Secreted phospholipase A2, lipoprotein hydrolysis,and atherosclerosis: integration with lipidomics |
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Authors: | Kei Yamamoto Yuki Isogai Hiroyasu Sato Yoshitaka Taketomi Makoto Murakami |
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Affiliation: | (1) Lipid Metabolism Project, The Tokyo Metropolitan Institute of Medical Science, 2-1-6 Kamikitazawa, Setagaya-ku, Tokyo 156–8506, Japan; |
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Abstract: | Phospholipase A2 (PLA2) is a group of enzymes that hydrolyze the sn-2 position of glycerophospholipids to yield fatty acids and lysophospholipids. Of many PLA2s or related enzymes identified to date, secreted PLA2s (sPLA2s) comprise the largest family that contains 10 catalytically active isozymes. Besides arachidonic acid released from cellular membranes for eicosanoid synthesis, several if not all sPLA2s have recently been implicated in hydrolysis of phospholipids in lipoprotein particles. The sPLA2-processed low-density lipoprotein (LDL) particles contain a large amount of lysophospholipids and exhibit the property of “small-dense” or “modified” LDL, which facilitates foam cell formation from macrophages. Transgenic overexpression of these sPLA2s leads to development of atherosclerosis in mice. More importantly, genetic deletion or pharmacological inhibition of particular sPLA2s significantly attenuates atherosclerosis and aneurysm. In this article, we will give an overview of current understanding of the role of sPLA2s in atherosclerosis, with recent lipidomics data showing the action of a subset of sPLA2s on lipoprotein phospholipids. |
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