{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["10"],"submitter":["Monks J"],"pubmed_abstract":["Secretory epithelial cells (sMEC) in mammary glands of lactating animals secrete lipids by a novel apocrine mechanism in which cytoplasmic lipid droplets (LD) contact and are enveloped by elements of the apical plasma membrane (APM) before being released into the lumen of the gland as membrane bound structures. The molecular properties of LD-APM contacts and the mechanisms regulating LD membrane envelopment and secretion are not fully understood. Perilipin-2 (Plin2) is a constitutive LD protein that has been proposed to tether LD to the APM through formation of a complex with the transmembrane protein, butyrophilin1a1 (BTN) and the redox enzyme, xanthine oxidoreductase (XOR). Using mice lacking Plin2 and physiological inhibition of apocrine lipid secretion, we demonstrate that LD-APM conta"],"journal":["Frontiers in cell and developmental biology"],"pagination":["958566"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9500548"],"repository":["biostudies-literature"],"pubmed_title":["Perilipin-2 promotes lipid droplet-plasma membrane interactions that facilitate apocrine lipid secretion in secretory epithelial cells of the mouse mammary gland."],"pmcid":["PMC9500548"],"pubmed_authors":["Monks J","Dzieciatkowska M","Libby AE","McManaman JL","Ladinsky MS","Orlicky DJ"],"additional_accession":[]},"is_claimable":false,"name":"Perilipin-2 promotes lipid droplet-plasma membrane interactions that facilitate apocrine lipid secretion in secretory epithelial cells of the mouse mammary gland.","description":"Secretory epithelial cells (sMEC) in mammary glands of lactating animals secrete lipids by a novel apocrine mechanism in which cytoplasmic lipid droplets (LD) contact and are enveloped by elements of the apical plasma membrane (APM) before being released into the lumen of the gland as membrane bound structures. The molecular properties of LD-APM contacts and the mechanisms regulating LD membrane envelopment and secretion are not fully understood. Perilipin-2 (Plin2) is a constitutive LD protein that has been proposed to tether LD to the APM through formation of a complex with the transmembrane protein, butyrophilin1a1 (BTN) and the redox enzyme, xanthine oxidoreductase (XOR). Using mice lacking Plin2 and physiological inhibition of apocrine lipid secretion, we demonstrate that LD-APM conta","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022","modification":"2025-04-21T14:30:06.091Z","creation":"2025-04-21T14:30:06.091Z"},"accession":"S-EPMC9500548","cross_references":{"pubmed":["36158190"],"doi":["10.3389/fcell.2022.958566"]}}