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Volumn 58, Issue 1, 2003, Pages 5-14

Mechanism of action of statins and fibrates;Mécanismes d'action des statines et des fibrates

Author keywords

Dyslipoproteinaemias; Fibrates; PPAR ; Statins

Indexed keywords

FIBRIC ACID DERIVATIVE; HIGH DENSITY LIPOPROTEIN CHOLESTEROL; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; LOW DENSITY LIPOPROTEIN CHOLESTEROL; STATIN; VERY LOW DENSITY LIPOPROTEIN CHOLESTEROL;

EID: 0038284773     PISSN: 00405957     EISSN: None     Source Type: Journal    
DOI: 10.2515/therapie:2003002     Document Type: Review
Times cited : (27)

References (59)
  • 1
    • 0036790614 scopus 로고    scopus 로고
    • Statin therapy in acute coronary syndromes: Mechanistic insight into clinical benefit
    • Sposito AC, Chapman MJ. Statin therapy in acute coronary syndromes: mechanistic insight into clinical benefit. Arterioscler Thromb Vasc Biol 2002; 22: 1524-34
    • (2002) Arterioscler Thromb Vasc Biol , vol.22 , pp. 1524-1534
    • Sposito, A.C.1    Chapman, M.J.2
  • 2
    • 0026027862 scopus 로고
    • Lowering of plasma cholesterol levels in animals by lovastatin and simvastatin
    • Chao Y, Chen JS, Hunt VM, et al. Lowering of plasma cholesterol levels in animals by lovastatin and simvastatin. Eur J Clin Pharmacol 1991; 40 Suppl. 1: S11-4
    • (1991) Eur J Clin Pharmacol , vol.40 , Issue.SUPPL. 1
    • Chao, Y.1    Chen, J.S.2    Hunt, V.M.3
  • 3
    • 0035996592 scopus 로고    scopus 로고
    • Influence of atorvastatin and simvastatin on apolipoprotein B metabolism in moderate combined hyperlipidemic subjects with low VLDL and LDL fractional clearance rates
    • Forster LF, Stewart G, Bedford D, et al. Influence of atorvastatin and simvastatin on apolipoprotein B metabolism in moderate combined hyperlipidemic subjects with low VLDL and LDL fractional clearance rates. Atherosclerosis 2002; 164: 129-45
    • (2002) Atherosclerosis , vol.164 , pp. 129-145
    • Forster, L.F.1    Stewart, G.2    Bedford, D.3
  • 4
    • 0022549920 scopus 로고
    • A receptor-mediated pathway for cholesterol homeostasis
    • Brown MS, Goldstein JL. A receptor- mediated pathway for cholesterol homeostasis. Science 1986; 232: 34-47
    • (1986) Science , vol.232 , pp. 34-47
    • Brown, M.S.1    Goldstein, J.L.2
  • 5
    • 0025992946 scopus 로고
    • Influence of lovastatin therapy on metabolism of low density lipoproteins in mixed hyperlipidaemia
    • Vega GL, Grundy SM. Influence of lovastatin therapy on metabolism of low density lipoproteins in mixed hyperlipidaemia. J Intern Med 1991; 230: 341-50
    • (1991) J Intern Med , vol.230 , pp. 341-350
    • Vega, G.L.1    Grundy, S.M.2
  • 6
    • 0020899787 scopus 로고
    • Mevinolin stimulates receptor-mediated clearance of low density lipoprotein from plasma in familial hypercholesterolemia heterozygotes
    • Bilheimer DW, Grundy SM, Brown MS, et al. Mevinolin stimulates receptor-mediated clearance of low density lipoprotein from plasma in familial hypercholesterolemia heterozygotes. Trans Assoc Am Phys 1983; 96: 1-9
    • (1983) Trans Assoc Am Phys , vol.96 , pp. 1-9
    • Bilheimer, D.W.1    Grundy, S.M.2    Brown, M.S.3
  • 7
    • 0019469390 scopus 로고
    • Dihydromevinolin, a potent hypocholesterolemic metabolite produced by aspergillus terreus
    • Albers-Schonberg G, Joshua H, Lopez MB, et al. Dihydromevinolin, a potent hypocholesterolemic metabolite produced by aspergillus terreus. J Antibiot (Tokyo) 1981; 34: 507-12
    • (1981) J Antibiot (Tokyo) , vol.34 , pp. 507-512
    • Albers-Schonberg, G.1    Joshua, H.2    Lopez, M.B.3
  • 8
    • 0023754423 scopus 로고
    • Discovery, biochemistry and biology of lovastatin
    • Alberts AW. Discovery, biochemistry and biology of lovastatin. Am J Cardiol 1988; 62: 10J-5J
    • (1988) Am J Cardiol , vol.62
    • Alberts, A.W.1
  • 9
    • 0017055252 scopus 로고
    • ML-236A, ML-236B, and ML-236C, new inhibitors of cholesterogenesis produced by penicillium citrinium
    • Endo A, Kuroda M, Tsujita Y. ML-236A, ML-236B, and ML-236C, new inhibitors of cholesterogenesis produced by penicillium citrinium. J Antibiot (Tokyo) 1976; 29: 1346-8
    • (1976) J Antibiot (Tokyo) , vol.29 , pp. 1346-1348
    • Endo, A.1    Kuroda, M.2    Tsujita, Y.3
  • 10
    • 0030941803 scopus 로고    scopus 로고
    • The SREBP pathway: Regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor
    • Brown MS, Goldstein JL. The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. Cell 1997; 89: 331-40
    • (1997) Cell , vol.89 , pp. 331-340
    • Brown, M.S.1    Goldstein, J.L.2
  • 11
    • 0031892148 scopus 로고    scopus 로고
    • Sterol regulation of 3-hydroxy-3-methylglutaryl-coenzyme A synthase gene through a direct interaction between sterol regulatory element binding protein and the trimeric CCAAT-binding factor/nuclear factor Y
    • Dooley KA, Millinder S, Osborne TF. Sterol regulation of 3-hydroxy-3-methylglutaryl-coenzyme A synthase gene through a direct interaction between sterol regulatory element binding protein and the trimeric CCAAT-binding factor/nuclear factor Y. J Biol Chem 1998; 273: 1349-56
    • (1998) J Biol Chem , vol.273 , pp. 1349-1356
    • Dooley, K.A.1    Millinder, S.2    Osborne, T.F.3
  • 12
    • 0021042806 scopus 로고
    • Alterations in the rates of synthesis and degradation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A reductase produced by cholestyramine and mevinolin
    • Edwards PA, Lan SF, Fogelman AM. Alterations in the rates of synthesis and degradation of rat liver 3-hydroxy-3-methylglutaryl coenzyme A reductase produced by cholestyramine and mevinolin. J Biol Chem 1983; 258: 10219-22
    • (1983) J Biol Chem , vol.258 , pp. 10219-10222
    • Edwards, P.A.1    Lan, S.F.2    Fogelman, A.M.3
  • 13
    • 0032104180 scopus 로고    scopus 로고
    • Activation of cholesterol synthesis in preference to fatty acid synthesis in liver and adipose tissue of transgenic mice overproducing sterol regulatory element-binding protein-2
    • Horton JD, Shimomura I, Brown MS, et al. Activation of cholesterol synthesis in preference to fatty acid synthesis in liver and adipose tissue of transgenic mice overproducing sterol regulatory element-binding protein-2. J Clin Invest 1998; 101: 2331-9
    • (1998) J Clin Invest , vol.101 , pp. 2331-2339
    • Horton, J.D.1    Shimomura, I.2    Brown, M.S.3
  • 14
    • 0019140920 scopus 로고
    • Feedback regulation of 3-hydroxy-3methylglutaryl coenzyme A reductase in livers of mice treated with mevinolin, a competitive inhibitor of the reductase
    • Kita T, Brown MS, Goldstein JL. Feedback regulation of 3-hydroxy-3methylglutaryl coenzyme A reductase in livers of mice treated with mevinolin, a competitive inhibitor of the reductase. J Clin Invest 1980; 66: 1094-100
    • (1980) J Clin Invest , vol.66 , pp. 1094-1100
    • Kita, T.1    Brown, M.S.2    Goldstein, J.L.3
  • 15
    • 0023918754 scopus 로고
    • Localization of 3-hydroxy-3-methylglutaryl CoA reductase and 3-hydroxy-3-methylglutaryl CoA synthase in the rat liver and intestine is affected by cholestyramine and mevinolin
    • Li AC, Tanaka RD, Callaway K, et al. Localization of 3-hydroxy-3-methylglutaryl CoA reductase and 3-hydroxy-3-methylglutaryl CoA synthase in the rat liver and intestine is affected by cholestyramine and mevinolin. J Lipid Res 1988; 29: 781-96
    • (1988) J Lipid Res , vol.29 , pp. 781-796
    • Li, A.C.1    Tanaka, R.D.2    Callaway, K.3
  • 16
    • 0342620065 scopus 로고
    • Lovastatin, an inhibitor of cholesterol synthesis, induces hydroxymethylglutaryl-coenzyme A reductase directly on membranes of expanded smooth endoplasmic reticulum in rat hepatocytes
    • Singer II, Scott S, Kazazis DM, et al. Lovastatin, an inhibitor of cholesterol synthesis, induces hydroxymethylglutaryl-coenzyme A reductase directly on membranes of expanded smooth endoplasmic reticulum in rat hepatocytes. Proc Natl Acad Sci USA 1988; 85: 5264-8
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5264-5268
    • Singer, I.I.1    Scott, S.2    Kazazis, D.M.3
  • 17
    • 0003042048 scopus 로고
    • Mevinolin, an inhibitor of cholesterol synthesis, induces mRNA for low density lipoprotein receptor in livers of hamsters and rabbits
    • Ma PT, Gil G, Sudhof TC, et al. Mevinolin, an inhibitor of cholesterol synthesis, induces mRNA for low density lipoprotein receptor in livers of hamsters and rabbits. Proc Natl Acad Sci USA. 1986; 83: 8370-4
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 8370-8374
    • Ma, P.T.1    Gil, G.2    Sudhof, T.C.3
  • 18
    • 0031847229 scopus 로고    scopus 로고
    • Sterol-independent, sterol response elementdependent, regulation of low density lipoprotein receptor gene expression
    • Makar RS, Lipsky PE, Cuthbert JA. Sterol-independent, sterol response elementdependent, regulation of low density lipoprotein receptor gene expression. J Lipid Res 1998; 39: 1647-54
    • (1998) J Lipid Res , vol.39 , pp. 1647-1654
    • Makar, R.S.1    Lipsky, P.E.2    Cuthbert, J.A.3
  • 19
    • 0029799452 scopus 로고    scopus 로고
    • Serum response element-like sequences of the human low density lipoprotein receptor promoter: Possible regulation sites for sterol-independent transcriptional activation
    • Pak YK. Serum response element-like sequences of the human low density lipoprotein receptor promoter: possible regulation sites for sterol-independent transcriptional activation. Biochem Mol Biol Int 1996; 38: 31-6
    • (1996) Biochem Mol Biol Int , vol.38 , pp. 31-36
    • Pak, Y.K.1
  • 20
    • 0033613147 scopus 로고    scopus 로고
    • A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood
    • Brown MS, Goldstein JL. A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood. Proc Natl Acad Sci USA. 1999; 96: 11041-8
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11041-11048
    • Brown, M.S.1    Goldstein, J.L.2
  • 21
    • 0032479439 scopus 로고    scopus 로고
    • Topology of SREBP cleavage-activating protein, a polytopic membrane protein with a sterol-sensing domain
    • Nohturfft A, Brown MS, Goldstein JL. Topology of SREBP cleavage-activating protein, a polytopic membrane protein with a sterol-sensing domain. J Biol Chem 1998; 273: 17243-50
    • (1998) J Biol Chem , vol.273 , pp. 17243-17250
    • Nohturfft, A.1    Brown, M.S.2    Goldstein, J.L.3
  • 22
    • 0032489460 scopus 로고    scopus 로고
    • Cleavage of sterol regulatory elementbinding proteins (SREBPs) at site-1 requires interaction with SREBP cleavageactivating protein: Evidence from in vivo competition studies
    • Sakai J, Nohturfft A, Goldstein JL, et al. Cleavage of sterol regulatory elementbinding proteins (SREBPs) at site-1 requires interaction with SREBP cleavageactivating protein: evidence from in vivo competition studies. J Biol Chem 1998; 273: 5785-93
    • (1998) J Biol Chem , vol.273 , pp. 5785-5793
    • Sakai, J.1    Nohturfft, A.2    Goldstein, J.L.3
  • 23
    • 0036671360 scopus 로고    scopus 로고
    • Cholesterol addition to ER membranes alters conformation of SCAP, the SREBP escort protein that regulates cholesterol metabolism
    • Brown AJ, Sun L, Feramisco JD, et al. Cholesterol addition to ER membranes alters conformation of SCAP, the SREBP escort protein that regulates cholesterol metabolism. Mol Cell 2002; 10: 237-45
    • (2002) Mol Cell , vol.10 , pp. 237-245
    • Brown, A.J.1    Sun, L.2    Feramisco, J.D.3
  • 24
    • 0037162719 scopus 로고    scopus 로고
    • Crucial step in cholesterol homeostasis: Sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER
    • Yang T, Espenshade PJ, Wright ME, et al. Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER. Cell 2002; 110: 489-500
    • (2002) Cell , vol.110 , pp. 489-500
    • Yang, T.1    Espenshade, P.J.2    Wright, M.E.3
  • 25
    • 0036792050 scopus 로고    scopus 로고
    • Insig-2, a second endoplasmic reticulum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins
    • Yabe D, Brown MS, Goldstein JL. Insig-2, a second endoplasmic reticulum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins. Proc Natl Acad Sci USA 2002; 99: 12753-8
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12753-12758
    • Yabe, D.1    Brown, M.S.2    Goldstein, J.L.3
  • 26
    • 0033529545 scopus 로고    scopus 로고
    • Secreted site-1 protease cleaves peptides corresponding to luminal loop of sterol regulatory element-binding proteins
    • Cheng D, Espenshade PJ, Slaughter CA, et al. Secreted site-1 protease cleaves peptides corresponding to luminal loop of sterol regulatory element-binding proteins. J Biol Chem 1999; 274: 22805-12
    • (1999) J Biol Chem , vol.274 , pp. 22805-22812
    • Cheng, D.1    Espenshade, P.J.2    Slaughter, C.A.3
  • 27
    • 0032185770 scopus 로고    scopus 로고
    • Molecular identification of the sterolregulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells
    • Sakai J, Rawson RB, Espenshade PJ, et al. Molecular identification of the sterolregulated luminal protease that cleaves SREBPs and controls lipid composition of animal cells. Mol Cell 1998; 2: 505-14
    • (1998) Mol Cell , vol.2 , pp. 505-514
    • Sakai, J.1    Rawson, R.B.2    Espenshade, P.J.3
  • 28
    • 0033613126 scopus 로고    scopus 로고
    • Sterols regulate cycling of SREBP cleavage-activating protein (SCAP) between endoplasmic reticulum and Golgi
    • Nohturfft A, DeBose-Boyd RA, Scheek S, et al. Sterols regulate cycling of SREBP cleavage-activating protein (SCAP) between endoplasmic reticulum and Golgi. Proc Natl Acad Sci USA 1999; 96: 11235-40
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 11235-11240
    • Nohturfft, A.1    DeBose-Boyd, R.A.2    Scheek, S.3
  • 29
    • 0030911517 scopus 로고    scopus 로고
    • Cleavage site for sterol-regulated protease localized to a leu-Ser bond in the lumenal loop of sterol regulatory element-binding protein-2
    • Duncan EA, Brown MS, Goldstein JL, et al. Cleavage site for sterol-regulated protease localized to a leu-Ser bond in the lumenal loop of sterol regulatory element-binding protein-2. J Biol Chem 1997; 272: 12778-85
    • (1997) J Biol Chem , vol.272 , pp. 12778-12785
    • Duncan, E.A.1    Brown, M.S.2    Goldstein, J.L.3
  • 30
    • 0033529560 scopus 로고    scopus 로고
    • Autocatalytic processing of site-1 protease removes propeptide and permits cleavage of sterol regulatory elementbinding proteins
    • Espenshade PJ, Cheng D, Goldstein JL, et al. Autocatalytic processing of site-1 protease removes propeptide and permits cleavage of sterol regulatory elementbinding proteins. J Biol Chem 1999; 274: 22795-804
    • (1999) J Biol Chem , vol.274 , pp. 22795-22804
    • Espenshade, P.J.1    Cheng, D.2    Goldstein, J.L.3
  • 31
    • 0030604717 scopus 로고    scopus 로고
    • Sterol-regulated release of SREBP-2 from cell membranes requires two sequential cleavages, one within a transmembrane segment
    • Sakai J, Duncan EA, Rawson RB, et al. Sterol-regulated release of SREBP-2 from cell membranes requires two sequential cleavages, one within a transmembrane segment. Cell 1996; 85: 1037-46
    • (1996) Cell , vol.85 , pp. 1037-1046
    • Sakai, J.1    Duncan, E.A.2    Rawson, R.B.3
  • 32
    • 0030602866 scopus 로고    scopus 로고
    • The peroxisome proliferator activated receptors (PPARS) and their effects on lipid metabolism and adipocyte differentiation
    • Schoonjans K, Staels B, Auwerx J. The peroxisome proliferator activated receptors (PPARS) and their effects on lipid metabolism and adipocyte differentiation. Biochim Biophys Acta 1996; 1302: 93-109
    • (1996) Biochim Biophys Acta , vol.1302 , pp. 93-109
    • Schoonjans, K.1    Staels, B.2    Auwerx, J.3
  • 33
    • 0029737127 scopus 로고    scopus 로고
    • Pharmacodynamic activity of lipoprotein lipase and hepatic lipase, and pharmacokinetic parameters measured in normolipidaemic subjects receiving ciprofibrate (100 or 200 mg/day) or micronised fenofibrate (200 mg/day) therapy for 23 days
    • Desager JP, Horsmans Y, Vandenplas C, et al. Pharmacodynamic activity of lipoprotein lipase and hepatic lipase, and pharmacokinetic parameters measured in normolipidaemic subjects receiving ciprofibrate (100 or 200 mg/day) or micronised fenofibrate (200 mg/day) therapy for 23 days. Atherosclerosis 1996; 124: S65-73
    • (1996) Atherosclerosis , vol.124
    • Desager, J.P.1    Horsmans, Y.2    Vandenplas, C.3
  • 34
    • 0020533327 scopus 로고
    • Effects of clofibrate, bezafibrate fenofibrate and probucol on plasma lipolytic enzymes in normolipaemic subjects
    • Heller F, Harvengt C. Effects of clofibrate, bezafibrate fenofibrate and probucol on plasma lipolytic enzymes in normolipaemic subjects. Eur J Clin Pharmacol 1983; 25: 57-63
    • (1983) Eur J Clin Pharmacol , vol.25 , pp. 57-63
    • Heller, F.1    Harvengt, C.2
  • 35
    • 0029610832 scopus 로고
    • Hypolipidemic activity of select fibrates correlates to changes in hepatic apolipoprotein C-III expression: A potential physiologic basis for their mode of action
    • Haubenwallner S, Essenburg AD, Barnett BC, et al. Hypolipidemic activity of select fibrates correlates to changes in hepatic apolipoprotein C-III expression: a potential physiologic basis for their mode of action. J Lipid Res 1995; 36: 2541-51
    • (1995) J Lipid Res , vol.36 , pp. 2541-2551
    • Haubenwallner, S.1    Essenburg, A.D.2    Barnett, B.C.3
  • 36
    • 0026631526 scopus 로고
    • A multicenter comparison of the effects of simvastatin and fenofibrate therapy in severe primary hypercholesterolemia, with particular emphasis on lipoproteins defined by their apolipoprotein composition
    • Bard JM, Parra HJ, Camare R, et al. A multicenter comparison of the effects of simvastatin and fenofibrate therapy in severe primary hypercholesterolemia, with particular emphasis on lipoproteins defined by their apolipoprotein composition. Metabolism 1992; 41: 498-503
    • (1992) Metabolism , vol.41 , pp. 498-503
    • Bard, J.M.1    Parra, H.J.2    Camare, R.3
  • 37
    • 0025697301 scopus 로고
    • Efficacy of ciprofibrate in primary type II and IV hyperlipidemia: The Italian multicenter study
    • Cattin L, Da Col PG, Feruglio FS, et al. Efficacy of ciprofibrate in primary type II and IV hyperlipidemia: the Italian multicenter study. Clin Ther 1990; 12: 482-8
    • (1990) Clin Ther , vol.12 , pp. 482-488
    • Cattin, L.1    Da Col, P.G.2    Feruglio, F.S.3
  • 38
    • 0021868786 scopus 로고
    • Effects of fenofibrate on high and low density lipoprotein metabolism in heterozygous familial hypercholesterolemia
    • Malmendier CL, Delcroix C. Effects of fenofibrate on high and low density lipoprotein metabolism in heterozygous familial hypercholesterolemia. Atherosclerosis 1985; 55: 161-9
    • (1985) Atherosclerosis , vol.55 , pp. 161-169
    • Malmendier, C.L.1    Delcroix, C.2
  • 39
    • 0029984528 scopus 로고    scopus 로고
    • Multicenter comparison of micronized fenofibrate and simvastatin in patients with primary type IIA or IIB hyperlipoproteinemia
    • Steinmetz A, Schwartz T, Hehnke U, et al. Multicenter comparison of micronized fenofibrate and simvastatin in patients with primary type IIA or IIB hyperlipoproteinemia. J Cardiovasc Pharmacol 1996; 27: 563-70
    • (1996) J Cardiovasc Pharmacol , vol.27 , pp. 563-570
    • Steinmetz, A.1    Schwartz, T.2    Hehnke, U.3
  • 40
    • 8944252340 scopus 로고    scopus 로고
    • Opposite regulation of human versus mouse apolipoprotein A-I by fibrates in human apolipoprotein A-1 transgenic mice
    • Berthou L, Duverger N, Emmanuel F, et al. Opposite regulation of human versus mouse apolipoprotein A-I by fibrates in human apolipoprotein A-1 transgenic mice. J Clin Invest 1996; 97: 2408-16
    • (1996) J Clin Invest , vol.97 , pp. 2408-2416
    • Berthou, L.1    Duverger, N.2    Emmanuel, F.3
  • 41
    • 0029119082 scopus 로고
    • Fibrates increase human apolipoprotein A-II expression through activation of the peroxisome proliferator-activated receptor
    • Vu-Dac N, Schoonjans K, Kosykh V, et al. Fibrates increase human apolipoprotein A-II expression through activation of the peroxisome proliferator-activated receptor. J Clin Invest 1995; 96: 741-50
    • (1995) J Clin Invest , vol.96 , pp. 741-750
    • Vu-Dac, N.1    Schoonjans, K.2    Kosykh, V.3
  • 42
    • 0028036723 scopus 로고
    • Negative regulation of the human apolipoprotein A-I promoter by fibrates can be attenuated by the interaction of the peroxisome proliferator-activated receptor with its response element
    • Vu-Dac N, Schoonjans K, Laine B, et al. Negative regulation of the human apolipoprotein A-I promoter by fibrates can be attenuated by the interaction of the peroxisome proliferator-activated receptor with its response element. J Biol Chem 1994; 269: 31012-8
    • (1994) J Biol Chem , vol.269 , pp. 31012-31018
    • Vu-Dac, N.1    Schoonjans, K.2    Laine, B.3
  • 43
    • 0030658022 scopus 로고    scopus 로고
    • Coordinate regulation of the expression of the fatty acid transport protein and acyl-CoA synthetase genes by PPARalpha and PPARgamma activators
    • Martin G, Schoonjans K, Lefebvre AM, et al. Coordinate regulation of the expression of the fatty acid transport protein and acyl-CoA synthetase genes by PPARalpha and PPARgamma activators. J Biol Chem 1997; 272: 28210-7
    • (1997) J Biol Chem , vol.272 , pp. 28210-28217
    • Martin, G.1    Schoonjans, K.2    Lefebvre, A.M.3
  • 44
    • 0032508696 scopus 로고    scopus 로고
    • Fatty acids activate transcription of the muscle carnitine palmitoyltransferase I gene in cardiac myocytes via the peroxisome proliferator-activated receptor alpha
    • Brandt JM, Djouadi F, Kelly DP. Fatty acids activate transcription of the muscle carnitine palmitoyltransferase I gene in cardiac myocytes via the peroxisome proliferator-activated receptor alpha. J Biol Chem 1998; 273: 23786-92
    • (1998) J Biol Chem , vol.273 , pp. 23786-23792
    • Brandt, J.M.1    Djouadi, F.2    Kelly, D.P.3
  • 45
    • 0032502704 scopus 로고    scopus 로고
    • Control of human muscle-type carnitine palmitoyltransferase I gene transcription by peroxisome proliferator-activated receptor
    • Mascaro C, Acosta E, Ortiz JA, et al. Control of human muscle-type carnitine palmitoyltransferase I gene transcription by peroxisome proliferator-activated receptor. J Biol Chem 1998; 273: 8560-3
    • (1998) J Biol Chem , vol.273 , pp. 8560-8563
    • Mascaro, C.1    Acosta, E.2    Ortiz, J.A.3
  • 46
    • 0029791412 scopus 로고    scopus 로고
    • PPARalpha and PPARgamma activators direct a distinct tissue-specific transcriptional response via a PPRE in the lipoprotein lipase gene
    • Schoonjans K, Peinado-Onsurbe J, Lefebvre AM, et al. PPARalpha and PPARgamma activators direct a distinct tissue-specific transcriptional response via a PPRE in the lipoprotein lipase gene. EMBO J 1996; 15: 5336-48
    • (1996) EMBO J , vol.15 , pp. 5336-5348
    • Schoonjans, K.1    Peinado-Onsurbe, J.2    Lefebvre, A.M.3
  • 47
    • 0028998129 scopus 로고
    • Mode of action of peroxisome proliferators as hypolipidemic drugs: Suppression of apolipoprotein C-III
    • Hertz R, Bishara-Shieban J, Bar-Tana J. Mode of action of peroxisome proliferators as hypolipidemic drugs: suppression of apolipoprotein C-III. J Biol Chem 1995; 270: 13470-5
    • (1995) J Biol Chem , vol.270 , pp. 13470-13475
    • Hertz, R.1    Bishara-Shieban, J.2    Bar-Tana, J.3
  • 48
    • 0028817459 scopus 로고
    • Fibrates downregulate apolipoprotein C-III expression independent of induction of peroxisomal acyl coenzyme A oxidase: A potential mechanism for the hypolipidemic action of fibrates
    • Staels B, Vu-Dac N, Kosykh VA, et al. Fibrates downregulate apolipoprotein C-III expression independent of induction of peroxisomal acyl coenzyme A oxidase: a potential mechanism for the hypolipidemic action of fibrates. J Clin Invest 1995; 95: 705-12
    • (1995) J Clin Invest , vol.95 , pp. 705-712
    • Staels, B.1    Vu-Dac, N.2    Kosykh, V.A.3
  • 49
    • 0029131206 scopus 로고
    • Regulation of rat liver apolipoprotein A-1, apolipoprotein A-11 and acyl-coenzyme A oxidase gene expression by fibrates and dietary fatty acids
    • Berthou L, Saladin R, Yaqoob P, et al. Regulation of rat liver apolipoprotein A-1, apolipoprotein A-11 and acyl-coenzyme A oxidase gene expression by fibrates and dietary fatty acids. Eur J Biochem 1995; 232: 179-87
    • (1995) Eur J Biochem , vol.232 , pp. 179-187
    • Berthou, L.1    Saladin, R.2    Yaqoob, P.3
  • 50
    • 0035138625 scopus 로고    scopus 로고
    • PPAR-alpha and PPAR-gamma activators induce cholesterol removal from human macrophage foam cells through stimulation of the ABCAI pathway
    • Chinetti G, Lestavel S, Becher V, et al. PPAR-alpha and PPAR-gamma activators induce cholesterol removal from human macrophage foam cells through stimulation of the ABCAI pathway. Nat Med 2001; 7: 53-8
    • (2001) Nat Med , vol.7 , pp. 53-58
    • Chinetti, G.1    Lestavel, S.2    Becher, V.3
  • 51
    • 0034705071 scopus 로고    scopus 로고
    • CLA-1/SR-B1 is expressed in atherosclerotic lesion macrophages and regulated by activators of peroxisome proliferator-activated receptors
    • Chinetti G, Gbaguidi FG, Griglio S, et al. CLA-1/SR-B1 is expressed in atherosclerotic lesion macrophages and regulated by activators of peroxisome proliferator-activated receptors. Circulation 2000; 101: 2411-7
    • (2000) Circulation , vol.101 , pp. 2411-2417
    • Chinetti, G.1    Gbaguidi, F.G.2    Griglio, S.3
  • 52
    • 0032484123 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor alpha activation modulates cellular redox status, represses nuclear factor-kappaB signaling, and reduces inflammatory cytokine production in aging
    • Poynter ME, Daynes RA. Peroxisome proliferator-activated receptor alpha activation modulates cellular redox status, represses nuclear factor-kappaB signaling, and reduces inflammatory cytokine production in aging. J Biol Chem 1998; 273: 32833-41
    • (1998) J Biol Chem , vol.273 , pp. 32833-32841
    • Poynter, M.E.1    Daynes, R.A.2
  • 53
    • 0032565868 scopus 로고    scopus 로고
    • Activation of human aortic smooth-muscle cells is inhibited by PPARα but not by PPARγ activators
    • Staels B, Koenig W, Habib A, et al. Activation of human aortic smooth-muscle cells is inhibited by PPARα but not by PPARγ activators. Nature 1998; 393: 790-3
    • (1998) Nature , vol.393 , pp. 790-793
    • Staels, B.1    Koenig, W.2    Habib, A.3
  • 54
    • 0036255486 scopus 로고    scopus 로고
    • DNA binding-independent induction of IkappaBalpha gene transcription by PPARalpha
    • Delerive P, De Bosscher K, Vanden Berghe W, et al. DNA binding-independent induction of IkappaBalpha gene transcription by PPARalpha. Mol Endocrinol 2002; 16: 1029-39
    • (2002) Mol Endocrinol , vol.16 , pp. 1029-1039
    • Delerive, P.1    De Bosscher, K.2    Vanden Berghe, W.3
  • 55
    • 0033527569 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor alpha negatively regulates the vascular inflammatory gene response by negative cross-talk with transcription factors NF-kappaB and AP-1
    • Delerive P, De Bosscher K, Besnard S, et al. Peroxisome proliferator-activated receptor alpha negatively regulates the vascular inflammatory gene response by negative cross-talk with transcription factors NF-kappaB and AP-1. J Biol Chem 1999; 274: 32048-54
    • (1999) J Biol Chem , vol.274 , pp. 32048-32054
    • Delerive, P.1    De Bosscher, K.2    Besnard, S.3
  • 56
    • 0005419053 scopus 로고    scopus 로고
    • PPAR activators inhibit thrombininduced endothelin-I production in human vascular endothelial cells
    • Delerive P, Martin-Nizard F, Chinetti G, et al. PPAR activators inhibit thrombininduced endothelin-I production in human vascular endothelial cells. Circulation 1998; 98. 17: 1-406-2137
    • (1998) Circulation , vol.98 , Issue.17
    • Delerive, P.1    Martin-Nizard, F.2    Chinetti, G.3
  • 57
    • 0035895313 scopus 로고    scopus 로고
    • PPARalpha agonists inhibit tissue factor expression in human monocytes and macrophages
    • Neve BP, Corseaux D, Chinetti G, et al. PPARalpha agonists inhibit tissue factor expression in human monocytes and macrophages. Circulation 2001; 103: 207-12
    • (2001) Circulation , vol.103 , pp. 207-212
    • Neve, B.P.1    Corseaux, D.2    Chinetti, G.3
  • 58
    • 0035823551 scopus 로고    scopus 로고
    • Negative regulation of human fibrinogen gene expression by peroxisome proliferator-activated receptor alpha agonists via inhibition of CCAAT box/enhancer-binding protein beta
    • Gervois P, Vu-Dac N, Kleemann R, et al. Negative regulation of human fibrinogen gene expression by peroxisome proliferator-activated receptor alpha agonists via inhibition of CCAAT box/enhancer-binding protein beta. J Biol Chem 2001; 276: 33471-7
    • (2001) J Biol Chem , vol.276 , pp. 33471-33477
    • Gervois, P.1    Vu-Dac, N.2    Kleemann, R.3
  • 59
    • 0034994075 scopus 로고    scopus 로고
    • Statin-induced inhibition of the Rho-signaling pathway activates PPARalpha and induces HDL apoA-I
    • Martin G, Duez H, Blanquart C, et al. Statin-induced inhibition of the Rho-signaling pathway activates PPARalpha and induces HDL apoA-I. J Clin Invest 2001; 107: 1423-32
    • (2001) J Clin Invest , vol.107 , pp. 1423-1432
    • Martin, G.1    Duez, H.2    Blanquart, C.3


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