Abstract
This work reports the effect of the apolipoproteins A-I and A-II (apoA-I and apoA-II) on the release of tumor necrosis factor (TNF)-α, interleukin (IL)-1β, IL-8, and IL-1 receptor antagonist (IL-1Ra) and on the oxidative burst of human neutrophils. By themselves, apoA-I and apoA-II do not affect the basal liberation of these cytokines, whereas apoA-I affects the release of IL-1β from lipopolysaccharide (LPS)-stimulated neutrophils and apoA-II affects IL-8 released from LPS-stimulated neutrophils. ApoA-II also decreases the production of IL-8 released by neutrophils stimulated with the acute phase apolipoprotein serum amyloid A. Both apoA-I and apoA-II exerted ∼30% inhibition on the oxidative burst of neutrophils stimulated by opsonized zymosan, as revealed by the luminol-enhanced chemiluminescence assay. These findings give additional support to the idea that the role of human plasma lipoproteins and apolipoproteins goes beyond their function in lipid transport and metabolism. HDL apolipoproteins appear to be a class of mediators that can participate in the regulation of the activity of neutrophils.
Similar content being viewed by others
Abbreviations
- apoA-I:
-
apolipoproteins A-I
- apoA-II:
-
apolipoproteins A-II
- IL:
-
interleukin
- IL-1Ra:
-
interleukin-1 receptor antagonist
- LPS:
-
hypopolysaccharide
- RPA:
-
RNAse protection assay
- SAA:
-
serum amyloid A
- TNF:
-
tumor necrosis factor
References
Kasiske, B.L., and Keane, W.F. (1991) Role of Lipid Peroxidation in the Inhibition of Mononuclear Cell Proliferation by Normal Lipoproteins, J. Lipid Res. 32, 775–781.
Rosenfeld, S.I., Packman, C.H., and Leddy, J.P. (1983) Inhibition of the Lytic Action of Cell-Bound Terminal Complement Components by Human High Density Lipoproteins and Apoproteins, J. Clin. Invest. 71, 795–808.
Alvarez, C., and Ramos, A. (1986) Lipids, Lipoproteins, and Apoproteins in Serum During Infection, Clin. Chem. 32, 142–145.
Clifton, P.M., Mackinnon, A.M., and Barter, P.J. (1985) Effects of Serum Amyloid A Protein (SAA) on Composition, Size, and Density of High Density Lipoproteins in Subjects with Myocardial Infarction, J. Lipid Res. 26, 1389–1398.
Coetzee, G.A., Strachan, F.A., van der Westhuyzen, D.R., Hoppe, H.C., Jeenah, M.S., and Beer, F.C. (1986) Serum Amyloid A-Containing Human High Density Lipoprotein 3. Density, Size, and Apolipoprotein Composition, J. Biol. Chem. 261, 9644–9651.
Fielding, C.J., and Fielding, P.E. (1995) Molecular Physiology of Reverse Cholesterol Transport, J. Lipid. Res. 36, 211–228.
Tall, A.R. (1990) Plasma High Density Lipoproteins. Metabolism and Relationship to Atherogenesis, J. Clin. Invest. 86, 379–384.
Karathanasis, S.K. (1992). Lipoprotein Metabolism: High Density Lipoprotein, in Molecular Genetics of Coronary Artery Disease (Lusis, A.J., Rotter, J.L., and Sparkes, R.S., eds.) pp. 140–171, Karger, Basel.
Shephard, E.G., de Beer, F.C., de Beer, M.C., Jeenah, M.S., Coetzee, G.A. and van der Westhuyzen, D.R. (1987) Neutrophil Association and Degradation of Normal and Acute-Phase High-Density Lipoprotein 3, Biochem. J. 248, 919–926.
Furlaneto, C.J., and Campa, A. (1997) The Effect in vitro of High-Density Lipoprotein from Healthy and Infected Humans on the Oxidative Metabolism of Polymorphonuclear Leukocytes, Cell Biochem. Funct. 15, 39–45.
Blackburn, W.D., Jr., Dohlman, J.G., Venkatachalapathi, Y.N., Pillion, D.J., Koopmann, W.J., Segrest, J.P., and Anantharamaiah, G.M. (1991) Apolipoprotein A-I Decreases Neutrophil Degranulation and Superoxide Production, J. Lipid Res. 32, 1911–1918.
Furlaneto, C.J., and Campa, A. (2000) A Novel Function of Serum Amyloid A: A Potent Stimulus for the Release of Tumor Necrosis Factor-α, Interleukin-1β, and Interleukin-8 by Human Blood Neutrophils, Biochem. Biophys. Res. Commun. 268, 405–408.
Morrison, D.C., and Jacobs, D.M. (1976) Binding of Polymixin B to the Lipid A Portion of Bacterial Lipopolysaccharides, Immunochemistry 13, 813–818.
Scapini, P., Calzetti, F., and Cassatella, M.A. (1999) On the Detection of Neutrophil-Derived Vascular Endothelial Growth Factor (VEGF), J. Immunol. Methods 232, 121–129.
Flohé, L., and Otting, F. (1984) Superoxide Dismutase Assays, Methods Enzymol. 105, 93–104.
Castellani, L.W., Navab, M., Lenten, B.J., Hedrick, C.C., Hama, S.Y., Goto, A.M., Fogelman, A.M., and Lusis, A.J. (1997) Over-expression of Apolipoprotein AII in Transgenic Mice Converts High Density Lipoproteins to Proinflammatory Particles, J. Clin. Invest. 100, 464–474.
Hyka, N., Dayer, J.M., Modoux, C., Kohno, T., Edwards C.K., III, Roux-Lombard, P., and Burger, D., Apolipoprotein A-I Inhibits the Production of Interleukin-1β and Tumor Necrosis Factor-α by Blocking Contact-Mediated Activation of Monocytes by T Lymphocytes, Blood 97, 2381–2389.
Cassatella, M.A., Meda, L., Gasperini, S., Calzetti, F., and Bonora, S. (1994) Interleukin 10 (IL-10) Upregulates IL-1 Receptor Antagonist Production from Lipopolysaccharide-Stimulated Human Polymorphonuclear Leukocytes by Delaying mRNA Degradation, J. Exp. Med. 179, 1695–1699.
Lagocki, P.A., and Scanu, A.M. (1980) In vitro Modulation of the Apolipoprotein Composition of High Density Lipoprotein. Displacement of Apolipoprotein AI from High Density Lipoprotein by Apolipoprotein A-II, J. Biol. Chem. 255, 3701–3706.
Ashby, D., Gamble, J., Vadas, M., Fidge, N., Siggins, S., Rye, K., and Barter, P.J. (2001) Lack of Effect of Serum Amyloid A (SAA) on the Ability of High-Density Lipoproteins to Inhibit Endothelial Cell Adhesion Molecule Expression, Atherosclerosis 154, 113–121.
Author information
Authors and Affiliations
Corresponding author
About this article
Cite this article
Furlaneto, C.J., Ribeiro, F.P., Hatanaka, E. et al. Apolipoproteins A-I and A-II downregulate neutrophil functions. Lipids 37, 925–928 (2002). https://doi.org/10.1007/s11745-002-0981-4
Received:
Revised:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/s11745-002-0981-4