{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Loix M"],"funding":["Fonds Wetenschappelijk Onderzoek"],"pagination":["515"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11803036"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["79(10)"],"pubmed_abstract":["Foamy macrophages and microglia containing lipid droplets (LDs) are a pathological hallmark of demyelinating disorders affecting the central nervous system (CNS). We and others showed that excessive accumulation of intracellular lipids drives these phagocytes towards a more inflammatory phenotype, thereby limiting CNS repair. To date, however, the mechanisms underlying LD biogenesis and breakdown in lipid-engorged phagocytes in the CNS, as well as their impact on foamy phagocyte biology and lesion progression, remain poorly understood. Here, we provide evidence that LD-associated protein perilipin-2 (PLIN2) controls LD metabolism in myelin-containing phagocytes. We show that PLIN2 protects LDs from lipolysis-mediated degradation, thereby impairing intracellular processing of myelin-derived"],"journal":["Cellular and molecular life sciences : CMLS"],"pubmed_title":["Perilipin-2 limits remyelination by preventing lipid droplet degradation."],"pmcid":["PMC11803036"],"funding_grant_id":["1141920N","1S15519N"],"pubmed_authors":["Wouters E","Bogie JFJ","Loix M","Swinnen JV","Dehairs J","McManaman JL","Hendriks JJA","Vanherle S","Haidar M","Kemps H"],"additional_accession":[]},"is_claimable":false,"name":"Perilipin-2 limits remyelination by preventing lipid droplet degradation.","description":"Foamy macrophages and microglia containing lipid droplets (LDs) are a pathological hallmark of demyelinating disorders affecting the central nervous system (CNS). We and others showed that excessive accumulation of intracellular lipids drives these phagocytes towards a more inflammatory phenotype, thereby limiting CNS repair. To date, however, the mechanisms underlying LD biogenesis and breakdown in lipid-engorged phagocytes in the CNS, as well as their impact on foamy phagocyte biology and lesion progression, remain poorly understood. Here, we provide evidence that LD-associated protein perilipin-2 (PLIN2) controls LD metabolism in myelin-containing phagocytes. We show that PLIN2 protects LDs from lipolysis-mediated degradation, thereby impairing intracellular processing of myelin-derived","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Sep","modification":"2025-04-04T01:36:19.732Z","creation":"2025-04-04T01:36:19.732Z"},"accession":"S-EPMC11803036","cross_references":{"pubmed":["36100764"],"doi":["10.1007/s00018-022-04547-0"]}}