bims-miptne Biomed News
on Mitochondrial permeability transition pore-dependent necrosis
Issue of 2026–02–01
nine papers selected by
Oluwatobi Samuel Adegbite, University of Liverpool



  1. Cells. 2026 Jan 19. pii: 179. [Epub ahead of print]15(2):
      Hyperphosphorylated collapsin response mediator protein 2 (CRMP2) is elevated in the cerebral cortex of an APP-SAA knock-in mouse model of Alzheimer's disease and binds the adenine nucleotide translocase (ANT) in a phosphorylation-dependent manner. We propose that, in Alzheimer's disease (AD) mitochondria, dissociation of hyperphosphorylated CRMP2 from ANT promotes opening of the permeability transition pore (PTP). We showed that purified ANT, when reconstituted into giant liposomes, forms large calcium-dependent channels resembling the PTP, which are effectively blocked by recombinant, unphosphorylated CRMP2. In synaptic mitochondria isolated from the cortices of APP-SAA knock-in mice and control B6J hAbeta mice, we observed an increased susceptibility to permeability transition pore (PTP) induction in AD mitochondria, accompanied by reduced viability of cultured cortical neurons. Pre-treatment of AD mice with the CRMP2-binding small molecule (S)-lacosamide ((S)-LCM), which prevents CRMP2 hyperphosphorylation and restores its interaction with ANT, attenuated PTP induction and improved neuronal viability. Interestingly, direct application of (S)-LCM to isolated mitochondria failed to suppress PTP induction, indicating that its protective effect requires upstream cellular mechanisms. These findings support a phosphorylation-dependent role for CRMP2 in regulating PTP induction in AD mitochondria and highlight (S)-LCM as a promising therapeutic candidate for mitigating mitochondrial dysfunction and enhancing neuronal viability in AD.
    Keywords:  (S)-lacosamide; Alzheimer’s disease; CRMP2; adenine nucleotide translocase; cortical neurons; mitochondria; permeability transition pore
    DOI:  https://doi.org/10.3390/cells15020179
  2. Curr Protein Pept Sci. 2026 Jan 22.
      Apoptosis, drug resistance, and cellular metabolism are all crucially regulated by mitochondria, especially through ion channels and translocases embedded in their membranes. The outer mitochondrial membrane (OMM) contains the voltage dependent anion channel (VDAC), which acts with proteins such as hexokinase II and BAX to regulate apoptosis and metabolic reprogramming in cancer while facilitating the flow of important metabolites and ions. Anti apoptotic proteins like Bcl2 and Mcl1 closely regulate the mitochondrial apoptosis induced channel (MAC), which is created by pro-apoptotic Bcl2 family members BAX and BAK and controls cytochrome c release when overexpressed, leading to drug resistance. Furthermore, the translocase of the outer membrane (TOM) complex, which regulates mitochondrial protein import, is frequently dysregulated in cancers. Numerous ion channels, such as potassium channels, the mitochondrial calcium uniporter (MCU), and the mitochondrial permeability transition pore (m-PTP), are found within the inner mitochondrial membrane (IMM) and regulate important functions like ATP synthesis, the control of reactive oxygen species (ROS), and apoptotic signaling. Cancer cells can avoid apoptosis, adapt to environmental stress, and become resistant to treatments like doxorubicin and cisplatin when these channels are dysregulated. Metabolic flexibility and antioxidant defense are improved by overexpressing or functionally modifying IMM potassium channels and calcium transporters. Additionally, drug resistance is facilitated by increased mitophagy and anti-apoptotic proteins that inhibit m-PTP opening. This review discusses the functions of mitochondrial ion channels.
    Keywords:  Apoptosis; cancer; cellular metabolism.; drug resistance; ion channels; mitochondria
    DOI:  https://doi.org/10.2174/0113892037410334251021155546
  3. Biomolecules. 2026 Jan 20. pii: 171. [Epub ahead of print]16(1):
      Mitochondrial Ca2+ signaling is increasingly recognized as a key integrator of synaptic activity, metabolism, and redox balance within the tripartite synapse. At excitatory synapses, Ca2+ influx through ionotropic glutamate receptors and voltage-gated channels is sensed and transduced by strategically positioned mitochondria, whose Ca2+ uptake and release tune tricarboxylic acid cycle activity, adenosine triphosphate synthesis, and reactive oxygen species (ROS) generation. Through these Ca2+-dependent processes, mitochondria are proposed to help set the threshold at which glutamatergic activity supports synaptic plasticity and homeostasis or, instead, drives hyperexcitability and excitotoxic stress. Here, we synthesize how mitochondrial Ca2+ dynamics in presynaptic terminals, postsynaptic spines, and perisynaptic astrocytic processes regulate glutamate uptake, recycling, and release, and how subtle impairments in these pathways may prime synapses for failure well before overt energetic collapse. We further examine the reciprocal interplay between Ca2+-dependent metabolic adaptations and glutamate homeostasis, the crosstalk between mitochondrial Ca2+ and ROS signals, and the distinct vulnerabilities of neuronal and astrocytic mitochondria. Finally, we discuss how disruption of this Ca2+-centered mitochondria-glutamatergic axis contributes to synaptic dysfunction and circuit vulnerability in neurodegenerative diseases, with a particular focus on Alzheimer's disease.
    Keywords:  Alzheimer’s disease; astrocyte–neuron communication; excitotoxicity; glutamate homeostasis; glutamatergic synapse; metabolic coupling; mitochondrial Ca2+ signaling; mitochondrial signaling; neuronal hyperexcitability; synaptic vulnerability
    DOI:  https://doi.org/10.3390/biom16010171
  4. Aging Cell. 2026 Feb;25(2): e70388
      Heart disease is the leading cause of death in the elderly population. Age-related heart failure is frequently associated with energy deficits in cardiomyocytes. These cells rely on their abundant, cristae-rich mitochondria for ATP production. ATP synthase, localized along the cristae rims, is central to this process. It is presumed that its function is tightly bound to its spatial organization, but details remain unclear. Here, we explored the spatiotemporal organization of ATP synthase in senescent human iPSC-derived CM in conjunction with its functions. We found changes in the stoichiometry of F1 and FO subunits in senescent CM. The ratio of FO-SU c to F1-SU β increased. The oligomeric organization of the complex was weakened. Using single-molecule localization and tracking microscopy, we observed an increased enzyme mobility within cristae that displayed increased fenestrations. This coincided with decreased mitochondrial ATP level, increased ATP hydrolysis capacity, and a moderate increase in mitochondrial transition pore opening. Disturbed ATP production was correlated with dysregulated calcium dynamics, characterized by heightened spikes and slower cytosolic clearance. Consequently, senescent cardiomyocytes exhibited irregular autonomous and paced beating patterns. These findings indicate that, in senescent cardiomyocytes, functional decline is closely linked to disrupted ATP metabolism, driven by the aberrant organization, dynamics, and activity of ATP synthase within remodeled cristae.
    Keywords:  ATP hydrolysis; ATP synthase organization; calcium dynamics; cardiomyocytes; contractility; cristae architecture; human induced pluripotent stem cells; mitochondrial permeability transition pore (mPTP); senescence; single molecule dynamics
    DOI:  https://doi.org/10.1111/acel.70388
  5. Int J Mol Sci. 2026 Jan 20. pii: 1007. [Epub ahead of print]27(2):
      Acetyl phosphate (AcP) is a microbial metabolite acting as a link between cell metabolism and signaling, providing the survival of bacteria in the host. AcP was also identified as an intermediate of pyruvate oxidation in mammalian mitochondria and was found in the human blood in some severe pathologies. The possible contribution of circulating AcP to the maintenance of the physiological or pathological states of the body has not been studied. Since AcP can function as a donor of phosphate groups, we have examined in vitro the influence of AcP on calcium signaling in mitochondria and cells by measuring the membrane potential and the calcium retention capacity of mitochondria by selective electrodes and by assaying the cell calcium signaling by Fura-2AM fluorescent radiometry. AcP was shown to induce a concentration-dependent increase in the mitochondrial resistance to calcium ion loading both in the control and in the presence of ADP. This effect was especially pronounced when mitochondria were incubated in a phosphate-free medium; under these conditions, AcP strongly raised the membrane potential and increased the rate of calcium uptake and the calcium retention capacity several times. Moreover, AcP induced similar changes in human cells when calcium signaling was activated by ATP, to a greater extent in neuroblastoma cells than in astrocytes. In the presence of AcP, a tendency for an increase in the amplitude and a decrease in the continuance of the ATP-induced calcium response was observed. These changes are probably associated with the activation of calcium buffering by mitochondria due to the delivery of phosphate during the hydrolysis of AcP. The results show that AcP is involved in the regulation of the Ca2+ balance in cells by activating the accumulation of calcium ions by mitochondria, especially under phosphate deficiency. A shift in calcium signaling mediated by AcP supplementation may be caused by hyperphosphatemia, which is now considered as one of basic contributors to cellular dysfunction and progression of various diseases, including sepsis.
    Keywords:  acetyl phosphate; astrocytes; calcium; hyperphosphatemia; mitochondria; mitochondrial permeability transition pore; neuroblastoma cells; purinergic signaling; sepsis
    DOI:  https://doi.org/10.3390/ijms27021007
  6. Cardiovasc Res. 2026 Jan 28. pii: cvag031. [Epub ahead of print]
       BACKGROUND: Succinate accumulates significantly during myocardial ischemia, and its rapid oxidation upon reperfusion is a critical driver of ischemia/reperfusion (I/R) injury. The transport of succinate across the mitochondrial inner membrane, particularly by the dicarboxylate carrier (DIC; SLC25A10), is hypothesized to play a crucial role in mediating these pathological succinate dynamics. However, tools to test this hypothesis by modulating mitochondrial succinate transport in biological systems are lacking.
    METHODS AND RESULTS: C57BL/6J mice, isolated Wistar Rat heart mitochondria, bovine heart mitochondrial membranes, C2C12 mouse myoblasts and primary adult cardiomyocytes were used as in vitro and in vivo models. Butylmalonate prodrugs were synthesized and tested. Isolated mitochondria were used to assess succinate-dependent respiration and reactive oxygen species (ROS) production. Cells were treated with succinate dehydrogenase (SDH) inhibitors or exposed to anoxia and butylmalonate esters. Mouse hearts were subjected to in vivo left anterior descending coronary artery ligation. Succinate and butylmalonate levels were measured by targeted liquid chromatography-tandem mass spectrometry, and infarct size by TTC (2,3,5-triphenyl-2H-tetrazolium chloride) staining.Knockdown of DIC, but not of the oxoglutarate carrier OGC, in C2C12 cells prevented succinate accumulation by SDH inhibition and anoxia. The only extant DIC inhibitor butylmalonate, is limited by poor cell permeability. We synthesized diacetoxymethyl butylmalonate (DAB), which efficiently delivers butylmalonate intramitochondrially in isolated heart mitochondria and cells. DAB inhibited succinate-dependent respiration and ROS production. DAB prevented succinate accumulation in cells treated with SDH inhibitors. DAB delivered butylmalonate to cardiac mitochondria when administered to mice in vivo and reduced infarct size by perturbing mitochondrial succinate transport.
    CONCLUSIONS: The DIC is a key node in the cellular distribution of succinate, controlling its transport between mitochondria and the cytosol. These findings highlight the potential of DIC as a promising therapeutic target for conditions where succinate elevation contributes to pathogenesis, such as cardiac I/R injury.
    Keywords:  SLC25A10; Succinate; butylmalonate; ischemia/reperfusion injury; mitochondrial dicarboxylate carrier; mitochondrial transport; myocardial infarction
    DOI:  https://doi.org/10.1093/cvr/cvag031
  7. Int J Mol Sci. 2026 Jan 22. pii: 1123. [Epub ahead of print]27(2):
      The BCL-2 family of proteins plays a central role in the regulation of apoptosis, with BCL-2 and BCL-xL representing two of its most prominent antiapoptotic members. This review explores the molecular regulation of BCL-2 and BCL-xL genes, emphasizing the structural domains that define the functions of the broader BCL-2 family. Beyond their canonical roles in preventing mitochondrial outer membrane permeabilization, both proteins contribute significantly to cancer development. Their overexpression enhances invasiveness and tumor progression, supports angiogenesis, and critically modulates cellular responses to chemotherapy, often conferring drug resistance. Additional non-apoptotic functions, including roles in metabolism, mitochondrial dynamics, and cellular homeostasis, further expand their biological relevance. Clinical trials exploring strategies to inhibit BCL-2 and BCL-xL, including selective BH3 mimetics and combination regimens, are discussed with emphasis on their potential and limitations in oncology. Overall, this review highlights the multifaceted contributions of BCL-2 and BCL-xL to cancer biology and underscores the importance of continued efforts to refine targeted therapeutic approaches.
    Keywords:  BCL-2; BCL-xL; BH3 mimetics; apoptosis regulation; cancer progression; drug resistance; therapeutic targeting
    DOI:  https://doi.org/10.3390/ijms27021123
  8. Mitochondrion. 2026 Jan 25. pii: S1567-7249(26)00005-X. [Epub ahead of print] 102115
      In recent years, PANoptosis, as a novel form of cell death that integrates multiple cell death pathways, has progressively emerged as a cutting-edge research field in the study of cell death and immune regulation. PANoptosis, a recently proposed form of inflammatory programmed cell death, integrates features of pyroptosis, apoptosis, and necroptosis, while emphasizing their interplay. It is mediated by the PANoptosome and plays a pivotal role in infections, inflammation, tumors, and degenerative diseases. Recent studies have demonstrated that ROS serve as critical signaling molecules for PANoptosome assembly. Given that mitochondria constitute the primary intracellular source of ROS, this establishes a crucial link between mitochondrial and PANoptosis activation. Mitochondria sustain energy production, calcium homeostasis, and signaling but also contribute to immune responses and cell death. Oxidative stress, obesity, and environmental pollutants can induce mitochondrial dysfunction, manifested through impaired mitochondrial dynamics, which subsequently leads to excessive ROS production and mtDNA leakage. These pathological changes ultimately trigger PANoptosis activation. This review systematically summarizes how mitochondrial dysfunction triggers PANoptosis through mechanisms such as ROS accumulation, aberrant mitochondrial dynamics, and mtDNA leakage. Furthermore, it explores the implications of this process in traumatic brain injury, inflammatory diseases, ischemic disorders, and diseases induced by environmental toxins (e.g., microplastics and heavy metals). Understanding the interplay between mitochondria and PANoptosis may provide critical insights into the pathogenesis of inflammation-related diseases and offer novel mitochondria-targeted therapeutic strategies.
    Keywords:  Mitochondrial DNA; Mitochondrial dynamics; Mitochondrial dysfunction; PANoptosis; PANoptosome; Reactive oxygen species
    DOI:  https://doi.org/10.1016/j.mito.2026.102115
  9. J Physiol. 2026 Jan 28.
      Cardiovascular diseases remain the leading cause of mortality worldwide, driven by complex, multiscale mechanisms that span molecular, cellular and organ-level dysfunction. Effective therapeutic strategies therefore require integrative approaches that link fundamental biology to translational applications. The 8th UC Davis CardioVascular Symposium gathered experts in ion channel biophysics, Ca2+ signalling, arrhythmia mechanisms and cardiovascular physiology to discuss recent advances and define emerging priorities. This white paper synthesizes the key themes and consensus points that emerged, highlighting progress in two core domains: (1) advances in cardiovascular electrophysiology and arrhythmia mechanisms, and (2) spatiotemporal dynamics of Ca2+ signalling in cardiac and vascular function and remodelling. We also identify conceptual and technical challenges that must be addressed to accelerate therapeutic discovery and emphasize cross-cutting opportunities where experimental and computational approaches can converge. By integrating ion channel biology and Ca2+ signalling mechanisms across scales, this work outlines new directions for advancing cardiovascular research and treatment.
    Keywords:  arrhythmia; calcium dynamics; calcium signalling; cardiovascular disease; ion channels
    DOI:  https://doi.org/10.1113/JP290180