ArticleJournal of cell science2016
Degradation of aggregated LDL occurs in complex extracellular sub-compartments of the lysosomal synapse.
Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Protocol for the quantification of digestive exophagy in cell culture.STAR protocols · 2026Article
- Biopersistence of man-made vitreous fibres (MMVF) / synthetic vitreous fibres (SVF): advancing from animal models to acellular testing.Particle and fibre toxicology · 2025Review
- High-Content Microscopy Drug Screening Platform for Regulators of the Extracellular Digestion of Lipoprotein Aggregates by Macrophages.ACS pharmacology & translational science · 2025Article
- Microglia degrade Alzheimer's amyloid-beta deposits extracellularly via digestive exophagy.Cell reports · 2024Article
- Signaling pathways regulating the extracellular digestion of lipoprotein aggregates by macrophages.Molecular biology of the cell · 2024Article
- The formation and consequences of cholesterol-rich deposits in atherosclerotic lesions.Frontiers in cardiovascular medicine · 2023Review
- Smooth Muscle Cell-Macrophage Interactions Leading to Foam Cell Formation in Atherosclerosis: Location, Location, Location.Frontiers in physiology · 2022Review
- Modified Lipoproteins Induce Arterial Wall Inflammation During Atherogenesis.Frontiers in cardiovascular medicine · 2022Review
- Pathways and Mechanisms of Cellular Cholesterol Efflux-Insight From Imaging.Frontiers in cell and developmental biology · 2022Review
- Lipolysis: cellular mechanisms for lipid mobilization from fat stores.Nature metabolism · 2021Review
- Remodeling of Macrophages in White Adipose Tissue under the Conditions of Obesity as well as Lipolysis.Oxidative medicine and cellular longevity · 2021Review
- Native and oxidised lipoproteins negatively regulate the serum amyloid A-induced NLRP3 inflammasome activation in human macrophages.Clinical & translational immunology · 2021Article
- Article
- Digestive exophagy: Phagocyte digestion of objects too large for phagocytosis.Traffic (Copenhagen, Denmark) · 2020Review
- TLR4 (Toll-Like Receptor 4)-Dependent Signaling Drives Extracellular Catabolism of LDL (Low-Density Lipoprotein) Aggregates.Arteriosclerosis, thrombosis, and vascular biology · 2020Article
- Review
- High-density lipoprotein or cyclodextrin extraction of cholesterol from aggregated LDL reduces foam cell formation.Journal of cell science · 2019Article
- Functional Characterization of LIPA (Lysosomal Acid Lipase) Variants Associated With Coronary Artery Disease.Arteriosclerosis, thrombosis, and vascular biology · 2019Article
- Cysteamine inhibits lysosomal oxidation of low density lipoprotein in human macrophages and reduces atherosclerosis in mice.Atherosclerosis · 2019Article
- Dynamic Actin Reorganization and Vav/Cdc42-Dependent Actin Polymerization Promote Macrophage Aggregated LDL (Low-Density Lipoprotein) Uptake and Catabolism.Arteriosclerosis, thrombosis, and vascular biology · 2019Article
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Authors and funding
6 authors.
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Abstract
Monocyte-derived cells use an extracellular, acidic, lytic compartment (a lysosomal synapse) for initial degradation of large objects or species bound to the extracellular matrix. Akin to osteoclast degradation of bone, extracellular catabolism is used by macrophages to degrade aggregates of low density lipoprotein (LDL) similar to those encountered during atherogenesis. However, unlike osteoclast catabolism, the lysosomal synapse is a highly dynamic and intricate structure. In this study, we use high resolution three dimensional imaging to visualize compartments formed by macrophages to catabolize aggregated LDL. We show that these compartments are topologically complex, have a convoluted structure and contain sub-regions that are acidified. These sub-regions are characterized by a close apposition of the macrophage plasma membrane and aggregates of LDL that are still connected to the extracellular space. Compartment formation is dependent on local actin polymerization. However, once formed, compartments are able to maintain a pH gradient when actin is depolymerized. These observations explain how compartments are able to maintain a proton gradient while remaining outside the boundaries of the plasma membrane.
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