Journal
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
Volume 20, Issue 5, Pages -Publisher
MDPI
DOI: 10.3390/ijms20051149
Keywords
lysophosphatidylcholine; lipoprotein-associated phospholipase A(2); lysophosphatidylcholine acyltransferase; lysophospholipase A(1); autotaxin; G protein-coupled receptor G2A
Funding
- Vascular and Medicinal Research Fund, Texas Heart Institute [765-64050]
- Kaohsiung Medical University [KMU-TP105D14, KMU-DK107012, KMUH106-6R64, KMUH107-7R66]
- Taiwan Ministry of Science and Technology [MOST 105-2320-B-037-004-MY3, MOST 107-2314-B-037-114-MY3, MOST107-2911-I-037-505, MOST106-2321-B-037-003, 107-2321-B-037-002, 106-2314-B-037-069-]
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Lysophosphatidylcholine (LPC) is increasingly recognized as a key marker/factor positively associated with cardiovascular and neurodegenerative diseases. However, findings from recent clinical lipidomic studies of LPC have been controversial. A key issue is the complexity of the enzymatic cascade involved in LPC metabolism. Here, we address the coordination of these enzymes and the derangement that may disrupt LPC homeostasis, leading to metabolic disorders. LPC is mainly derived from the turnover of phosphatidylcholine (PC) in the circulation by phospholipase A(2) (PLA(2)). In the presence of Acyl-CoA, lysophosphatidylcholine acyltransferase (LPCAT) converts LPC to PC, which rapidly gets recycled by the Lands cycle. However, overexpression or enhanced activity of PLA(2) increases the LPC content in modified low-density lipoprotein (LDL) and oxidized LDL, which play significant roles in the development of atherosclerotic plaques and endothelial dysfunction. The intracellular enzyme LPCAT cannot directly remove LPC from circulation. Hydrolysis of LPC by autotaxin, an enzyme with lysophospholipase D activity, generates lysophosphatidic acid, which is highly associated with cancers. Although enzymes with lysophospholipase A(1) activity could theoretically degrade LPC into harmless metabolites, they have not been found in the circulation. In conclusion, understanding enzyme kinetics and LPC metabolism may help identify novel therapeutic targets in LPC-associated diseases.
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