GEOapplication/xmlftp://ftp.ncbi.nlm.nih.gov/geo/series/GSE341nnn/GSE341595/primaryOK200TranscriptomicsMus musculusExpression profiling by high throughput sequencinghttps://www.ncbi.nlm.nih.gov/geo/query/acc.cgi?acc=GSE341595GEOGSEfalseAlox15 restrains glycolysis to support M2 macrophage effector function during helminth immunity.Macrophage polarization by type-2 cytokines is central to anti-helminth immunity and tissue repair. While some hallmark changes in macrophages are well-characterized and associated with protection against helminths, it is still unclear how macrophages exert their anti-helminth effects. In this context, we investigated Arachidonate 15-lipoxygenase (Alox15), a lipoxygenase well known for its role in macrophage polarization in the context of metabolic diseases, and a hallmark of type-2 macrophage (M2) human polarization. We show that in the absence of Alox15, M2 cannot trap and kill helminths. Surprisingly, expression of M2 markers was normal despite a loss of function. Instead, we found a concomitant increase in pro-inflammatory responses due to an uncontrolled activation of glycolysis. We further show that activation of Peroxisome proliferator-activated receptor-delta (PPAR-δ) by lipids downstream of Docosapentaenoic acid (DPA) can restore normal glycolysis control, highlighting a novel role of lipids in the fine-tuning of the metabolic support required for optimal macrophage polarization.2026/08/25GSE341595GSM9913739GSM9913717GSM9913718GSM9913737GSM9913715GSM9913716GSM9913738GSM9913719GSM9913753GSM9913731GSM9913732GSM9913751GSM9913730GSM9913752GSM9913735GSM9913736GSM9913714GSM9913733GSM9913734GSM9913750GSM9913728GSM9913729GSM9913748GSM9913726GSM9913749GSM9913727GSM9913742GSM9913720GSM9913743GSM9913721GSM9913740GSM9913741GSM9913746GSM9913724GSM9913725GSM9913747GSM9913722GSM9913744GSM9913745GSM991372330215341595Mus musculus