db/db leptin receptor-deficient mice and high-fat diet/streptozotocin-induced mice. USP20 expression was downregulated in the myocardium of diabetic mice. Cardiomyocyte-specific USP20 deficiency aggravated cardiac remodeling and myocardial dysfunction in diabetic mice. LC-MS/MS analysis, along with Co-IP results, demonstrated the interaction between stimulator of interferon genes (STING) and USP20. In mechanism, USP20 directly binds to STING and promotes its degradation through the autophagy pathway by deubiquitinating p62 via its active site C154, thereby alleviating the myocardial inflammation and improving ventricular remodeling and heart failure induced by diabetes.
    Keywords:  Sting; USP20; deubiquitinating enzyme; diabetic cardiomyopathy; p62
    DOI:  https://doi.org/10.1096/fj.202503913R
  3. Cardiovasc Res. 2026 Jan 30. pii: cvag029. [Epub ahead of print]
       AIMS: CCAAT-enhancer-binding protein (C/EBP) β is a member of the basic leucine zipper transcription factor family that regulates cell differentiation, proliferation, cell death and survival, and inflammation. Although C/EBPβ plays both protective and detrimental roles in the heart at baseline and during stress, the cell type-specific functions of C/EBPβ in the heart are unknown. Here, we investigated the role of endogenous C/EBPβ in cardiomyocytes during pressure overload-induced heart failure.
    METHODS AND RESULTS: We found that C/EBPβ expression was reduced in wild-type (WT) mouse heart homogenates after 4 weeks of transverse aortic constriction (TAC). To elucidate the role of endogenous C/EBPβ during cardiac stress in vivo, we generated cardiomyocyte-specific Cebpb knockout (Cebpb-cKO) mice. Cebpb-cKO mice were born at a normal Mendelian ratio but displayed slightly decreased cardiac function under baseline conditions, starting at 3 months of age. Notably, in contrast to a previous report using systemic heterozygous Cebpb-knockout mice, which exhibited cardiac protection against TAC, Cebpb-cKO mice showed significantly exacerbated systolic dysfunction, cardiac hypertrophy, and fibrosis after 4 weeks of TAC. Cebpb-cKO mice also exhibited decreased expression of antioxidant genes, including Mnsod and Catalase, both at baseline and under TAC conditions. On the other hand, rescue of the C/EBPβ level in cardiomyocytes using AAV9-cTnT-Cebpb alleviated the left ventricular (LV) dysfunction in response to TAC.
    CONCLUSIONS: Our findings suggest that C/EBPβ has a cell-type specific role in the heart and that endogenous C/EBPβ in cardiomyocytes plays a salutary role during pressure overload.
    Keywords:  C/EBPβ; antioxidant; cardiomyocyte; pressure overload
    DOI:  https://doi.org/10.1093/cvr/cvag029