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Yaghmour, M. H.

Publications and source records attributed to Yaghmour, M. H..

2 recordsLinked to original sources

HDL-associated phosphatidylserine blunts myeloid activation and protects from atherosclerosis

Background and aimsLipids play a critical role in atherosclerosis. Low-density lipoprotein (LDL)-cholesterol and certain lipid classes like sphingomyelins are associated with inflammation and poor cardiovascular outcomes. Phosphatidylserine (PS), on the other hand, is a negatively charged anti-inflammatory phospholipid class involved in efferocytosis. In this study, we sought to investigate its anti-atherosclerotic properties through a combination of complementary human lipidomics analyses, in vitro assays and in vivo experiments in Apoe-/- mice. MethodsHuman lipidomics studies were performed on the 300OB cohort comprising 300 obese and overweight individuals at risk of cardiovascular disease. In vitro assays were carried out using human monocytes and macrophages, and in vivo experiments included histopathological, immunophenotyping and single-cell transcriptomic analyses. ResultsIn humans, we identified PS as an anti-inflammatory and atheroprotective biomarker. Hence, we developed a high-density lipoprotein (HDL)-like formulation enriched in PS to exploit its properties in a targeted fashion in mice. In vitro, this formulation potently inhibited inflammatory cytokine production on human myeloid cells. Our in-depth in vivo experiments provided evidence of the formulations potent plaque-stabilizing and anti-inflammatory actions. These effects were mediated by a shift in the monocyte/macrophage compartment toward homeostatic/repairing phenotypes. ConclusionsCollectively, our results demonstrate that HDL-associated PS potently suppresses inflammation and atheroprogression, and holds promise as a viable approach to improve immunomodulatory therapies.

immunology↗

Insulin-like peptide secretion is mediated by peroxisome-Golgi interplay

Insulin is a peptide hormone that is secreted in Golgi-derived dense-core vesicles from mammalian pancreatic beta-cells in response to nutrients. In Drosophila melanogaster, three insulin-like peptides are secreted as neuropeptides from the insulin-producing cells in the brain. Peroxisomes are lipid-metabolizing organelles that engage into various membrane contact sites with other organelles. Impaired peroxisomal metabolism has been associated with beta-cell apoptosis and impaired insulin secretion. How peroxisomes contribute to insulin and neuropeptide secretion is unknown. Here we demonstrate that peroxisomes interact with the Golgi apparatus in Drosophila insulin-producing cells. Secretion of insulin-like peptide 2 is cell-intrinsically impaired in mutants lacking the peroxisome assembly factor Pex19. Loss of peroxisomes shifts the profile of sphingolipids towards longer sphingoid bases and leads to accumulation of sphingolipids in the Golgi. We show that peroxisomes dynamically interact with the Golgi in insulin-producing cells and that Pex19 directly contributes to peroxisome-Golgi interaction via the fatty acyl-CoA reductase FAR2/waterproof in the peroxisomal membrane. We propose that this peroxisome-Pex19-Golgi axis is required to adjust Golgi membranes upon starvation by withdrawing lipids with longer side chains, thereby optimizing Golgi membrane flexibility for dense-core vesicle secretion upon refeeding.

cell biology↗