ArticleJournal of bioenergetics and biomembranes2026
Epigenetic activation of PDLIM7 via H3K27 acetylation mitigates neuroinflammation and neurodegeneration in parkinson's disease models.
Article in Journal of bioenergetics and biomembranes, 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
This study investigates the role and regulatory mechanisms of PDZ and LIM domain protein 7 (PDLIM7) in the pathology of Parkinson’s disease (PD) and evaluates its potential as a therapeutic target, specifically focusing on epigenetic regulation through histone acetylation. We investigated PDLIM7 expression and regulatory mechanisms in PD using a multi-level strategy that combined bioinformatics analysis, postmortem human substantia nigra tissues, and 6-hydroxydopamine (6-OHDA)-induced PD models in mice and cell lines. Utilizing functional tests, such as immunohistochemistry (IHC), ubiquitination analysis, chromatin immunoprecipitation (ChIP), co-immunoprecipitation (Co-IP), and immunofluorescence (IF), the epigenetic and post-translational regulation of PDLIM7 was examined. Motor behavior was assessed using rotarod and pole tests. Additionally, we evaluated the therapeutic potential of N-(4-chloro-3-trifluoromethyl-phenyl)-2-ethoxybenzamide (CTPB), a histone acetyltransferase (HAT) activator, in modulating PDLIM7 expression and attenuating neuroinflammatory responses, both in vitro and in vivo. PDLIM7 was remarkably downregulated in PD tissues and models. Overexpression of PDLIM7 mitigated α-synuclein aggregation, restored tyrosine hydroxylase (TH) expression, reduced glial activation as shown by IHC and IF markers including TH and glial fibrillary acidic protein (GFAP), and improved motor performance in 6-OHDA-lesioned mice. Mechanistically, histone H3 lysine 27 acetylation (H3K27ac) mediated by cyclic AMP response element-binding protein (CBP)/p300 regulated PDLIM7 transcription, and CTPB treatment enhanced PDLIM7 expression and rescued neuronal apoptosis and PD phenotypes. Furthermore, PDLIM7 promoted the ubiquitination and degradation of p65, suppressing nuclear factor kappaB (NF-κB)-driven expression of pro-inflammatory cytokines including interleukin (IL)-6 and IL-1β, and thereby attenuating neuroimmune dysregulation. PDLIM7 acts as an epigenetic-immune regulator in PD by linking H3K27ac to NF-κB inhibition. Targeting the CBP/p300-H3K27ac-PDLIM7 pathway may alleviate neuroinflammation and deficiencies in motor skills in PD.
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