ArticleThe Journal of biological chemistry2013
Lactosylceramide interacts with and activates cytosolic phospholipase A2α.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 33 citations in OpenAlex.
- Evidence for cPLA2 activation in Alzheimer's disease synaptic pathology.Acta neuropathologica communications · 2026Article
- Glycolipids implicated as mediators of clinically visible retinal pigment epithelial migration in age-related macular degeneration.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- Review
- Convergence: Lactosylceramide-Centric Signaling Pathways Induce Inflammation, Oxidative Stress, and Other Phenotypic Outcomes.International journal of molecular sciences · 2021Review
- The Involvement of Lactosylceramide in Central Nervous System Inflammation Related to Neurodegenerative Disease.Frontiers in aging neuroscience · 2021Review
- Mitochondria as intracellular signaling platforms in health and disease.The Journal of cell biology · 2020Review
- Regulation of triglyceride metabolism in medaka (Oryzias latipes) hepatocytes by Neu3a sialidase.Fish physiology and biochemistry · 2020Article
- Article
- Recognition and protection of glycosphingolipids by synthetic nanoparticle receptors.Chemical communications (Cambridge, England) · 2019Article
- Role of Bioactive Sphingolipids in Inflammation and Eye Diseases.Advances in experimental medicine and biology · 2019Article
- Inhibition of glycosphingolipid synthesis reverses skin inflammation and hair loss in ApoE-/- mice fed western diet.Scientific reports · 2018Article
- Comparative lipid analysis in the normal and cancerous organoids of MDCK cells.Journal of biochemistry · 2016Article
- Cytosolic phospholipase A₂: physiological function and role in disease.Journal of lipid research · 2015Review
- Regulation of astrocyte activation by glycolipids drives chronic CNS inflammation.Nature medicine · 2014Article
- Role of cytosolic phospholipase A2 in oxidative and inflammatory signaling pathways in different cell types in the central nervous system.Molecular neurobiology · 2014Review
- Lactosylceramide promotes hypertrophy through ROS generation and activation of ERK1/2 in cardiomyocytes.Glycobiology · 2014Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lactosylceramide (LacCer) is a member of the glycosphingolipid family and is known to be a bioactive lipid in various cell physiological processes. However, the direct targets of LacCer and cellular events mediated by LacCer are largely unknown. In this study, we examined the effect of LacCer on the release of arachidonic acid (AA) and the activity of cytosolic phospholipase A2α (cPLA2α). In CHO-W11A cells, treatment with 1-phenyl-2-palmitoylamino-3-morpholino-1-propanol (PPMP), an inhibitor of glucosylceramide synthase, reduced the glycosphingolipid level, and the release of AA induced by A23187 or platelet-activating factor was inhibited. The addition of LacCer reversed the PPMP effect on the stimulus-induced AA release. Exogenous LacCer stimulated the release of AA, which was decreased by treatment with an inhibitor of cPLA2α or silencing of the enzyme. Treatment of CHO-W11A cells with LacCer induced the translocation of full-length cPLA2α and its C2 domain from the cytosol to the Golgi apparatus. LacCer also induced the translocation of the D43N mutant of cPLA2α. Treatment of L929 cells with TNF-α induced LacCer generation and mediated the translocation of cPLA2α and AA release, which was attenuated by treatment with PPMP. In vitro studies were then conducted to test whether LacCer interacts directly with cPLA2α. Phosphatidylcholine vesicles containing LacCer increased cPLA2α activity. LacCer bound to cPLA2α and its C2 domain in a Ca(2+)-independent manner. Thus, we propose that LacCer is a direct activator of cPLA2α.
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