Effect of lysophosphatidylcholine on transmembrane signal transduction - PubMed (original) (raw)

Affiliations

PMID: 9526092

Review

Effect of lysophosphatidylcholine on transmembrane signal transduction

N V Prokazova et al. Biochemistry (Mosc). 1998 Jan.

Abstract

Lysophosphatidylcholine (LPC), 1-acyl-sn-glycero-3-phosphocholine, is well known as an intermediate of metabolism of phosphatidylcholine (PC), the main phospholipid component in all eukaryotic and many prokaryotic cells. LPC is produced as a result of PC hydrolysis by several isoforms of phospholipase A2 (PLA2) and in the reaction mediated by lecithin-cholesterol acyltransferase that transfers the fatty acid residue from PC to cholesterol. LPC is classified as a second messengers that is produced by activation of cytosolic hormone-activated PLA2. It was shown that LPC inhibits transmembrane signaling via receptors, which in their active form are linked to G-proteins. There is a viewpoint that LPC abolishes formation of the complex between the receptor and G-protein. The effect of LPC on protein kinase C (PKC) activation is considered in this review. It was shown that low (less than 20 microM) and high (more than 30 microM) concentrations of LPC activated and inhibited PKC, respectively. The mechanism of LPC-induced activation of PKC still remains unclear. However, the studies of the effect of LPC on signal transduction through the PKC-mediated pathway showed that LPC probably plays an auxiliary role. It was suggested that LPC may prolong the effect of the direct activators of PKC (such as 1,2-diacylglycerol or phorbol esters). The physiological role of the elevation of LPC level in tissues is associated with its ability to enhance or even evoke cell proliferation, stimulate adhesion and differentiation of lymphoid cells, have mitogenic effect on macrophages, activate human T-lymphocytes, initiate monocyte chemotaxis, decrease myocardial sensitivity to cholinergic stimulation, impair contractility of arterial smooth muscle, and modulate aggregation of platelets.

PubMed Disclaimer

Cited by

Lysophosphatidylcholine induces inflammatory activation of human coronary artery smooth muscle cells.
Aiyar N, Disa J, Ao Z, Ju H, Nerurkar S, Willette RN, Macphee CH, Johns DG, Douglas SA. Aiyar N, et al. Mol Cell Biochem. 2007 Jan;295(1-2):113-20. doi: 10.1007/s11010-006-9280-x. Epub 2006 Aug 8. Mol Cell Biochem. 2007. PMID: 16896535
Novel phospholipase A activity secreted by Legionella species.
Flieger A, Gong S, Faigle M, Deeg M, Bartmann P, Neumeister B. Flieger A, et al. J Bacteriol. 2000 Mar;182(5):1321-7. doi: 10.1128/JB.182.5.1321-1327.2000. J Bacteriol. 2000. PMID: 10671453 Free PMC article.
Decreased MARCKS Protein Expression in Kidney Cortex Membrane Fractions of Cathepsin B Knockout Mice Is Associated with Reduced Lysophosphatidylcholine and Protein Kinase C Activity.
Kawakibi T, Bala N, Liu LP, Searcy LA, Denslow ND, Alli AA. Kawakibi T, et al. Biomedicines. 2023 May 20;11(5):1489. doi: 10.3390/biomedicines11051489. Biomedicines. 2023. PMID: 37239160 Free PMC article.
MALDI-TOF Mass Spectrometry Revealed Significant Lipid Variations in Follicular Fluid and Somatic Follicular Cells but Not in Enclosed Oocytes between the Large Dominant and Small Subordinate Follicles in Bovine Ovary.
Bertevello PS, Teixeira-Gomes AP, Labas V, Cordeiro L, Blache MC, Papillier P, Singina G, Uzbekov R, Maillard V, Uzbekova S. Bertevello PS, et al. Int J Mol Sci. 2020 Sep 11;21(18):6661. doi: 10.3390/ijms21186661. Int J Mol Sci. 2020. PMID: 32932995 Free PMC article.
Potential mechanisms for the enhancement of HERG K+ channel function by phospholipid metabolites.
Wang J, Zhang Y, Wang H, Han H, Nattel S, Yang B, Wang Z. Wang J, et al. Br J Pharmacol. 2004 Feb;141(4):586-99. doi: 10.1038/sj.bjp.0705646. Epub 2004 Jan 26. Br J Pharmacol. 2004. PMID: 14744814 Free PMC article.

Effect of lysophosphatidylcholine on transmembrane signal transduction - PubMed (original) (raw)