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Volumn 50, Issue 1, 2011, Pages 102-109

HDL-associated paraoxonase-1 can redistribute to cell membranes and influence sensitivity to oxidative stress

Author keywords

Atherosclerosis; Bacterial virulence; Endothelium; Free radicals; Lipoprotein; Oxidative stress; Quorum quenching

Indexed keywords

ARYLDIALKYLPHOSPHATASE 1; CYCLODEXTRIN; HIGH DENSITY LIPOPROTEIN; LIPOPROTEIN; SCAVENGER RECEPTOR BI;

EID: 78650703449     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2010.09.002     Document Type: Article
Times cited : (86)

References (37)
  • 2
    • 0035170229 scopus 로고    scopus 로고
    • High density lipoproteins and arteriosclerosis: Role of cholesterol efflux and reverse cholesterol transport
    • A. von Eckardstein, J.R. Nofer, and G. Assmann High density lipoproteins and arteriosclerosis: role of cholesterol efflux and reverse cholesterol transport Arterioscler. Thromb. Vasc. Biol. 21 2001 13 27
    • (2001) Arterioscler. Thromb. Vasc. Biol. , vol.21 , pp. 13-27
    • Von Eckardstein, A.1    Nofer, J.R.2    Assmann, G.3
  • 4
    • 0027763632 scopus 로고
    • Protection of low-density lipoprotein against oxidative modification by high-density lipoprotein associated paraoxonase
    • M.I. Mackness, S. Arrol, C. Abbot, and P.N. Durrington Protection of low-density lipoprotein against oxidative modification by high-density lipoprotein associated paraoxonase Atherosclerosis 104 1993 129 135
    • (1993) Atherosclerosis , vol.104 , pp. 129-135
    • Mackness, M.I.1    Arrol, S.2    Abbot, C.3    Durrington, P.N.4
  • 10
    • 0037040274 scopus 로고    scopus 로고
    • Enzymatically active paraoxonase-1 is located at the external membrane of producing cells and released by a high affinity, saturable, desorption mechanism
    • S. Deakin, I. Leviev, M. Gomaraschi, L. Calabresi, G. Franceschini, and R.W. James Enzymatically active paraoxonase-1 is located at the external membrane of producing cells and released by a high affinity, saturable, desorption mechanism J. Biol. Chem. 277 2002 4301 4308
    • (2002) J. Biol. Chem. , vol.277 , pp. 4301-4308
    • Deakin, S.1    Leviev, I.2    Gomaraschi, M.3    Calabresi, L.4    Franceschini, G.5    James, R.W.6
  • 11
    • 33745026603 scopus 로고
    • The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum
    • R.J. Havel, H.A. Eder, and J.H. Bragton The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum J. Clin. Invest. 34 1955 1345 1353
    • (1955) J. Clin. Invest. , vol.34 , pp. 1345-1353
    • Havel, R.J.1    Eder, H.A.2    Bragton, J.H.3
  • 12
    • 0027412483 scopus 로고
    • Identification of a distinct human high-density lipoprotein subspecies defined by a lipoprotein-associated protein, K-45: Identity of K-45 with paraoxonase
    • M.-C. Blatter, R.W. James, S. Messmer, F. Barja, and D. Pometta Identification of a distinct human high-density lipoprotein subspecies defined by a lipoprotein-associated protein, K-45: identity of K-45 with paraoxonase Eur. J. Biochem. 211 1993 871 879
    • (1993) Eur. J. Biochem. , vol.211 , pp. 871-879
    • Blatter, M.-C.1    James, R.W.2    Messmer, S.3    Barja, F.4    Pometta, D.5
  • 13
    • 0029055646 scopus 로고
    • Reactive oxygen intermediates induce regulated secretion of von Willebrand factor from cultured human vascular endothelial cells
    • U.M. Vischer, L. Jornot, C.B. Wollheim, and J.M. Theler Reactive oxygen intermediates induce regulated secretion of von Willebrand factor from cultured human vascular endothelial cells Blood 85 1995 3164 3172
    • (1995) Blood , vol.85 , pp. 3164-3172
    • Vischer, U.M.1    Jornot, L.2    Wollheim, C.B.3    Theler, J.M.4
  • 14
    • 0343114388 scopus 로고    scopus 로고
    • Structure-activity relationship of staurosporine analogs in regulating expression of endothelial nitric-oxide synthase gene
    • H. Li, and U. Forstermann Structure-activity relationship of staurosporine analogs in regulating expression of endothelial nitric-oxide synthase gene Mol. Pharmacol. 57 2000 427 435
    • (2000) Mol. Pharmacol. , vol.57 , pp. 427-435
    • Li, H.1    Forstermann, U.2
  • 15
    • 0037609040 scopus 로고    scopus 로고
    • Posttranscriptional control of quorum-sensing-dependent virulence genes by DksA in Pseudomonas aeruginosa
    • F. Jude, T. Köhler, P. Branny, K. Perron, M.P. Mayer, R. Comte, and C. van Delden Posttranscriptional control of quorum-sensing-dependent virulence genes by DksA in Pseudomonas aeruginosa J. Bacteriol. 185 2003 3558 3566
    • (2003) J. Bacteriol. , vol.185 , pp. 3558-3566
    • Jude, F.1    Köhler, T.2    Branny, P.3    Perron, K.4    Mayer, M.P.5    Comte, R.6    Van Delden, C.7
  • 16
    • 34247213490 scopus 로고    scopus 로고
    • Paraoxonase-2 reduces oxidative stress in vascular cells and decreases endoplasmic reticulum stress-induced caspase activation
    • S. Horke, I. Witte, P. Wilgenbus, M. Krüger, D. Strand, and U. Förstermann Paraoxonase-2 reduces oxidative stress in vascular cells and decreases endoplasmic reticulum stress-induced caspase activation Circulation 115 2007 2055 2064
    • (2007) Circulation , vol.115 , pp. 2055-2064
    • Horke, S.1    Witte, I.2    Wilgenbus, P.3    Krüger, M.4    Strand, D.5    Förstermann, U.6
  • 17
    • 0028306066 scopus 로고
    • Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides
    • S.P. Wolff Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides Meth. Enzymol. 233 1994 182 189
    • (1994) Meth. Enzymol. , vol.233 , pp. 182-189
    • Wolff, S.P.1
  • 18
    • 0032820452 scopus 로고    scopus 로고
    • Quantifying cellular oxidative stress by dichlorofluorescein assay using microplate reader
    • H. Wang, and J.A. Joseph Quantifying cellular oxidative stress by dichlorofluorescein assay using microplate reader Free Radic. Biol. Med. 27 1999 612 616
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 612-616
    • Wang, H.1    Joseph, J.A.2
  • 19
    • 0021192013 scopus 로고
    • Cytoskeleton of rat aortic smooth muscle cells: Normal conditions and experimental intimal thickening
    • O. Kocher, O. Skalli, W.S. Bloom, and G. Gabbiani Cytoskeleton of rat aortic smooth muscle cells: normal conditions and experimental intimal thickening Lab. Investig. 50 1984 645 652 (Pubitemid 14119416)
    • (1984) Laboratory Investigation , vol.50 , Issue.6 , pp. 645-652
    • Kocher, O.1    Skalli, O.2    Bloom, W.S.3    Gabbiani, G.4
  • 21
    • 0022881517 scopus 로고
    • A monoclonal antibody against alpha-smooth muscle actin: A new probe for smooth muscle differentiation
    • O. Skalli, P. Ropraz, A. Trzeciak, G. Benzonana, D. Gillessen, and G. Gabbiani A monoclonal antibody against alpha-smooth muscle actin: a new probe for smooth muscle differentiation J. Cell Biol. 103 1986 2787 2796
    • (1986) J. Cell Biol. , vol.103 , pp. 2787-2796
    • Skalli, O.1    Ropraz, P.2    Trzeciak, A.3    Benzonana, G.4    Gillessen, D.5    Gabbiani, G.6
  • 23
    • 0032877947 scopus 로고    scopus 로고
    • Human serum paraoxonase/arylesterase's retained hydrophobic N-terminal leader sequence associates with HDLs by binding phospholipids: Apolipoprotein A-I stabilizes activity
    • R.C. Sorenson, C.L. Bisgaier, M. Aviram, C. Hsu, S. Billecke, and B.N. La Du Human serum paraoxonase/arylesterase's retained hydrophobic N-terminal leader sequence associates with HDLs by binding phospholipids: apolipoprotein A-I stabilizes activity Arterioscler. Thromb. Vasc. Biol. 19 1999 2214 2225
    • (1999) Arterioscler. Thromb. Vasc. Biol. , vol.19 , pp. 2214-2225
    • Sorenson, R.C.1    Bisgaier, C.L.2    Aviram, M.3    Hsu, C.4    Billecke, S.5    La Du, B.N.6
  • 25
    • 60549091035 scopus 로고    scopus 로고
    • High-density lipoproteins, inflammation and oxidative stress
    • F. Tabet, and K.A. Rye High-density lipoproteins, inflammation and oxidative stress Clin. Sci. 116 2009 87 98
    • (2009) Clin. Sci. , vol.116 , pp. 87-98
    • Tabet, F.1    Rye, K.A.2
  • 26
    • 17644367506 scopus 로고    scopus 로고
    • Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase
    • O. Khersonsky, and D.S. Tawfik Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase Biochemistry 44 2005 6371 6382
    • (2005) Biochemistry , vol.44 , pp. 6371-6382
    • Khersonsky, O.1    Tawfik, D.S.2
  • 27
    • 0042261695 scopus 로고    scopus 로고
    • Lactonase and lactonizing activities of human serum paraoxonase (PON1) and rabbit serum PON3
    • J.F. Teiber, D.I. Draganov, and B.N. La Du Lactonase and lactonizing activities of human serum paraoxonase (PON1) and rabbit serum PON3 Biochem. Pharmacol. 66 2003 887 896
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 887-896
    • Teiber, J.F.1    Draganov, D.I.2    La Du, B.N.3
  • 28
    • 13844298811 scopus 로고    scopus 로고
    • Very low density lipoproteins provide a vector for secretion of paraoxonase-1 from cells
    • S. Deakin, X. Moren, and R.W. James Very low density lipoproteins provide a vector for secretion of paraoxonase-1 from cells Atherosclerosis 179 2005 17 25
    • (2005) Atherosclerosis , vol.179 , pp. 17-25
    • Deakin, S.1    Moren, X.2    James, R.W.3
  • 32
    • 33644542104 scopus 로고    scopus 로고
    • Oxidative stress promotes polarization of human T cell differentiation towards a T helper 2 phenotype
    • M.R. King, A.S. Ismail, L.S. Davis, and D.R. Karp Oxidative stress promotes polarization of human T cell differentiation towards a T helper 2 phenotype J. Immunol. 176 2006 2765 2772
    • (2006) J. Immunol. , vol.176 , pp. 2765-2772
    • King, M.R.1    Ismail, A.S.2    Davis, L.S.3    Karp, D.R.4
  • 33
    • 52049103174 scopus 로고    scopus 로고
    • Macrophage paraoxonase 1 (PON1) binding sites
    • M. Efrat, and M. Aviram Macrophage paraoxonase 1 (PON1) binding sites Biochem. Biophys. Res. Commun. 376 2008 105 110
    • (2008) Biochem. Biophys. Res. Commun. , vol.376 , pp. 105-110
    • Efrat, M.1    Aviram, M.2
  • 34
    • 46249112510 scopus 로고    scopus 로고
    • Dominant role of paraoxonases in inactivation of the Pseudomonas aeruginosa quorum-sensing signal N-(3-oxododecanoyl)-l-homoserine lactone
    • J.F. Teiber, S. Horke, D.C. Haines, P.K. Chowdhary, J. Xiao, G.L. Kramer, R.W. Haley, and D.I. Draganov Dominant role of paraoxonases in inactivation of the Pseudomonas aeruginosa quorum-sensing signal N-(3-oxododecanoyl)-l- homoserine lactone Infect. Immun. 76 2008 2512 2519
    • (2008) Infect. Immun. , vol.76 , pp. 2512-2519
    • Teiber, J.F.1    Horke, S.2    Haines, D.C.3    Chowdhary, P.K.4    Xiao, J.5    Kramer, G.L.6    Haley, R.W.7    Draganov, D.I.8
  • 37
    • 0030753875 scopus 로고    scopus 로고
    • Increased immunolocalization of paraoxonase, clusterin, and apolipoprotein A-I in the human artery wall with the progression of atherosclerosis
    • B. Mackness, R. Hunt, P.N. Durrington, and M.I. Mackness Increased immunolocalization of paraoxonase, clusterin, and apolipoprotein A-I in the human artery wall with the progression of atherosclerosis Arterioscler. Thromb. Vasc. Biol. 17 1997 1233 1238
    • (1997) Arterioscler. Thromb. Vasc. Biol. , vol.17 , pp. 1233-1238
    • Mackness, B.1    Hunt, R.2    Durrington, P.N.3    Mackness, M.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.