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Article

Cellular Plasmalogen Content Does Not Influence Arachidonic Acid Levels or Distribution in Macrophages: A Role for Cytosolic Phospholipase A2γ in Phospholipid Remodeling

1
Instituto de Biología y Genética Molecular, Consejo Superior de Investigaciones Científicas (CSIC), Universidad de Valladolid, 47003 Valladolid, Spain
2
Centro de Investigación Biomédica en Red de Diabetes y Enfermedades Metabólicas Asociadas (CIBERDEM), 28029 Madrid, Spain
3
Department of Chemistry, National and Kapodistrian University of Athens, Panepistimiopolis, 15771 Athens, Greece
*
Author to whom correspondence should be addressed.
Cells 2019, 8(8), 799; https://doi.org/10.3390/cells8080799
Received: 11 July 2019 / Revised: 26 July 2019 / Accepted: 30 July 2019 / Published: 31 July 2019
(This article belongs to the Special Issue Phospholipids: Dynamic Lipid Signaling in Health and Diseases)
Availability of free arachidonic acid (AA) constitutes a rate limiting factor for cellular eicosanoid synthesis. AA distributes differentially across membrane phospholipids, which is largely due to the action of coenzyme A-independent transacylase (CoA-IT), an enzyme that moves the fatty acid primarily from diacyl phospholipid species to ether-containing species, particularly the ethanolamine plasmalogens. In this work, we examined the dependence of AA remodeling on plasmalogen content using the murine macrophage cell line RAW264.7 and its plasmalogen-deficient variants RAW.12 and RAW.108. All three strains remodeled AA between phospholipids with similar magnitude and kinetics, thus demonstrating that cellular plasmalogen content does not influence the process. Cell stimulation with yeast-derived zymosan also had no effect on AA remodeling, but incubating the cells in AA-rich media markedly slowed down the process. Further, knockdown of cytosolic-group IVC phospholipase A2γ (cPLA2γ) by RNA silencing significantly reduced AA remodeling, while inhibition of other major phospholipase A2 forms such as cytosolic phospholipase A2α, calcium-independent phospholipase A2β, or secreted phospholipase A2 had no effect. These results uncover new regulatory features of CoA-IT-mediated transacylation reactions in cellular AA homeostasis and suggest a hitherto unrecognized role for cPLA2γ in maintaining membrane phospholipid composition via regulation of AA remodeling. View Full-Text
Keywords: arachidonic acid; eicosanoids; inflammation; phospholipid remodeling; phospholipase A2; monocytes/macrophages arachidonic acid; eicosanoids; inflammation; phospholipid remodeling; phospholipase A2; monocytes/macrophages
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MDPI and ACS Style

Lebrero, P.; Astudillo, A.M.; Rubio, J.M.; Fernández-Caballero, L.; Kokotos, G.; Balboa, M.A.; Balsinde, J. Cellular Plasmalogen Content Does Not Influence Arachidonic Acid Levels or Distribution in Macrophages: A Role for Cytosolic Phospholipase A2γ in Phospholipid Remodeling. Cells 2019, 8, 799. https://doi.org/10.3390/cells8080799

AMA Style

Lebrero P, Astudillo AM, Rubio JM, Fernández-Caballero L, Kokotos G, Balboa MA, Balsinde J. Cellular Plasmalogen Content Does Not Influence Arachidonic Acid Levels or Distribution in Macrophages: A Role for Cytosolic Phospholipase A2γ in Phospholipid Remodeling. Cells. 2019; 8(8):799. https://doi.org/10.3390/cells8080799

Chicago/Turabian Style

Lebrero, Patricia, Alma M. Astudillo, Julio M. Rubio, Lidia Fernández-Caballero, George Kokotos, María A. Balboa, and Jesús Balsinde. 2019. "Cellular Plasmalogen Content Does Not Influence Arachidonic Acid Levels or Distribution in Macrophages: A Role for Cytosolic Phospholipase A2γ in Phospholipid Remodeling" Cells 8, no. 8: 799. https://doi.org/10.3390/cells8080799

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