메뉴 건너뛰기




Volumn 41, Issue 7, 2000, Pages 1136-1144

Effect of ER-27856, a novel squalene synthase inhibitor, on plasma cholesterol in rhesus monkeys: Comparison with 3-hydroxy-3-methylglutaryl-CoA reductase inhibitors

Author keywords

Cholesterol biosynthesis; Cholesterol lowering; Enzyme inhibition; ER 97856; HMG CoA reductase; Rhesus monkeys; Squalene synthase

Indexed keywords

5 [N [2 BUTENYL 3 (2 METHOXYPHENYL)] N METHYLAMINO] 1,1 PENTHYLIDINEBIS(PHOSPHONIC ACID)TRISODIUM; ATORVASTATIN; CHOLESTEROL; DEXAMETHASONE; ER 27856; ER 28448; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; INSULIN; PRAVASTATIN; SIMVASTATIN; SQUALENE SYNTHASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 0033942443     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (65)

References (49)
  • 1
    • 84944359172 scopus 로고
    • Lipid research clinics program
    • Lipid Research Clinics. 1984. Lipid Research Clinics Program. J. Am. Med. Assoc. 252: 2545-2548.
    • (1984) J. Am. Med. Assoc. , vol.252 , pp. 2545-2548
  • 2
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein, J. L., and M. S. Brown. 1990. Regulation of the mevalonate pathway. Nature. 343: 425-430.
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 3
    • 0031692691 scopus 로고    scopus 로고
    • Treating patients with documented atherosclerosis to National Cholesterol Education Program-recommended low-density-lipoprotein cholesterol goals with atorvastatin, fluvastatin, lovastatin and simvastatin
    • Brown, A. S., R. G. Bakker-Arkema, L. Yellen, R. W. Henley, Jr., R. Guthrie, C. F Campbell, M. Koren, W. Woo, R. McLain, and D. M. Black. 1998. Treating patients with documented atherosclerosis to National Cholesterol Education Program-recommended low-density-lipoprotein cholesterol goals with atorvastatin, fluvastatin, lovastatin and simvastatin. J. Am. Coll. Cardiol. 32: 665-672.
    • (1998) J. Am. Coll. Cardiol. , vol.32 , pp. 665-672
    • Brown, A.S.1    Bakker-Arkema, R.G.2    Yellen, L.3    Henley R.W., Jr.4    Guthrie, R.5    Campbell, C.F.6    Koren, M.7    Woo, W.8    McLain, R.9    Black, D.M.10
  • 5
    • 0028883828 scopus 로고
    • Prevention of coronary heart disease with pravastatin in men with hypercholesterolemia
    • West of Scotland Coronary Prevention Study Group
    • Shepherd, J., S. M. Cobbe, I. Ford, C. G. Isles, A. R. Lorimer, P. W. MacFarlane, J. H. McKillop, and C. J. Packard. 1995. Prevention of coronary heart disease with pravastatin in men with hypercholesterolemia. West of Scotland Coronary Prevention Study Group. N. Engl. J. Med. 333: 1301-1307.
    • (1995) N. Engl. J. Med. , vol.333 , pp. 1301-1307
    • Shepherd, J.1    Cobbe, S.M.2    Ford, I.3    Isles, C.G.4    Lorimer, A.R.5    MacFarlane, P.W.6    McKillop, J.H.7    Packard, C.J.8
  • 6
    • 0027987849 scopus 로고
    • Randotnised trial of cholesterol-lowering in 4444 patients with coronary heart disease: The Scandinavian simvastatin survival study (4S)
    • Scandinavian Simvastatin Survival Study Group. 1994. Randotnised trial of cholesterol-lowering in 4444 patients with coronary heart disease: the Scandinavian Simvastatin Survival Study (4S). Lancet. 344: 1383-1389.
    • (1994) Lancet , vol.344 , pp. 1383-1389
  • 7
    • 0023217436 scopus 로고
    • New developments in lipid-lowering therapy: The role of inhibitors of hydroxymethylglutaryl-coenzyme A reductase
    • Tobert, J. A. 1987. New developments in lipid-lowering therapy: the role of inhibitors of hydroxymethylglutaryl-coenzyme A reductase. Circulation. 76: 534-538.
    • (1987) Circulation , vol.76 , pp. 534-538
    • Tobert, J.A.1
  • 8
    • 0029101804 scopus 로고
    • Comparative evaluation of the safety and efficacy of HMG-CoA reductase inhibitor monotherapy in the treatment of primary hypercholesterolemia
    • Hsu, I., S. A. Spinler, and N. E. Johnson. 1995. Comparative evaluation of the safety and efficacy of HMG-CoA reductase inhibitor monotherapy in the treatment of primary hypercholesterolemia. Ann. Pharmacother. 29: 743-759.
    • (1995) Ann. Pharmacother. , vol.29 , pp. 743-759
    • Hsu, I.1    Spinler, S.A.2    Johnson, N.E.3
  • 10
    • 0029118101 scopus 로고
    • Effects of 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors on mitochondrial respiration in ischaemic dog hearts
    • Satoh, K., A. Yamato, T. Nakai, K. Hoshi, and K. Ichihara. 1995. Effects of 3-hydroxy-3-methylglutaryl coenzyme A reductase inhibitors on mitochondrial respiration in ischaemic dog hearts. Br. J. Pharmacol. 116: 1894-1898.
    • (1995) Br. J. Pharmacol. , vol.116 , pp. 1894-1898
    • Satoh, K.1    Yamato, A.2    Nakai, T.3    Hoshi, K.4    Ichihara, K.5
  • 11
    • 0027369405 scopus 로고
    • Influences of pravastatin and simvastatin, HMG-CoA reductase inhibitors, on myocardial stunning in dogs
    • Ichihara, K., K. Satoh, and V. Abiko. 1993. Influences of pravastatin and simvastatin, HMG-CoA reductase inhibitors, on myocardial stunning in dogs. J. Cardiovasc. Pharmacol. 22: 852-856.
    • (1993) J. Cardiovasc. Pharmacol. , vol.22 , pp. 852-856
    • Ichihara, K.1    Satoh, K.2    Abiko, V.3
  • 13
    • 0030615072 scopus 로고    scopus 로고
    • Ro 48-8.071, a new 2,3-oxidosqualene:Lanosterol cyclase inhibitor lowering plasma cholesterol in hamsters, squirrel monkeys, and minipigs: Comparison to simvastatin
    • Morand, O. H., J. D. Aebi, H. Dehmlow, Y. H. Ji, N. Gains, H. Lengsfeld, and J. Himber. 1997. Ro 48-8.071, a new 2,3-oxidosqualene:lanosterol cyclase inhibitor lowering plasma cholesterol in hamsters, squirrel monkeys, and minipigs: comparison to simvastatin. J. Lipid Res. 38: 373-390.
    • (1997) J. Lipid Res. , vol.38 , pp. 373-390
    • Morand, O.H.1    Aebi, J.D.2    Dehmlow, H.3    Ji, Y.H.4    Gains, N.5    Lengsfeld, H.6    Himber, J.7
  • 24
    • 0030943097 scopus 로고    scopus 로고
    • Biological activities of novel zaragozic acids, the potent inhibitors of squalene synthase, produced by the fungus, Mollisia sp. SANK 10294
    • Tanimoto, T., K. Hamano, K Onodera, T. Osoya, M. Kakusaka, T. Hirayama, Y. Shimada, T. Koga, and Y. Tsujita. 1997. Biological activities of novel zaragozic acids, the potent inhibitors of squalene synthase, produced by the fungus, Mollisia sp. SANK 10294. J. Antibiol. (Tokyo). 50: 390-394.
    • (1997) J. Antibiol. (Tokyo) , vol.50 , pp. 390-394
    • Tanimoto, T.1    Hamano, K.2    Onodera, K.3    Osoya, T.4    Kakusaka, M.5    Hirayama, T.6    Shimada, Y.7    Koga, T.8    Tsujita, Y.9
  • 25
    • 0021894240 scopus 로고
    • Squalene synthetase
    • Agnew, W. S. 1985. Squalene synthetase. Methods Enzimol. 110: 359-373.
    • (1985) Methods Enzimol. , vol.110 , pp. 359-373
    • Agnew, W.S.1
  • 26
    • 0026559054 scopus 로고
    • The synthesis of (4R-cis)-1,1-dimethylethyl-6-cyanomethyl-2,2-dimethyl-1,3-dioxane-4-acetate, a key intermediate for the preparation of CI-981, a highly potent, tissue selective inhibitor of HMG-CoA reductase
    • Brower, P. L., D. E. Butler, C. F. Deering, T. V. Le, A. Millar, T. N. Nanninga, and B. D. Roth. 1992. The synthesis of (4R-cis)-1,1-dimethylethyl-6-cyanomethyl-2,2-dimethyl-1,3-dioxane-4-acetate, a key intermediate for the preparation of CI-981, a highly potent, tissue selective inhibitor of HMG-CoA reductase. Tetrahedron Lett. 33: 2279-2282.
    • (1992) Tetrahedron Lett. , vol.33 , pp. 2279-2282
    • Brower, P.L.1    Butler, D.E.2    Deering, C.F.3    Le, T.V.4    Millar, A.5    Nanninga, T.N.6    Roth, B.D.7
  • 28
    • 0022516611 scopus 로고
    • Characteristics of rat liver microsomal 3-hydroxy-3-methylglutaryl-coenzyme A reductase
    • Ness, G. C., C. E. Sample, M. Smith, L. C. Pendleton, and D. C. Eichler. 1986. Characteristics of rat liver microsomal 3-hydroxy-3-methylglutaryl-coenzyme A reductase. Biochem. J. 233: 167-172.
    • (1986) Biochem. J. , vol.233 , pp. 167-172
    • Ness, G.C.1    Sample, C.E.2    Smith, M.3    Pendleton, L.C.4    Eichler, D.C.5
  • 29
    • 0018761890 scopus 로고
    • Active and inactive forms of 3-hydroxy-3-methylglutaryl coenzyme A reductase in the liver of the rat. Comparison with the rate of cholesterol synthesis in different physiological states
    • Brown, M.S., J. L. Goldstein, and J. M. Dietschy. 1979. Active and inactive forms of 3-hydroxy-3-methylglutaryl coenzyme A reductase in the liver of the rat. Comparison with the rate of cholesterol synthesis in different physiological states. J. Biol. Chem. 254: 5144-5149.
    • (1979) J. Biol. Chem. , vol.254 , pp. 5144-5149
    • Brown, M.S.1    Goldstein, J.L.2    Dietschy, J.M.3
  • 33
    • 0027453262 scopus 로고
    • Rapid fluorometric assay of LDL-R activity by DiI-labeled LDL
    • Stephan, Z. F., and E. C. Yurachek. 1993. Rapid fluorometric assay of LDL-R activity by Dil-labeled LDL. J. Lipid Res. 34: 325-330.
    • (1993) J. Lipid Res. , vol.34 , pp. 325-330
    • Stephan, Z.F.1    Yurachek, E.C.2
  • 35
    • 0025778632 scopus 로고
    • Novel chemical approaches in prodrug design
    • Bundgaard, H. 1991. Novel chemical approaches in prodrug design. Drugs Future. 16: 443-458.
    • (1991) Drugs Future , vol.16 , pp. 443-458
    • Bundgaard, H.1
  • 36
    • 0017093514 scopus 로고
    • Comparison of the serum low density lipoprotein and of its apoprotein in the pig, rhesus monkey and baboon with that in man
    • Chapman, M. J., and S. Goldstein. 1976. Comparison of the serum low density lipoprotein and of its apoprotein in the pig, rhesus monkey and baboon with that in man. Atherosclerosis. 25: 267-291.
    • (1976) Atherosclerosis , vol.25 , pp. 267-291
    • Chapman, M.J.1    Goldstein, S.2
  • 37
    • 0033613147 scopus 로고    scopus 로고
    • A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood
    • Brown, M. S., and J. L. Goldstein. 1999. A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood. Proc. Natl. Acad. Sci. USA. 96: 11041-11048.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11041-11048
    • Brown, M.S.1    Goldstein, J.L.2
  • 38
    • 0032032592 scopus 로고    scopus 로고
    • Comparative dose efficacy study of atorvastatin versus simvastatin, pravastatin, lovastatin, and fluvastatin in patients with hypercholesterolemia
    • Jones, P., S. Kafonek, I. Laurora, and D. Hunninghake. 1998. Comparative dose efficacy study of atorvastatin versus simvastatin, pravastatin, lovastatin, and fluvastatin in patients with hypercholesterolemia. Am. J. Cardiol. 81: 582-587.
    • (1998) Am. J. Cardiol. , vol.81 , pp. 582-587
    • Jones, P.1    Kafonek, S.2    Laurora, I.3    Hunninghake, D.4
  • 39
    • 0020619724 scopus 로고
    • Mevalonolactone inhibits the rate of synthesis and enhances the rate of degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in rat hepatocytes
    • Edwards, P. A., S. F. Lan, R. D. Tanaka, and A. M. Fogelman. 1983. Mevalonolactone inhibits the rate of synthesis and enhances the rate of degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase in rat hepatocytes. J. Biol. Chem. 258: 7272-7275.
    • (1983) J. Biol. Chem. , vol.258 , pp. 7272-7275
    • Edwards, P.A.1    Lan, S.F.2    Tanaka, R.D.3    Fogelman, A.M.4
  • 40
    • 0023902411 scopus 로고
    • Multivalent control of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Mevalonate-derived product inhibits translation of mRNA and accelerates degradation of enzyme
    • Nakanishi, M., J. L. Goldstein, and M. S. Brown. 1988. Multivalent control of 3-hydroxy-3-methylglutaryl coenzyme A reductase. Mevalonate-derived product inhibits translation of mRNA and accelerates degradation of enzyme. J. Biol. Chem. 263: 8929-8937.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8929-8937
    • Nakanishi, M.1    Goldstein, J.L.2    Brown, M.S.3
  • 41
    • 0026461126 scopus 로고
    • Distinct sterol and non-sterol signals for the regulated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Roitelman, J., and R. D. Simoni. 1992. Distinct sterol and non-sterol signals for the regulated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase. J. Biol. Chem. 267: 25264-25273.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25264-25273
    • Roitelman, J.1    Simoni, R.D.2
  • 42
    • 0028285272 scopus 로고
    • Non-sterol compounds that regulate cholesterogenesis. Analogues of FPP reduce 3-hydroxy-3-methylglutaryl-coenzyme A reductase levels
    • Bradfute, D. L., and R. D. Simoni. 1994. Non-sterol compounds that regulate cholesterogenesis. Analogues of FPP reduce 3-hydroxy-3-methylglutaryl-coenzyme A reductase levels. J. Biol. Chem. 269: 6645-6650.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6645-6650
    • Bradfute, D.L.1    Simoni, R.D.2
  • 43
    • 0028307290 scopus 로고
    • Identification of farnesol as the non-sterol derivative of mevalonic acid required for the accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
    • Correll, C. C., L. Ng, and P. A. Edwards. 1994. Identification of farnesol as the non-sterol derivative of mevalonic acid required for the accelerated degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J. Biol. Chem. 269: 17390-17393.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17390-17393
    • Correll, C.C.1    Ng, L.2    Edwards, P.A.3
  • 44
    • 0029969302 scopus 로고    scopus 로고
    • Regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase degradation by the non-sterol mevalonate metabolite farnesol in vivo
    • Meigs, T. E., D. S. Roseman, and R. D. Simoni. 1996. Regulation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase degradation by the non-sterol mevalonate metabolite farnesol in vivo. J. Biol. Chem. 271: 7916-7922.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7916-7922
    • Meigs, T.E.1    Roseman, D.S.2    Simoni, R.D.3
  • 45
    • 0028157541 scopus 로고
    • Mevalonic acid-dependent degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase in vivo and in vitro
    • Correll, C. C., and P. A. Edwards. 1994. Mevalonic acid-dependent degradation of 3-hydroxy-3-methylglutaryl-coenzyme A reductase in vivo and in vitro. J. Biol. Chem. 269: 633-638.
    • (1994) J. Biol. Chem. , vol.269 , pp. 633-638
    • Correll, C.C.1    Edwards, P.A.2
  • 46
    • 0031568243 scopus 로고    scopus 로고
    • Inhibition of squalene synthase but not squalene cyclase prevents mevalonate-mediated suppression of 3-hydroxy-3-methylglutaryl coenzyme A reductase synthesis at a posttranscriptional level
    • Peffley, D. M., and A. K. Gayen. 1997. Inhibition of squalene synthase but not squalene cyclase prevents mevalonate-mediated suppression of 3-hydroxy-3-methylglutaryl coenzyme A reductase synthesis at a posttranscriptional level. Arch. Biochem. Biophys. 337: 251-260.
    • (1997) Arch. Biochem. Biophys. , vol.337 , pp. 251-260
    • Peffley, D.M.1    Gayen, A.K.2
  • 47
    • 0031239831 scopus 로고    scopus 로고
    • Farnesol as a regulator of HMG-CoA reductase degradation: Characterization and role of farnesyl pyrophosphatase
    • Meigs, T. E., and R. D. Simoni. 1997. Farnesol as a regulator of HMG-CoA reductase degradation: characterization and role of farnesyl pyrophosphatase. Arch. Biochem. Biophys. 345: 1-9.
    • (1997) Arch. Biochem. Biophys. , vol.345 , pp. 1-9
    • Meigs, T.E.1    Simoni, A.R.D.2
  • 48
    • 0032895029 scopus 로고    scopus 로고
    • HMG-CoA reductase regulation: Use of structurally diverse first half-reaction squalene synthetase inhibitors to characterize the site of mevalonate-derived non-sterol regulator production in cultured IM-9 cells
    • Petras, S. F., S. Lindsey, and H. J. Harwood, Jr. 1999. HMG-CoA reductase regulation: use of structurally diverse first half-reaction squalene synthetase inhibitors to characterize the site of mevalonate-derived non-sterol regulator production in cultured IM-9 cells. J. Lipid Res. 40: 24-38.
    • (1999) J. Lipid Res. , vol.40 , pp. 24-38
    • Petras, S.F.1    Lindsey, S.2    Harwood H.J., Jr.3
  • 49
    • 0033615648 scopus 로고    scopus 로고
    • A highly conserved signal controls degradation of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase in eukaryotes
    • Gardner, R. G., and R. Y. Hampton. 1999. A highly conserved signal controls degradation of 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductase in eukaryotes. J. Biol. Chem. 274: 31671-31678.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31671-31678
    • Gardner, R.G.1    Hampton, R.Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.