ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2026
β-Adducin Restrains PLA2G4A-Dependent Lysosomal Membrane Permeabilization and Neuronal Death in Ischemic Stroke.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Failure to preserve vulnerable neurons in the ischemic penumbra remains a barrier in ischemic stroke. Lysosomal membrane permeabilization (LMP) is increasingly recognized as a critical event in ischemic neuronal death, yet the endogenous mechanisms that preserve lysosomal integrity remain poorly defined. Here, we identify β-adducin (Add2) as an endogenous protector of lysosomal homeostasis in ischemic neurons. We found that β-adducin was markedly reduced in neurons after cerebral ischemia in both middle cerebral artery occlusion and oxygen-glucose deprivation/reoxygenation models. Neuron-specific knockdown of Add2 increased infarct volume, worsened neurological deficits, and enhanced neuronal apoptosis. Mechanistically, β-adducin interacted with cytosolic phospholipase A2 group IVA (PLA2G4A) and restricted its accumulation on lysosomes. Loss of β-adducin enhanced lysosomal localization of PLA2G4A, promoted LMP, increased cytosolic leakage of cathepsins, and exacerbated neuronal injury, whereas silencing PLA2G4A attenuated these effects. Upstream, ischemic stress reduced FTO expression, increased N
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