메뉴 건너뛰기




Volumn 39, Issue 11, 1998, Pages 2150-2160

Lipoproteins are substrates for human secretory group IIA phospholipase A2: Preferential hydrolysis of acute phase HDL

Author keywords

Atherosclerosis; Free fatty acids; Group IIA phospholipase A2; Hydrolysis; Lipoproteins; Lysophosphatidylcholine

Indexed keywords

ALKENYL GROUP; ALKYL ETHER; ARACHIDONIC ACID; CHOLINE; FATTY ACID; HIGH DENSITY LIPOPROTEIN; LINOLENIC ACID; LIPOPROTEIN; LYSOPHOSPHATIDYLCHOLINE; PHOSPHATIDYLETHANOLAMINE; PHOSPHOLIPASE A2; SERUM AMYLOID A; SPHINGOMYELIN;

EID: 0031785119     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (85)

References (51)
  • 5
    • 0025174365 scopus 로고
    • 2 mRNA synthesis is stimulated by two distinct mechanisms in rat vascular smooth muscle cells
    • 2 mRNA synthesis is stimulated by two distinct mechanisms in rat vascular smooth muscle cells. FEBS Lett. 261: 171-174.
    • (1990) FEBS Lett. , vol.261 , pp. 171-174
    • Nakano, T.1    Ohara, O.2    Teraoka, H.3    Arita, H.4
  • 9
    • 0030798853 scopus 로고    scopus 로고
    • 2 gene family in mammals
    • 2 gene family in mammals. J. Biol. Chem. 272: 17247-17250.
    • (1997) J. Biol. Chem. , vol.272 , pp. 17247-17250
    • Tischfield, J.A.1
  • 10
    • 0028859490 scopus 로고
    • Anti-inflammatory HDL becomes pro-inflammatory during the acute phase response. Loss of protective effect of HDL against LDL oxidation in aortic wall cell co-cultures
    • Van Lenten, B. J., S. Y. Hama, F. C. de Beer, D. M. Stafforini, T. M. McIntyre, S. M. Prescott, B. N. La Du, A. M. Fogelman, and M. Navab. 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 co-cultures. J. Clin. Invest. 96: 2758-2767.
    • (1995) J. Clin. Invest. , vol.96 , pp. 2758-2767
    • Van Lenten, B.J.1    Hama, S.Y.2    De Beer, F.C.3    Stafforini, D.M.4    McIntyre, T.M.5    Prescott, S.M.6    La Du, B.N.7    Fogelman, A.M.8    Navab, M.9
  • 11
    • 0025268435 scopus 로고
    • High-density lipoprotein inhibits the oxidative modification of low-density lipoprotein
    • Parthasarathy, S., J. Barnett, and L. C. Fong. 1990. High-density lipoprotein inhibits the oxidative modification of low-density lipoprotein. Biochim. Biophys. Acta. 1044: 275-283.
    • (1990) Biochim. Biophys. Acta , vol.1044 , pp. 275-283
    • Parthasarathy, S.1    Barnett, J.2    Fong, L.C.3
  • 12
    • 0024996141 scopus 로고
    • Plasma high density lipoproteins. Metabolism and relationship to atherogenesis
    • Tall, A. R. 1990. Plasma high density lipoproteins. Metabolism and relationship to atherogenesis. J. Clin. Invest. 86: 379-384.
    • (1990) J. Clin. Invest. , vol.86 , pp. 379-384
    • Tall, A.R.1
  • 13
    • 0022259289 scopus 로고
    • Mechanism of the hepatic lipase induced accumulation of high-density lipoprotein cholesterol by cells in culture
    • Bamberger, M., S. Lund-Katz, M. C. Phillips, and G. H. Rothblat. 1985. Mechanism of the hepatic lipase induced accumulation of high-density lipoprotein cholesterol by cells in culture. Biochemistry. 24: 3693-3701.
    • (1985) Biochemistry , vol.24 , pp. 3693-3701
    • Bamberger, M.1    Lund-Katz, S.2    Phillips, M.C.3    Rothblat, G.H.4
  • 15
    • 0026613053 scopus 로고
    • 2-modified LDL is taken up at enhanced rate by macrophages
    • 2-modified LDL is taken up at enhanced rate by macrophages. Biochem. Biophys. Res. Commun. 185: 465-472.
    • (1992) Biochem. Biophys. Res. Commun. , vol.185 , pp. 465-472
    • Aviram, M.1    Maor, I.2
  • 17
    • 0023037824 scopus 로고
    • Serum amyloid A-containing human high density lipoprotein 3. Density, size, and apolipoprotein composition
    • Coetzee, G. A., A. F. Strachan, D. R. van der Westhuyzen, H. C. Hoppe, M. S. Jeenah, and F. C. de Beer. 1986. Serum amyloid A-containing human high density lipoprotein 3. Density, size, and apolipoprotein composition. J. Biol. Chem. 261: 9644-9651.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9644-9651
    • Coetzee, G.A.1    Strachan, A.F.2    Van Der Westhuyzen, D.R.3    Hoppe, H.C.4    Jeenah, M.S.5    De Beer, F.C.6
  • 19
    • 0016663362 scopus 로고
    • Quantification of Coomassie Blue-stained proteins in polyacrylamide gels based on analyses of eluted dye
    • Fenner, C., R. R. Trant, D. T. Mason, and J. W. Wikman-Coffelt. 1975. Quantification of Coomassie Blue-stained proteins in polyacrylamide gels based on analyses of eluted dye. Anal. Biochem. 63: 595-602.
    • (1975) Anal. Biochem. , vol.63 , pp. 595-602
    • Fenner, C.1    Trant, R.R.2    Mason, D.T.3    Wikman-Coffelt, J.W.4
  • 20
    • 0020973547 scopus 로고
    • Receptor-mediated endocytosis of low-density lipoprotein in cultured cells
    • Goldstein, J. L., S .K. Basu, and M. S. Brown. 1983. Receptor-mediated endocytosis of low-density lipoprotein in cultured cells. Meth. Enzymol. 98: 241-260.
    • (1983) Meth. Enzymol. , vol.98 , pp. 241-260
    • Goldstein, J.L.1    Basu, S.K.2    Brown, M.S.3
  • 22
    • 70449158340 scopus 로고
    • A simple method for the isolation and purification of total lipids from animal tissue
    • Folch, J., M. Lees, and G. H. Sloane Stanley. 1957. A simple method for the isolation and purification of total lipids from animal tissue. J. Biol. Chem. 226: 497-509.
    • (1957) J. Biol. Chem. , vol.226 , pp. 497-509
    • Folch, J.1    Lees, M.2    Sloane Stanley, G.H.3
  • 23
    • 0024332379 scopus 로고
    • Molecular species of glycerophospholipids and sphingomyelins of human erythrocytes: Improved method of analysis
    • Myher, J. J., A. Kuksis, and S. Pind. 1989. Molecular species of glycerophospholipids and sphingomyelins of human erythrocytes: improved method of analysis. Lipids. 24: 396-407.
    • (1989) Lipids , vol.24 , pp. 396-407
    • Myher, J.J.1    Kuksis, A.2    Pind, S.3
  • 24
    • 0024320626 scopus 로고
    • Molecular species of glycerophospholipids and sphingomyelins of human plasma: Comparison to red blood cells
    • Myher, J. J., A. Kuksis, and S. Pind. 1989. Molecular species of glycerophospholipids and sphingomyelins of human plasma: comparison to red blood cells. Lipids. 24: 408-418.
    • (1989) Lipids , vol.24 , pp. 408-418
    • Myher, J.J.1    Kuksis, A.2    Pind, S.3
  • 25
    • 0021736887 scopus 로고
    • Determination of plasma total lipid profiles by capillary gas-liquid chromatography
    • Myher, J. J., and A. Kuksis. 1984. Determination of plasma total lipid profiles by capillary gas-liquid chromatography. J. Biochem. Biophys. Methods. 10: 13-23.
    • (1984) J. Biochem. Biophys. Methods , vol.10 , pp. 13-23
    • Myher, J.J.1    Kuksis, A.2
  • 26
    • 0028808781 scopus 로고
    • Determination of lipid ester ozonides and core aldehydes by high-performance liquid chromatography with on-line mass spectrometry
    • Ravandi, A., A. Kuksis, J. J. Myher, and L. Marai. 1995. Determination of lipid ester ozonides and core aldehydes by high-performance liquid chromatography with on-line mass spectrometry. J. Biochem. Biophys. Methods. 30: 271-285.
    • (1995) J. Biochem. Biophys. Methods , vol.30 , pp. 271-285
    • Ravandi, A.1    Kuksis, A.2    Myher, J.J.3    Marai, L.4
  • 28
    • 0026647903 scopus 로고
    • Serum amyloid A changes high density lipoproteins cellular affinity. A clue to serum amyloid A's principal function
    • Kisilevsky, R., and L. Subrahmanyan. 1992. Serum amyloid A changes high density lipoproteins cellular affinity. A clue to serum amyloid A's principal function. Lab. Invest. 66: 778-785.
    • (1992) Lab. Invest. , vol.66 , pp. 778-785
    • Kisilevsky, R.1    Subrahmanyan, L.2
  • 29
    • 0019969508 scopus 로고
    • Serum amyloid-A-protein concentration in inflammatory diseases and its relationship t1o the incidence of reactive systemic amyloidosis
    • de Beer, F. C., E. A. Fagan, G. R. V. Hughes, R. K. Mallya, J. G. Lanham, and M.B. Pepys. 1982. Serum amyloid-A-protein concentration in inflammatory diseases and its relationship t1o the incidence of reactive systemic amyloidosis. Lancet. 2: 231-234.
    • (1982) Lancet , vol.2 , pp. 231-234
    • De Beer, F.C.1    Fagan, E.A.2    Hughes, G.R.V.3    Mallya, R.K.4    Lanham, J.G.5    Pepys, M.B.6
  • 30
    • 0028202075 scopus 로고
    • Expression of apolipoprotein serum amyloid A mRNA in human atherosclerotic lesions and cultured vascular cells: Impliations for serum amyloid A function
    • Meek, R. L., S. Urieli-Shoval, and E. P. Benditt. 1994. Expression of apolipoprotein serum amyloid A mRNA in human atherosclerotic lesions and cultured vascular cells: impliations for serum amyloid A function. Proc. Natl. Acad. Sci. USA. 91: 3186-3190.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3186-3190
    • Meek, R.L.1    Urieli-Shoval, S.2    Benditt, E.P.3
  • 33
    • 0025281462 scopus 로고
    • Syndromes of accelerated atherosclerosis: Role of vascular injury and smooth muscle cell proliferation
    • Ip, J. H., V. Fuster, L. Badimon, J. Badimon, M. B. Taubman, and J. H. Chesebro. 1990. Syndromes of accelerated atherosclerosis: role of vascular injury and smooth muscle cell proliferation. J. Am. Coll. Cardiol. 15: 1667-1687.
    • (1990) J. Am. Coll. Cardiol. , vol.15 , pp. 1667-1687
    • Ip, J.H.1    Fuster, V.2    Badimon, L.3    Badimon, J.4    Taubman, M.B.5    Chesebro, J.H.6
  • 34
    • 0029862974 scopus 로고    scopus 로고
    • 2 enzymes present in P388D1 macrophages
    • 2 enzymes present in P388D1 macrophages. J. Biol. Chem. 271: 6758-6765.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6758-6765
    • Balsinde, J.1    Dennis, E.A.2
  • 39
    • 0026781978 scopus 로고
    • Lysophosphatidylcholine, a component of atherogenic lipoproteins, induces mononuclear leukocyte adhesion molecules in cultured human and rabbit arterial endothelial cells
    • Kume, N., M. I. Cybulsky, and M. A. Gimbrone, Jr. 1992. Lysophosphatidylcholine, a component of atherogenic lipoproteins, induces mononuclear leukocyte adhesion molecules in cultured human and rabbit arterial endothelial cells. J. Clin. Invest. 90: 1138-1144.
    • (1992) J. Clin. Invest. , vol.90 , pp. 1138-1144
    • Kume, N.1    Cybulsky, M.I.2    Gimbrone Jr., M.A.3
  • 41
    • 0001096583 scopus 로고
    • Lysophosphatidylcholine: A chemotactic factor for human monocytes and its potential role in atherogenesis
    • Quinn, M. T., S. Parthasarathy, and D. Steinberg. 1988. Lysophosphatidylcholine: a chemotactic factor for human monocytes and its potential role in atherogenesis. Proc. Natl. Acad. Sci. USA. 85: 2805-2809.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2805-2809
    • Quinn, M.T.1    Parthasarathy, S.2    Steinberg, D.3
  • 42
    • 0029920565 scopus 로고    scopus 로고
    • Expression of human phospholipid hydroperoxide glutathione peroxidase gene for protection of host cells from lipid hydroperoxide-mediated injury
    • Yagi, K., S. Komura, H. Kojima, Q. Sun, N. Nagata, N. Ohishi, and M. Nishikimi. 1996. Expression of human phospholipid hydroperoxide glutathione peroxidase gene for protection of host cells from lipid hydroperoxide-mediated injury. Biochem. Biophys. Res. Commun. 219: 486-491.
    • (1996) Biochem. Biophys. Res. Commun. , vol.219 , pp. 486-491
    • Yagi, K.1    Komura, S.2    Kojima, H.3    Sun, Q.4    Nagata, N.5    Ohishi, N.6    Nishikimi, M.7
  • 43
    • 0029996539 scopus 로고    scopus 로고
    • Cytotoxicity of phosphatidylcholine hydroperoxides is exerted through decomposition of fatty acid hydroperoxide moiety
    • Kaneko, T., N. Baba, and M. Matsuo. 1996. Cytotoxicity of phosphatidylcholine hydroperoxides is exerted through decomposition of fatty acid hydroperoxide moiety. Free Radical Biol. Med. 21: 173-179.
    • (1996) Free Radical Biol. Med. , vol.21 , pp. 173-179
    • Kaneko, T.1    Baba, N.2    Matsuo, M.3
  • 44
    • 0026332055 scopus 로고
    • HDL: Structure, function and metabolism
    • Brewer, H. B., Jr., and D. J. Racier. 1991. HDL: structure, function and metabolism. Prog, Lipid Res. 30: 139-144.
    • (1991) Prog, Lipid Res. , vol.30 , pp. 139-144
    • Brewer Jr., H.B.1    Racier, D.J.2
  • 45
    • 0026333959 scopus 로고
    • Role of oxidized low density lipoprotein in atherogenesis
    • Witztum, J. L., and D. Steinberg. 1991. Role of oxidized low density lipoprotein in atherogenesis. J. Clin. Invest. 88: 1785-1792.
    • (1991) J. Clin. Invest. , vol.88 , pp. 1785-1792
    • Witztum, J.L.1    Steinberg, D.2
  • 46
    • 0024603895 scopus 로고
    • Beyond cholesterol. Modifications of low-density lipoprotein that increase its atherogenicity
    • Steinberg, D., S. Parthasarathy, T. E. Carew, J. C. Khoo, and J. L. Witztum. 1989. Beyond cholesterol. Modifications of low-density lipoprotein that increase its atherogenicity. N. Engl. J. Med. 320:915-924.
    • (1989) N. Engl. J. Med. , vol.320 , pp. 915-924
    • Steinberg, D.1    Parthasarathy, S.2    Carew, T.E.3    Khoo, J.C.4    Witztum, J.L.5
  • 48
    • 0029883764 scopus 로고    scopus 로고
    • The role of oxidized lipoproteins in atherogenesis
    • Berliner, J. A., and J. W. Heinecke. 1996. The role of oxidized lipoproteins in atherogenesis. Free Radical Biol. & Med. 30: 707-727.
    • (1996) Free Radical Biol. & Med. , vol.30 , pp. 707-727
    • Berliner, J.A.1    Heinecke, J.W.2
  • 49
    • 0030046797 scopus 로고    scopus 로고
    • Identification of scavenger receptor SR-BI as a high density lipoprotein receptor
    • Acton, S., A. Rigotti, K. T. Landschulz, S. Xu, H. H. Hobbs, and M. Krieger. 1996. Identification of scavenger receptor SR-BI as a high density lipoprotein receptor. Science. 271: 518-520.
    • (1996) Science , vol.271 , pp. 518-520
    • Acton, S.1    Rigotti, A.2    Landschulz, K.T.3    Xu, S.4    Hobbs, H.H.5    Krieger, M.6
  • 51
    • 0029009131 scopus 로고
    • Fatty acid modulation of cell responsiveness
    • Rotondo, D. 1995. Fatty acid modulation of cell responsiveness. Biochem. Soc. Trans. 23: 191-196.
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 191-196
    • Rotondo, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.