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Serum lysophosphatidic acid is produced through diverse phospholipase pathways.

Authors: Aoki, Junken  Taira, Akitsu  Takanezawa, Yasukazu  Kishi, Yasuhiro  Hama, Kotaro  Kishimoto, Tatsuya  Mizuno, Koji  Saku, Keijiro  Taguchi, Ryo  Arai, Hiroyuki 
Citation: Aoki J, etal., J Biol Chem. 2002 Dec 13;277(50):48737-44. doi: 10.1074/jbc.M206812200. Epub 2002 Sep 26.
Pubmed: (View Article at PubMed) PMID:12354767
DOI: Full-text: DOI:10.1074/jbc.M206812200

Lysophosphatidic acid (LPA) is a lipid mediator with multiple biological activities that accounts for many biological properties of serum. LPA is thought to be produced during serum formation based on the fact that the LPA level is much higher in serum than in plasma. In this study, to better understand the pathways of LPA synthesis in serum, we evaluated the roles of platelets, plasma, and phospholipases by measuring LPA using a novel enzyme-linked fluorometric assay. First, examination of platelet-depleted rats showed that half of the LPA in serum is produced via a platelet-dependent pathway. However, the amount of LPA released from isolated platelets after they are activated by thrombin or calcium ionophore accounted for only a small part of serum LPA. Most of the platelet-derived LPA was produced in a two-step process: lysophospholipids such as lysophosphatidylcholine (LPC), lysophosphatidylethanolamine, and lysophosphatidylserine, were released from activated rat platelets by the actions of two phospholipases, group IIA secretory phospholipase A(2) (sPLA(2)-IIA) and phosphatidylserine-specific phospholipase A(1) (PS-PLA(1)), which were abundantly expressed in the cells. Then these lysophospholipids were converted to LPA by the action of plasma lysophospholipase D (lysoPLD). Second, accumulation of LPA in incubated plasma was strongly accelerated by the addition of recombinant lysoPLD with a concomitant decrease in LPC accumulation, indicating that the enzyme produces LPA by hydrolyzing LPC produced during the incubation. In addition, incubation of plasma isolated from human subjects who were deficient in lecithin-cholesterol acyltransferase (LCAT) did not result in increases of either LPC or LPA. The present study demonstrates multiple pathways for LPA production in serum and the involvement of several phospholipases, including PS-PLA(1), sPLA(2)-IIA, LCAT, and lysoPLD.


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CRRD Object Information
CRRD ID: 15090854
Created: 2019-12-20
Species: All species
Last Modified: 2019-12-20
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.