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• W2182912456 abstract "EDITORIAL FOCUSLysophospholipids in the regulation of endothelial barrier functionHazel LumHazel Lum 1 Department of Pharmacology, Rush Presbyterian St. Luke's Medical Center, Chicago, Illinois 60612Published Online:01 Dec 2001https://doi.org/10.1152/ajplung.2001.281.6.L1335MoreSectionsPDF (76 KB)Download PDF ToolsExport citationAdd to favoritesGet permissionsTrack citations ShareShare onFacebookTwitterLinkedInEmail serum is known to contain heat-stable and trypsin-sensitive bioactive factors that possess diverse biological activities, including promotion of wound healing and tissue regeneration as well as inflammatory processes. To date, some of these factors are identified to be lysophospholipid ligands [i.e., lysophosphatidic acid (LPA) and sphingosine 1-phosphate (S1P)] that bind with high affinity to and signal through members of a subfamily of G protein-coupled receptors encoded by the endothelial differentiation genes (6). In addition to endothelial differentiation gene receptors, several other biologically active phospholipids [i.e., platelet-activating factor (PAF), lysophosphatidylcholine (8), and species of oxidized phosphatidylcholine (11)] activate the PAF receptor, another lipid ligand-specific G protein-coupled receptor (7).Most of these lipid mediators possess potent proinflammatory properties that directly activate the vascular endothelium. Recent work shows that LPA and S1P activate the transcription factor nuclear factor-κB; generate production of the cytokines monocyte chemoattractant protein-1 and interleukin-8; and upregulate expression of the adhesion molecules vascular cell adhesion molecule-1, E-selectin, and intercellular adhesion molecule-1 (14) as well as increase leukocyte adhesion to the endothelial cell surface (15). Furthermore, they are mitogenic. In particular, S1P is a potent endothelial cell chemotactic agent, and, therefore, these lipids are proposed to be critical regulators in wound healing processes. PAF and other phospholipids (8, 11) that signal through the PAF receptor are also highly proinflammatory. It is well known that PAF increases vascular epithelial as well as endothelial permeability, leukocyte extravasation, and promotion of cytokine production and is implicated in several vascular diseases including vasculitis and asthma (3, 9).With the exception of PAF, the regulation of endothelial barrier function by these lipid mediators is not well known. LPA and S1P appear to promote endothelial barrier restrictiveness (1, 4, 10), a surprising property in light of their proinflammatory and angiogenic actions. But LPA is also shown to impair endothelial barrier function (16, 17a), thus underscoring the incomplete understanding of the function, regulation, and physiological role of these lipids in vascular biology. The paper by Minnear et al. (12) in this issue of American Journal of Physiology-Lung Cellular and Molecular Physiology adds further support to the barrier-promoting actions of the lysophospholipids and some insight into their physiological significance. These authors provide evidence that the barrier-promoting effects of these lipids may account for the permeability-decreasing activity of platelets. S1P is primarily stored in platelets and released on cellular activation (18), whereas LPA is released by both nonstimulated and stimulated platelets as well as by activated fibroblasts, adipocytes, and tumor cells (13). LPA is also found in mildly oxidized low-density lipoprotein (17). On their generation and release, most of these lysophospholipids are bound to serum proteins such as albumin or lipoproteins. A key finding by Minnear et al. (12) is that platelet-derived lipids form a complex with albumin, which then confers barrier-promoting effects to the endothelium. The identity of the responsible lipid(s) has yet to be determined.An interesting finding by Minnear et al. (12) is that LPA was not detected from the lipid-albumin complexes in one of the two platelet batches examined despite the fact that the lipid-albumin fraction from both batches yielded potent permeability-decreasing activity. This finding strongly suggests that other lipids associated with albumin in addition to LPA play a role in the promotion of barrier function. Furthermore, in the in vivo situation, LPA bound to albumin is derived from multiple sources including platelets. Therefore, the barrier-promoting property attributable to LPA from platelets is likely to be less than that of those lipids derived predominantly from platelets, such as S1P. Indeed, Yatomi et al. (18) found that activated platelets released predominantly S1P, not LPA. Furthermore, platelets in blood clots released greater amounts of SPP than platelets stimulated with thrombin, ADP, or Ca2+ionophores in the absence of clots (5), suggesting that lipids secreted by platelets are stimulus selective. Thus it is clear that the lipid profile associated with albumin is critically influenced by the physiological state of platelets and, therefore, is of great importance in the regulation of endothelial activities. However, in the study by Minnear et al. (12), who used nonactivated platelets, the lipid composition associated with albumin varied between the two platelet batches, indicating yet undetermined factors responsible for the difference. Thus there is a need to fully understand the determinants of lipid composition changes associated with albumin, which is fundamental to our understanding of platelet-endothelial cell biology in health and disease.FOOTNOTESAddress for reprint requests and other correspondence: H. Lum, Dept. of Pharmacology, Rush Presbyterian St. Luke's Medical Center, 2242 W. Harrison St., Suite 260, Chicago, IL 60612 (E-mail:[email protected]edu).REFERENCES1 Alexander JS, Patton WF, Christman BW, Cuiper LL, Haselton FR.Platelet-derived lysophosphatidic acid decreases endothelial permeability in vitro.Am J Physiol Heart Circ Physiol2741998H115H122Link | ISI | Google Scholar3 Barnes PJ.Platelet activating factor and asthma.Ann NY Acad Sci6291991193204Crossref | PubMed | ISI | Google Scholar4 English D, Kovala AT, Welch Z, Harvey KA, Siddiqui RA, Brindley DN, Garcia JG.Induction of endothelial cell chemotaxis by sphingosine 1-phosphate and stabilization of endothelial monolayer barrier function by lysophosphatidic acid, potential mediators of hematopoietic angiogenesis.J Hematother Stem Cell Res81999627634Crossref | PubMed | Google Scholar5 English D, Welch Z, Kovala AT, Harvey K, Volpert OV, Brindley DN, Garcia JG.Sphingosine 1-phosphate released from platelets during clotting accounts for the potent endothelial cell chemotactic activity of blood serum and provides a novel link between hemostasis and angiogenesis.FASEB J14200022552265Crossref | PubMed | ISI | Google Scholar6 Fukushima N, Ishii I, Contos JJ, Weiner JA, Chun J.Lysophospholipid receptors.Annu Rev Pharmacol Toxicol412001507534Crossref | PubMed | ISI | Google Scholar7 Honda Z, Nakamura M, Seyama Y, Shimizu T.Properties of the guinea-pig lung platelet-activating factor receptor encoded by the cloned cDNA.J Lipid Mediators51992105107PubMed | Google Scholar8 Huang YH, Schafer-Elinder L, Wu R, Claesson HE, Frostegard J.Lysophosphatidylcholine (LPC) induces proinflammatory cytokines by a platelet-activating factor (PAF) receptor-dependent mechanism.Clin Exp Immunol1161999326331Crossref | PubMed | ISI | Google Scholar9 Koltai M, Hosford D, Braquet P.Role of PAF and cytokines in microvascular tissue injury.J Lab Clin Med1191992461466PubMed | Google Scholar10 Lee MJ, Thangada S, Claffey KP, Ancellin N, Liu CH, Kluk M, Volpi M, Sha'afi RI, Hla T.Vascular endothelial cell adherens junction assembly and morphogenesis induced by sphingosine-1-phosphate.Cell991999301312Crossref | PubMed | ISI | Google Scholar11 Marathe GK, Davies SS, Harrison KA, Silva AR, Murphy RC, Castro-Faria-Neto H, Prescott SM, Zimmerman GA, Mcintyre TM.Inflammatory platelet-activating factor-like phospholipids in oxidized low density lipoproteins are fragmented alkyl phosphatidylcholines.J Biol Chem27419992839528404Crossref | PubMed | ISI | Google Scholar12 Minnear FL, Patil S, Bell D, Gainor JP, Morton CA.Platelet lipid(s) bound to albumin increases endothelial electrical resistance: mimicked by LPA.Am J Physiol Lung Cell Mol Physiol2812001L1337L1344Link | ISI | Google Scholar13 Pages C, Simon M, Valet P, Saulnier-Blache JS.Lysophosphatidic acid synthesis and release(1).Prostaglandins642001110Crossref | PubMed | ISI | Google Scholar14 Palmetshofer A, Robson SC, Nehls V.Lysophosphatidic acid activates nuclear factor kappa B and induces proinflammatory gene expression in endothelial cells.Thromb Haemost82199915321537Crossref | PubMed | ISI | Google Scholar15 Rizza C, Leitinger N, Yue J, Fischer DJ, Wang DA, Shih PT, Lee H, Tigyi G, Berliner JA.Lysophosphatidic acid as a regulator of endothelial/leukocyte interaction.Lab Invest79199912271235PubMed | ISI | Google Scholar16 Schulze C, Smales C, Rubin LL, Staddon JM.Lysophosphatidic acid increases tight junction permeability in cultured brain endothelial cells.J Neurochem6819979911000Crossref | PubMed | ISI | Google Scholar17 Siess W, Zangl KJ, Essler M, Bauer M, Brandl R, Corrinth C, Bittman R, Tigyi G, Aepfelbacher M.Lysophosphatidic acid mediates the rapid activation of platelets and endothelial cells by mildly oxidized low density lipoprotein and accumulates in human atherosclerotic lesions.Proc Natl Acad Sci USA96199969316936Crossref | PubMed | ISI | Google Scholar17a Van Nieuw Amerongen GP, Vermeer MA, van Hinsbergh VWMRole of RhoA and Rho kinase in lysophosphatidic acid-induced endothelial barrier dysfunction.Arterioscler Thromb Vasc Biol202000E127E133Crossref | PubMed | ISI | Google Scholar18 Yatomi Y, Ohmori T, Rile G, Kazama F, Okamoto H, Sano T, Satoh K, Kume S, Tigyi G, Igarashi Y, Ozaki Y.Sphingosine 1-phosphate as a major bioactive lysophospholipid that is released from platelets and interacts with endothelial cells.Blood96200034313438Crossref | PubMed | ISI | Google Scholar Previous Back to Top Next FiguresReferencesRelatedInformationCited ByOxidative Stress and Microvessel Barrier Dysfunction27 May 2020 | Frontiers in Physiology, Vol. 11Membrane lipid interactions in intestinal ischemia/reperfusion-induced InjuryClinical Immunology, Vol. 153, No. 1Presence of secretory group IIa and V phospholipase A2 and cytosolic group IVα phospholipase A2 in chondrocytes from patients with rheumatoid arthritisClinical Chemistry and Laboratory Medicine (CCLM), Vol. 42, No. 6 More from this issue > Volume 281Issue 6December 2001Pages L1335-L1336 Copyright & PermissionsCopyright © 2001 the American Physiological Societyhttps://doi.org/10.1152/ajplung.2001.281.6.L1335PubMed11704527History Published online 1 December 2001 Published in print 1 December 2001 PDF download Metrics Downloaded 113 times" @default.
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