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Yidenk, M.

Publications and source records attributed to Yidenk, M..

2 recordsLinked to original sources

Loss of Nuclear TDP-43 Impairs Lipid Metabolism in Microglia-Like Cells

Amyotrophic lateral sclerosis (ALS) is a fatal neurodegenerative disease marked by progressive motor neuron loss, with TDP-43 pathology present in over 90% of cases. While neuroinflammation is a recognized hallmark, the role of microglia in ALS pathogenesis remains incompletely understood. Here, we demonstrate that TDP-43 regulates microglial function via triglyceride metabolism. Using shRNA-mediated TARDBP knockdown in human monocyte-derived microglia-like cells (MDMi), we observed suppressed cholesterol biosynthesis, upregulation of fatty acid metabolism genes, lipid droplet accumulation, enhanced phagocytic activity, and increased IL-1{beta} production. Inhibiting diacylglycerol acyltransferase (DGAT) enzymes reduced lipid droplet formation, phagocytosis, and IL-1{beta}, directly linking the triglyceride pathway to microglial activation. Patient-derived MDMi from both sporadic and TARDBP-mutant ALS cases showed overlapping as well as distinct alterations, some of which were reversed by DGAT inhibition. Our findings identify dysregulated triglyceride metabolism as a novel pathway through which TDP-43 mediates microglial dysfunction, highlighting a potential therapeutic target for ALS. Graphical Abstract O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=130 SRC="FIGDIR/small/676815v1_ufig1.gif" ALT="Figure 1"> View larger version (52K): org.highwire.dtl.DTLVardef@f10b2dorg.highwire.dtl.DTLVardef@114d48forg.highwire.dtl.DTLVardef@8f25f9org.highwire.dtl.DTLVardef@63309_HPS_FORMAT_FIGEXP M_FIG C_FIG HighlightsO_LITDP-43 nuclear depletion causes increased LD, driven by triglyceride accumulation. C_LIO_LITDP-43 nuclear depletion causes increased phagocytosis and pro-inflammatory cytokine expression. C_LIO_LIInhibiting triglyceride synthesis using DGAT inhibitors rescues LD and pro-inflammatory phenotype in TDP-43 depleted MDMi C_LIO_LIALS patient-derived MDMi display increased LD and IL1B expression, rescued by DGAT inhibitors C_LI

neuroscience↗

IL-1RA Disrupts ATP Activation of P2RX7 in Human Monocyte-Derived Microglia-like Cells

The immune system has a dynamic role in neurodegenerative diseases, and purinergic receptors allow immune cells to recognize neuronal signaling, cell injury, or stress. Purinergic Receptor 7 (P2RX7) can modulate inflammatory cascades and its expression is upregulated in Alzheimers disease (AD) brain tissue. P2RX7 expression is enriched in microglia, and elevated levels are found in microglia surrounding amyloid-beta plaques in the brain. While P2RX7 is thought to play a role in neurodegenerative diseases, how it modulates pathology and disease progression is not well understood. Here, we utilize a human monocyte-derived microglia-like cell (MDMi) model to interrogate P2RX7 activation and downstream consequences on microglia function. By using MDMi derived from human donors, we can examine how human donor variation impacts microglia function. We assessed P2RX7-driven IL1{beta} and IL18 production and amyloid-beta peptide 1-42 (A{beta}1-42) uptake levels. Our results show that ATP-stimulation of MDMi triggers upregulation of IL1{beta} and IL18 expression. This upregulation of cytokine gene expression is blocked with the A740003 P2RX7 antagonist. We find that high extracellular ATP conditions also reduced MDMi capacity for A{beta}1-42 uptake, and this loss of function is prevented through A740003 inhibition of P2RX7. In addition, pretreatment of MDMi with IL-1RA limited ATP-driven IL1{beta} and IL18 gene expression upregulation, indicating that ATP immunomodulation of P2RX7 is IL-1R dependent. A{beta}1-42 uptake was higher with IL-1RA pretreatment compared to ATP treatment alone, suggesting P2RX7 regulates phagocytic engulfment through IL-1 signaling. Overall, our results demonstrate that P2RX7 is a key response protein for high extracellular ATP in human microglia-like cells, and its function can be modulated by IL-1 signaling. This work opens the door to future studies examining anti-IL-1 biologics to increase the clearance of amyloid-beta.

immunology↗