The role of serum amyloid A and sphingosine-1-phosphate on high-density lipoprotein functionality

References

Annema, W., Nijstad, N., Tolle, M., de Boer, J.F., Buijs, R.V., Heeringa, P., van der Giet, M., and Tietge, U.J., (2010). Myeloperoxidase and serum amyloid A contribute to impaired in vivo reverse cholesterol transport during the acute phase response but not group iia secretory phospholipase a(2). J. Lipid. Res. 51, 743–754.10.1194/jlr.M000323Search in Google Scholar

Argraves, K.M., Gazzolo, P.J., Groh, E.M., Wilkerson, B.A., Matsuura, B.S., Twal, W.O., Hammad, S.M., and Argraves, W.S. (2008). High density lipoprotein-associated sphingosine 1-phosphate promotes endothelial barrier function. J. Biol. Chem. 283, 25074–25081.10.1074/jbc.M801214200Search in Google Scholar

Artl, A., Marsche, G., Lestavel, S., Sattler, W., and Malle, E. (2000). Role of serum amyloid A during metabolism of acute-phase HDL by macrophages. Arterioscler Thromb. Vasc. Biol. 20, 763–772.10.1161/01.ATV.20.3.763Search in Google Scholar

Artl, A., Marsche, G., Pussinen, P., Knipping, G., Sattler, W., and Malle, E. (2002). Impaired capacity of acute-phase high density lipoprotein particles to deliver cholesteryl ester to the human huh-7 hepatoma cell line. Int. J. Biochem. Cell Biol. 34, 370–381.10.1016/S1357-2725(01)00132-7Search in Google Scholar

Assmann, G. and Nofer, J.R. (2003). Atheroprotective effects of high-density lipoproteins. Ann. Rev. Med. 54, 321–341.10.1146/annurev.med.54.101601.152409Search in Google Scholar

Badolato, R., Wang, J.M., Murphy, W.J., Lloyd, A.R., Michiel, D.F., Bausserman, L.L., Kelvin, D.J., and Oppenheim, J.J. (1994). Serum amyloid A is a chemoattractant: Induction of migration, adhesion, and tissue infiltration of monocytes and polymorphonuclear leukocytes. J. Exp. Med. 180, 203–209.10.1084/jem.180.1.203Search in Google Scholar

Banka, C.L., Yuan, T., de Beer, M.C., Kindy, M., Curtiss, L.K., and de Beer, F.C. (1995). Serum amyloid A (SAA): influence on HDL-mediated cellular cholesterol efflux. J. Lipid. Res. 36, 1058–1065.10.1016/S0022-2275(20)39863-1Search in Google Scholar

Baranova, I.N., Bocharov, A.V., Vishnyakova, T.G., Kurlander, R., Chen, Z., Fu, D., Arias, I.M. Csako, G., Patterson, A.P., and Eggerman, T.L. (2010). Cd36 is a novel serum amyloid A (SAA) receptor mediating saa binding and saa-induced signaling in human and rodent cells. J. Biol. Chem. 285, 8492–8506.10.1074/jbc.M109.007526Search in Google Scholar

Barter, P.J. (2002). Hugh Sinclair lecture: the regulation and remodelling of HDL by plasma factors. Atherosclerosis (Suppl.) 3, 39–47.10.1016/S1567-5688(02)00041-7Search in Google Scholar

Barter, P., Kastelein, J., Nunn, A., and Hobbs, R. (2003). High density lipoproteins (HDLs) and atherosclerosis; the unanswered questions. Atherosclerosis 168, 195–211.10.1016/S0021-9150(03)00006-6Search in Google Scholar

Barter, P.J., Caulfield, M., Eriksson, M., Grundy, S.M., Kastelein, J.J., Komajda, M., Lopez-Sendon, J., Mosca, M., Tardif, J.C., and Waters, D.D. (2007). Effects of torcetrapib in patients at high risk for coronary events. N. Engl. J. Med. 357, 2109–2122.10.1056/NEJMoa0706628Search in Google Scholar

Blaho, V.A. and Hla, T. (2011). Regulation of mammalian physiology, development, and disease by the sphingosine 1-phosphate and lysophosphatidic acid receptors. Chem. Rev. 111, 6299–6320.10.1021/cr200273uSearch in Google Scholar

Cabana, V.G., Siegel, J.N., and Sabesin, S.M. (1989). Effects of the acute phase response on the concentration and density distribution of plasma lipids and apolipoproteins. J. Lipid Res. 30, 39–49.10.1016/S0022-2275(20)38390-5Search in Google Scholar

Cabana, V.G., Lukens, J.R., Rice, K.S., Hawkins, T.J., and Getz, G.S. (1996). HDL content and composition in acute phase response in three species: triglyceride enrichment of HDL a factor in its decrease. J. Lipid Res. 37, 2662–2674.10.1016/S0022-2275(20)37469-1Search in Google Scholar

Cabana, V.G., Reardon, C.A., Feng, N., Neath, S., Lukens, J., and Getz, G.S. (2003). Serum paraoxonase: effect of the apolipoprotein composition of hdl and the acute phase response. J. Lipid Res. 44, 780–792.10.1194/jlr.M200432-JLR200Search in Google Scholar PubMed

Cabana, V.G., Feng, N., Reardon, C.A., Lukens, J., Webb, N.R., de Beer, F.C., and Getz, G.S. (2004). Influence of ApoA-i and ApoE on the formation of serum amyloid A-containing lipoproteins in vivo and in vitro. J. Lipid Res. 45, 317–325.10.1194/jlr.M300414-JLR200Search in Google Scholar PubMed

Cai, L., de Beer, M.C., de Beer, F.C., and van der Westhuyzen, D.R. (2005). Serum amyloid A is a ligand for scavenger receptor class b type i and inhibits high density lipoprotein binding and selective lipid uptake. J. Biol. Chem. 280, 2954–2961.10.1074/jbc.M411555200Search in Google Scholar PubMed

Cheng, N., He, R., Tia, J., Ye, P.P., and Ye, R.D. (2008). Cutting edge: Tlr2 is a functional receptor for acute-phase serum amyloid A. J. Immunol. 181, 22–26.10.4049/jimmunol.181.1.22Search in Google Scholar PubMed PubMed Central

Christenson, K., Bjorkman, L., Tangemo, C., and Bylund, J. (2008). Serum amyloid A inhibits apoptosis of human neutrophils via a p2x7-sensitive pathway independent of formyl peptide receptor-like 1. J. Leukoc. Biol. 83, 139–148.10.1189/jlb.0507276Search in Google Scholar PubMed

Christoffersen, C., Obinata, H., Kumaraswamy, S.B., Galvani, S., Ahnstrom, J., Sevvana, M., Egerer-Sieber, C., Muller, Y.A., Hla, T., Nielsen, L.B., et al. (2011). Endothelium-protective sphingosine-1-phosphate provided by hdl-associated apolipoprotein M. Proc. Natl. Acad. Sci. USA 108, 9613–9618.10.1073/pnas.1103187108Search in Google Scholar PubMed PubMed Central

Chun, J., Goetzl, E.J., Hla, T., Igarashi, Y., Lynch, K.R., Moolenaar, W. Moolenaar, Pyne, S., and Tigyi, G. (2002). International union of pharmacology. XXXIV. Lysophospholipid receptor nomenclature. Pharmacol. Rev. 54, 265–269.10.1124/pr.54.2.265Search in Google Scholar

Coetzee, G.A., Strachan, A.F., van der Westhuyzen, D.R., Hoppe, H.C., Jeenah, M.S., and de Beer, F.C. (1986). Serum amyloid A-containing human high density lipoprotein 3. Density, size, and apolipoprotein composition. J. Biol. Chem. 261, 9644–9651.10.1016/S0021-9258(18)67562-3Search in Google Scholar

Corsetti, J.P., Zareba, W., Moss, A.J., Rainwater, D.L., and Sparks, C.E. (2006). Elevated HDL is a risk factor for recurrent coronary events in a subgroup of non-diabetic postinfarction patients with hypercholesterolemia and inflammation. Atherosclerosis 187, 191–197.10.1016/j.atherosclerosis.2005.09.012Search in Google Scholar

de Beer, M.C., Wroblewski, J.M., Noffsinger, V.P., Ji, A., Meyer, J.M., van der Westhuyzen, D.R., de Beer, F.C., and Webb, N.R. (2013). The impairment of macrophage-to-feces reverse cholesterol transport during inflammation does not depend on serum amyloid A. J. Lipids 2013, 283–486.Search in Google Scholar

de Souza, J.A., vindis, C., Negre-Salvayre, A., Rye, K.A., Couturier, K.A., Therond, P., Chantepie, S. Salvayre, R., Chapman, M.J., and Kontush, A. (2010). Small, dense HDL 3 particles attenuate apoptosis in endothelial cells: pivotal role of apolipoprotein A-I. J. Cell Mol. Med. 14, 608–620.Search in Google Scholar

Dong, Z., Wu, T., Qin, W., An, C., Wang, Z., Zhang, M., Zhang, Y., Zhang, C., and An, F. (2011). Serum amyloid A directly accelerates the progression of atherosclerosis in apolipoprotein E-deficient mice. Mol. Med. 17, 1357–1364.10.2119/molmed.2011.00186Search in Google Scholar

Glomset, J.A. (1968). The plasma lecithins: Cholesterol acyltransferase reaction. J. Lipid Res. 9, 155–167.10.1016/S0022-2275(20)43114-1Search in Google Scholar

Gordon, T., Castelli, W.P., Hjortland, M.C., Kannel, W.B., and Dawber, T.R. (1977). High density lipoprotein as a protective factor against coronary heart disease. The Framingham study. Am. J. Med. 62, 707–714.10.1016/0002-9343(77)90874-9Search in Google Scholar

Hannun, Y.A. and Obeid, L.M. (2008). Principles of bioactive lipid signalling: lessons from sphingolipids. Nat. Rev. Mol. Cell Biol. 9, 139–150.10.1038/nrm2329Search in Google Scholar PubMed

Hanson, M.A., Roth, C.B., Jo, E., Griffith, M.T., Scott, F.L., Reingart, G., Desale, H., Clemons, B., Cahalan, S.M., Schuerer, S.C., et al. (2012). Crystal structure of a lipid g protein-coupled receptor. Science 335, 851–855.10.1126/science.1215904Search in Google Scholar PubMed PubMed Central

Hatanaka, E., Dermargos, A., Armelin, H.A., Curi, R., and Campa, A. (2011). Serum amyloid A induces reactive oxygen species (ROS) production and proliferation of fibroblast. Clin. Exp. Immunol. 163, 362–367.10.1111/j.1365-2249.2010.04300.xSearch in Google Scholar PubMed PubMed Central

He, R.L., Zhou, J., Hanson, C.Z., Chen, J., Cheng, N., and Ye, R.D. (2009). Serum amyloid A induces γ-CSF expression and neutrophilia via toll-like receptor 2. Blood 113, 429–437.10.1182/blood-2008-03-139923Search in Google Scholar PubMed PubMed Central

Jurek, A., Turyna, B., Kubit, K., and Klein, A. (2008). The ability of HDL to inhibit VCAM-1 expression and oxidized LDL uptake is impaired in renal patients. Clin. Biochem. 41, 1015–1018.10.1016/j.clinbiochem.2008.04.019Search in Google Scholar PubMed

Kappelle, P.J., Bijzet, J., Hazenberg, B.P., and Dullaart, R.P. (2011). Lower serum paraoxonase-1 activity is related to higher serum amyloid A levels in metabolic syndrome. Arch. Med. Res. 42, 219–225.10.1016/j.arcmed.2011.05.002Search in Google Scholar PubMed

Khansari, N., Shakiba, Y., and Mahmoudi, M. (2009). Chronic inflammation and oxidative stress as a major cause of age-related diseases and cancer. Recent Pat. Inflamm. Allergy. Drug Discov. 3, 73–80.10.2174/187221309787158371Search in Google Scholar PubMed

Kilpatrick, R.D., McAllister, C.J., Kovesdy, C.P., Derose, S.F., Kopple, J.D., and Kalantar-Zadeh, K. (2007). Association between serum lipids and survival in hemodialysis patients and impact of race. J. Am. Soc. Nephrol. 18, 293–303.10.1681/ASN.2006070795Search in Google Scholar PubMed

King, V.L., Thompson, J., and Tannock, L.R. (2011). Serum amyloid A in atherosclerosis. Curr. Opin. Lipidol. 22, 302–307.10.1097/MOL.0b013e3283488c39Search in Google Scholar PubMed

Kisilevsky, R. and Subrahmanyan, L. (1992). Serum amyloid A changes high density lipoprotein’s cellular affinity. A clue to serum amyloid A’s principal function. Lab. Invest. 66, 778–785.Search in Google Scholar

Kisilevsky, R. and Tam, S.P. (2003). Macrophage cholesterol efflux and the active domains of serum amyloid A 2.1. J. Lipid Res. 44, 2257–2269.10.1194/jlr.M300133-JLR200Search in Google Scholar PubMed

Koch, A., Pfeilschifter, J., and Huwiler, A. (2013). Sphingosine 1-phosphate in renal diseases. Cellular Physiology and Biochemistry 31, 745–760.10.1159/000350093Search in Google Scholar PubMed

Kumaraswamy, S.B., Linder, A., Akesson, P., and Dahlback, B. (2012). Decreased plasma concentrations of apolipoprotein m in sepsis and systemic inflammatory response syndromes. Crit. Care 16, R60.10.1186/cc11305Search in Google Scholar PubMed PubMed Central

Kumon, Y., Nakauchi, Y., Suehiro, T., Shiinoki, T., Tanimoto, N., Inoue, M., Nakamura, T. Hashimoto, K., and Sipe, J.D. (2002). Proinflammatory cytokines but not acute phase serum amyloid A or C-reactive protein, downregulate paraoxonase 1 (pon1) expression by HepG2 cells. Amyloid 9, 160–164.10.3109/13506120209114817Search in Google Scholar PubMed

Kwon, Y.G., Min, J.K., Kim, K.M., Lee, D.J., Billar, T.R., and Kim, Y.M. (2001). Sphingosine 1-phosphate protects human umbilical vein endothelial cells from serum-deprived apoptosis by nitric oxide production. J. Biol. Chem. 276, 10627–10633.10.1074/jbc.M011449200Search in Google Scholar PubMed

Lakota, K., Mrak-Poljsak, K., Bozic, B., Tomsic, M., and Sodin-Semrl, S. (2013). Serum amyloid A activation of human coronary artery endothelial cells exhibits a neutrophil promoting molecular profile. Microvasc, Res, 90, 55–63.10.1016/j.mvr.2013.07.011Search in Google Scholar

Le Goff, W., Guerin, M., and Chapman, M.J. (2004). Pharmacological modulation of cholesteryl ester transfer protein, a new therapeutic target in atherogenic dyslipidemia. Pharmacol. Ther. 101, 17–38.10.1016/j.pharmthera.2003.10.001Search in Google Scholar

Le Stunff, H., Peterson, C., Thornton, R. Milstein, S., Mandala, S.M., and Spiegel, S. (2002). Characterization of murine sphingosine-1-phosphate phosphohydrolase. J. Biol. Chem. 277, 8920–8927.10.1074/jbc.M109968200Search in Google Scholar

Lee, M.J., Van Brocklyn, J.R., Thangada, S., Liu, C.H., Hand, A.R., Menzeleev, R., Spiegel, S., and Hla, T. (1998). Sphingosine-1-phosphate as a ligand for the G protein-coupled receptor Edg-1. Science 279, 1552–1555.10.1126/science.279.5356.1552Search in Google Scholar

Lee, M.J., Thangada, S., Claffey, K.P., Ancellin, N., Liu, C.H., Kluk, M., Volpi, M., Sha’afi, R.I., and Hla, T. (1999). Vascular endothelial cell adherens junction assembly and morphogenesis induced by sphingosine-1-phosphate. Cell 99, 301–312.10.1016/S0092-8674(00)81661-XSearch in Google Scholar

Lee, H.Y., Kim, M.K., Park, K.S., Bae, Y.H., Yun, J., Park, J.I., Kwak, J.Y., and Bae, Y.S. (2005). Serum amyloid A stimulates matrix-metalloproteinase-9 upregulation via formyl peptide receptor like-1-mediated signaling in human monocytic cells. Biochem. Biophys. Res. Commun. 330, 989–998.10.1016/j.bbrc.2005.03.069Search in Google Scholar

Lee, H.Y., Kim, S.D., Shim, J.W., Kim, H.J., Yun, J., Baek, S.H., Kim, K., and Bae, Y.S. (2010). A pertussis toxin sensitive G-protein-independent pathway is involved in serum amyloid A-induced formyl peptide receptor 2-mediated Ccl2 production. Exp. Mol. Med. 42, 302–309.10.3858/emm.2010.42.4.029Search in Google Scholar

Lee, H.Y., Kim, S.D., Baek, S.H., Choi, J.H., Cho, K.H., Zabel, B.A., and Bae, Y.S. (2013a). Serum amyloid A stimulates macrophage foam cell formation via lectin-like oxidized low-density lipoprotein receptor 1 upregulation. Biochem. Biophys. Res. Commun 433, 18–23.10.1016/j.bbrc.2013.02.077Search in Google Scholar

Lee, H.Y., Kim, S.D., Baek, S.H., Choi, J.H., and Bae, Y.S. (2013b). Role of formyl peptide receptor 2 on the serum amyloid A-induced macrophage foam cell formation. Biochem. Biophys. Res. Commun. 433, 255–259.10.1016/j.bbrc.2013.03.002Search in Google Scholar

Liang, J.S., Schreiber, B.M., Salmona, M., Phillip, G., Gonnerman, W.A., de Beer F.C., and Sipe, J.D. (1996). Amino terminal region of acute phase, but not constitutive, serum amyloid A (ApoSAA) specifically binds and transports cholesterol into aortic smooth muscle and HepG2 cells. J. Lipid Res. 37, 2109–2116.10.1016/S0022-2275(20)37293-XSearch in Google Scholar

Malle, E., Steinmetz, A., and Raynes, J.G. (1993). Serum amyloid A (SAA): an acute phase protein and apolipoprotein. Atherosclerosis 102, 131–146.10.1016/0021-9150(93)90155-NSearch in Google Scholar

Marhaug, G. and Husby, G. (1982). Serum amyloid A protein in high density lipoprotein fraction of human acute phase serum. Lancet 2, 1463.10.1016/S0140-6736(82)91362-9Search in Google Scholar

McGillicuddy, F.C., de la Llera Moya, M., Hinkle, C.C., Joshi, M.R., Chiquoine, E.H., Billheimer, J.T., Rothblat, G.H., and Reilly, M.P. (2009). Inflammation impairs reverse cholesterol transport in vivo. Circulation 119, 1135–1145.10.1161/CIRCULATIONAHA.108.810721Search in Google Scholar PubMed PubMed Central

Medina-Urrutia, A., Juarez-Rojas, J.G., Martinez-Alvarado, R., Jorge-Galarza, E., Posadas-Sanchez, R., Cardoso-Saldana, G., Caracas-Portilla, N., Mendoza-Perez, E., and Posadas-Romero, C. (2008). High-density lipoprotein subclasses distribution and composition in Mexican adolescents with low HDL cholesterol and/or high triglyceride concentrations, and its association with insulin and C-reactive protein. Atherosclerosis 201, 392–397.10.1016/j.atherosclerosis.2008.02.029Search in Google Scholar PubMed

Meek, R.L., Urieli-Shoval, S., and Benditt, E.P. (1994). Expression of apolipoprotein serum amyloid A mRNA in human atherosclerotic lesions and cultured vascular cells: implications for serum amyloid A function. Proc. Natl. Acad. USA 91, 3186–3190.10.1073/pnas.91.8.3186Search in Google Scholar PubMed PubMed Central

Migita, K., Kawabe, Y., Tominaga, M., Origuchi, T., Aoyagi, T., and Eguchi, K. (1998). Serum amyloid A protein induces production of matrix metalloproteinases by human synovial fibroblasts. Lab. Invest. 78, 535–539.Search in Google Scholar

Mineo, C., Deguchi, H., Griffin, J.H., and Shaul, P.W. (2006). Endothelial and antithrombotic actions of HDL. Circ. Res. 98, 1352–1364.10.1161/01.RES.0000225982.01988.93Search in Google Scholar PubMed

Mullan, R.H., McCormick, J., Connolly, M., Bresnihan, B., Veale, D.J., and Fearon, U. (2010). A role for the high-density lipoprotein receptor sr-b1 in synovial inflammation via serum amyloid-A. Am. J. Pathol. 176, 1999–2008.10.2353/ajpath.2010.090014Search in Google Scholar PubMed PubMed Central

Murata, N., Sato, K., Kon, J., Tomura, H., Yanagita, M., Kuwabara, A., Ui, M., and Okajima, F. (2000). Interaction of sphingosine 1-phosphate with plasma components, including lipoproteins, regulates the lipid receptor-mediated actions. Biochem. J. 352 Pt 3, 809–815.10.1042/bj3520809Search in Google Scholar

Ng, C.J., Shih, D.M., Hama, S.Y., Villa, N., Navab, M., and Reddy, S.T. (2005). The paraoxonase gene family and atherosclerosis. Free Radic. Biol. Med. 38, 153–163.10.1016/j.freeradbiomed.2004.09.035Search in Google Scholar PubMed

Niemi, K., Teirila, L., Lappalainen, J., Rajamaki, K., Baumann, M.H., Oorni, K., Wolff, H., Kovanen, P.T., Matikainen, S., and Eklund, K.K. (2011). Serum amyloid A activates the nlrp3 inflammasome via p2x7 receptor and a cathepsin B-sensitive pathway. J. Immunol. 186, 6119–6128.10.4049/jimmunol.1002843Search in Google Scholar PubMed

Nofer, J.R., Kehrel, B., Fobker, M., Levkau, B., Assmann, G., and von Eckardstein, A. (2002). HDL and arteriosclerosis: beyond reverse cholesterol transport. Atherosclerosis 161, 1–16.10.1016/S0021-9150(01)00651-7Search in Google Scholar

Nofer, J.R., van der Giet, M., Tolle, M., Wolinska, I., von Wnuck Lipinski, K., Baba, H.A., Tietge, U.J., Godecke, A., Ishii, I., Kleuser, B., et al. (2004). HDL induces NO-dependent vasorelaxation via the lysophospholipid receptor S1P3. J. Clin. Invest. 113, 569–581.10.1172/JCI200418004Search in Google Scholar

Ogawa, C., Kihara, A., Gokoh, M., and Igarashi, Y. (2003). Identification and characterization of a novel human sphingosine-1-phosphate phosphohydrolase, Hspp2. J. Biol. Chem. 278, 1268–1272.10.1074/jbc.M209514200Search in Google Scholar

Ohta, T., Nakamura, R., Ikeda, Y., Shinohara, M., Miyazaki, A., Horiuchi, S., and Matsuda, I. (1992). Differential effect of subspecies of lipoprotein containing apolipoprotein A-I on cholesterol efflux from cholesterol-loaded macrophages: functional correlation with lecithin:cholesterol acyltransferase. Biochim. Biophys. Acta 1165, 119–128.10.1016/0005-2760(92)90083-8Search in Google Scholar

Ohta, S., Tanaka, M., Sakakura, K., Kawakami, T., Aimoto, S., and Saito, H. (2009). Defining lipid-binding regions of human serum amyloid A using its fragment peptides. Chem. Phys. Lipids 162, 62–68.10.1016/j.chemphyslip.2009.07.008Search in Google Scholar PubMed

Olivera, A. and Spiegel, S. (1993). Sphingosine-1-phosphate as second messenger in cell proliferation induced by PDGF and FCS mitogens. Nature 365, 557–560.10.1038/365557a0Search in Google Scholar PubMed

Patel, H., Fellowes, R., Coade, S., and Woo, P. (1998). Human serum amyloid A has cytokine-like properties. Scand. J. Immunol. 48, 410–418.10.1046/j.1365-3083.1998.00394.xSearch in Google Scholar PubMed

Qiao, J.H., Xie, P.Z., Fishbein, M.C., Kreuzer, J., Drake, T.A., Demer, L.L., and Lusis, A.J. (1994). Pathology of atheromatous lesions in inbred and genetically engineered mice. Genetic determination of arterial calcification. Arterioscler Thromb. 14, 1480–1497.10.1161/01.ATV.14.9.1480Search in Google Scholar

Sandri, S., Rodriguez, D., Gomes, E., Monteiro, H.P., Russo, M., and Campa, A. (2008). Is serum amyloid A an endogenous Tlr4 agonist? J. Leukoc. Biol. 83, 1174–1180.10.1189/jlb.0407203Search in Google Scholar PubMed

Sattler, K.J., Elbasan, S., Keul, P., Elter-Schulz, M., Bode, C., Graler, M.H., Brocker-Preuss, M., Budde, T., Erbel, T., Heusch, G., et al. (2010). Sphingosine 1-phosphate levels in plasma and HDL are altered in coronary artery disease. Basic Res. Cardiol. 105, 821–832.10.1007/s00395-010-0112-5Search in Google Scholar PubMed

Schuchardt, M., Tölle M., Prüfer, J., and van der Giet, M. (2011). Pharmacological relevance and potential of phingosine 1-phosphate in the vascular system. Br. J. Pharmacol. 162, 1140–1162.10.1111/j.1476-5381.2011.01260.xSearch in Google Scholar

Schwartz, G.G., Olsson. A.G., Ballantyne, C.M., Barter, P.J., Holme, I.M., Kallend, D., Leiter, L.A., Leitersdorf, E., McMurray, J.J., Shah, J.J., et al. (2009). Rationale and design of the dal-outcomes trial: efficacy and safety of dalcetrapib in patients with recent acute coronary syndrome. Am. Heart J. 158, 896–901 e893.10.1016/j.ahj.2009.09.017Search in Google Scholar

Song, C., Shen, Y., Yamen, Y., Hsu, K., Yan, W., Witting, P.K., Geczy, C.L., and Freedman, S.B. (2009a). Serum amyloid A may potentiate prothrombotic and proinflammatory events in acute coronary syndromes. Atherosclerosis 202, 596–604.10.1016/j.atherosclerosis.2008.04.049Search in Google Scholar

Song, C., Hsu, K., Yamen, E., Yan, E., Fock, J., Witting, P.K., Geczy, P.K., and Freedman, S.B. (2009b). Serum amyloid A induction of cytokines in monocytes/macrophages and lymphocytes. Atherosclerosis 207, 374–383.10.1016/j.atherosclerosis.2009.05.007Search in Google Scholar

Stein, O. and Stein, Y. (1999). Atheroprotective mechanisms of HDL. Atherosclerosis 144, 285–301.10.1016/S0021-9150(99)00065-9Search in Google Scholar

Stonik, J.A., Remaley, A.T., Demosky, S.J., Neufeld, E.B., Bocharov, A., and Brewer, H.B. (2004). Serum amyloid a promotes abca1-dependent and abca1-independent lipid efflux from cells. Biochem. Biophys. Res. Commun. 321, 936–941.10.1016/j.bbrc.2004.07.052Search in Google Scholar

Sullivan, C.P., Seidl, S.E., Rich, C.B., Raymondjean, M., and Schreiber, M. (2010). Secretory phospholipase A2, group iia is a novel serum amyloid A target gene: activation of smooth muscle cell expression by an interleukin-1 receptor-independent mechanism. J. Biol. Chem. 285, 565–575.10.1074/jbc.M109.070565Search in Google Scholar

Tam, S.P., Flexman, A., Hulme, J., and Kisilevsky, R. (2002). Promoting export of macrophage cholesterol: the physiological role of a major acute-phase protein, serum amyloid A 2.1. J. Lipid Res. 43, 1410–1420.10.1194/jlr.M100388-JLR200Search in Google Scholar

Tanimoto, N., Kumon, Y., Suehiro, T., Ohkubo, S., Ikeda, Y., Nishiya, K., and Hashimoto, K. (2003). Serum paraoxonase activity decreases in rheumatoid arthritis. Life Sci. 72, 2877–2885.10.1016/S0024-3205(03)00195-4Search in Google Scholar

Tolle, M., Pawlak, A., Schuchardt, M., Kawamura, A., Tietge, U.J., Lorkowski, S., Keul, P., Assmann, P., Chun, P., Levkau, B., et al. (2008). HDL-associated lysosphingolipids inhibit NAD(P)H oxidase-dependent monocyte chemoattractant protein-1 production. Arterioscler Thromb. Vasc. Biol. 28, 1542–1548.10.1161/ATVBAHA.107.161042Search in Google Scholar PubMed PubMed Central

Tolle, M., Huang, T., Schuchardt, T., Jankowski, T., Prufer, T., Jankowski, J., Tietge, U.J., Zidek, W., and van der Giet, M. (2012). High-density lipoprotein loses its anti-inflammatory capacity by accumulation of pro-inflammatory-serum amyloid A. Cardiovasc. Res. 94, 154–162.10.1093/cvr/cvs089Search in Google Scholar

Tsun, J.G., Shiu, S.W., Wong, S.W., Yung, S., Chan, S., and Tan, K.C. (2013). Impact of serum amyloid A on cellular cholesterol efflux to serum in type 2 diabetes mellitus. Atherosclerosis 231, 405–410.10.1016/j.atherosclerosis.2013.10.008Search in Google Scholar

Urieli-Shoval, S., Meek, R.L., Hanson, R.H., Eriksen, N., and Benditt, N. (1994). Human serum amyloid A genes are expressed in monocyte/macrophage cell lines. Am. J. Pathol. 145, 650–660.Search in Google Scholar

van der Westhuyzen, D.R., Cai, L., de Beer, M.C., and de Beer, F.C. (2005). Serum amyloid A promotes cholesterol efflux mediated by scavenger receptor B-I. J. Biol. Chem. 280, 35890–35895.10.1074/jbc.M505685200Search in Google Scholar

Van Lenten, B.J., Hama, S.Y., de Beer, F.C., Stafforini, F.C., McIntyre, F.C., Prescott, S.M., La Du, B.N., Fogelman, A.M., and Navab, M. (1995). Anti-inflammatory HDL becomes pro-inflammatory during the acute phase response. Loss of protective effect of HDL against LDL oxidation in aortic wall cell cocultures. J. Clin. Invest. 96, 2758–2767.10.1172/JCI118345Search in Google Scholar

Van Lenten, B.J., Navab, M., Shih, D., Fogelman, A.M., and Lusis, A.J. (2001). The role of high-density lipoproteins in oxidation and inflammation. Trends Cardiovasc. Med. 11, 155–161.10.1016/S1050-1738(01)00095-0Search in Google Scholar

Vaziri, N.D., Moradi, H., Pahl, H., Fogelman, A.M., and Navab, M. (2009). In vitro stimulation of HDL anti-inflammatory activity and inhibition of LDL pro-inflammatory activity in the plasma of patients with end-stage renal disease by an Apoa-1 mimetic peptide. Kidney Int. 76, 437–444.10.1038/ki.2009.177Search in Google Scholar PubMed PubMed Central

Vedhachalam, C., Chetty, P.S., Nickel, M., Dhanasekaran, P., Lund-Katz, S., Rothblat, G.H., and Phillips, M.C. (2010). Influence of apolipoprotein (Apo) A-I structure on nascent high density lipoprotein (HDL) particle size distribution. J. Biol. Chem. 285, 31965–31973.10.1074/jbc.M110.126292Search in Google Scholar PubMed PubMed Central

Venkataraman, K., Thangada, S., Michaud, J., Oo, J., Ai, Y., Lee, Y.M., Wu, M., Parikh, N.S., Kahn, F., Proia, R.L., et al. (2006). Extracellular export of sphingosine kinase-1a contributes to the vascular s1p gradient. Biochem. J. 397, 461–471.10.1042/BJ20060251Search in Google Scholar PubMed PubMed Central

Wang, X., Chai, H., Wang, Z., Lin, P.H., Yao, Q., and Chen, C. (2008). Serum amyloid A induces endothelial dysfunction in porcine coronary arteries and human coronary artery endothelial cells. Am. J. Physiol. Heart. Circ. Physiol. 295, H2399–H2408.10.1152/ajpheart.00238.2008Search in Google Scholar PubMed PubMed Central

Wang, D.X., Liu, H., Yan, L.R., Zhang, Y.P., Guan, X.Y., Xu, Z.M., Jia, Y.H., and Li, Y.S. (2013). The relationship between serum amyloid A and apolipoprotein A-i in high-density lipoprotein isolated from patients with coronary heart disease. Chin. Med. J. (Engl) 126, 3656–3661.Search in Google Scholar

Watson, A.D., Navab, M., Hama, S.Y., Sevanian, A., Prescott, A., Stafforini, A., McIntyre, T.M., Du, B.N., Fogelman, A.M., and Berliner, J.A. (1995a). Effect of platelet activating factor-acetylhydrolase on the formation and action of minimally oxidized low density lipoprotein. J. Clin. Invest. 95, 774–782.10.1172/JCI117726Search in Google Scholar PubMed PubMed Central

Watson, A.D., Berliner, J.A., Hama, S.Y., La Du, B.N., Faull, K.F., Fogelman, A.M., and Navab, A.M. (1995b). Protective effect of high density lipoprotein associated paraoxonase. Inhibition of the biological activity of minimally oxidized low density lipoprotein. J. Clin. Invest. 96, 2882–2891.10.1172/JCI118359Search in Google Scholar PubMed PubMed Central

Weichhart, T., Kopecky, C., Kubicek, M., Haidinger, M., Doller, D., Katholnig, K., Suarna, C., Eller, P., Tolle, P., Gerner, P., et al. (2012). Serum amyloid A in uremic HDL promotes inflammation. J. Am. Soc. Nephrol. 23, 934–947.10.1681/ASN.2011070668Search in Google Scholar PubMed PubMed Central

Wilkerson, B.A., Grass, G.D., Wing, S.B., Argraves, S.B., and Argraves, S.B. (2012). Sphingosine 1-phosphate (S1p) carrier-dependent regulation of endothelial barrier: high density lipoprotein (HDL)-s1p prolongs endothelial barrier enhancement as compared with albumin-S1P via effects on levels, trafficking, and signaling of S1P1. J. Biol. Chem. 287, 44645–44653.10.1074/jbc.M112.423426Search in Google Scholar PubMed PubMed Central

Witting, P.K., Song, C., Hsu, K., Hua, S., Parry, S.N., Aran, R., Geczy, C., and Freedman, C. (2011). The acute-phase protein serum amyloid A induces endothelial dysfunction that is inhibited by high-density lipoprotein. Free Radic. Biol. Med. 51, 1390–1398.10.1016/j.freeradbiomed.2011.06.031Search in Google Scholar PubMed

Xia, P., Vadas, M.A., Rye, M.A., Barter, P.J., and Gamble, P.J. (1999). High density lipoproteins (HDL) interrupt the sphingosine kinase signaling pathway. A possible mechanism for protection against atherosclerosis by HDL. J. Biol. Chem. 274, 33143–33147.10.1074/jbc.274.46.33143Search in Google Scholar PubMed

Yamada, T., Kakihara, T., Kamishima, T., Fukuda, T., and Kawai, T. (1996). Both acute phase and constitutive serum amyloid A are present in atherosclerotic lesions. Pathol. Int. 46, 797–800.10.1111/j.1440-1827.1996.tb03552.xSearch in Google Scholar PubMed

Yang, Y., Yan, B., Fu, B., Xu, Y., and Tian, Y. (2005). Relationship between plasma lipid concentrations and HDL subclasses. Clin. Chim. Acta 354, 49–58.10.1016/j.cccn.2004.11.015Search in Google Scholar PubMed