메뉴 건너뛰기




Volumn 47, Issue 6, 2008, Pages 391-404

Sterol regulators of cholesterol homeostasis and beyond: The oxysterol hypothesis revisited and revised

Author keywords

24(S); 25 epoxycholesterol; 27 Hydroxycholesterol; Desmosterol; Kandutsch; Lanosterol; Niemann Pick type C disease; Oxysterols; Sulfation

Indexed keywords

CHOLESTEROL; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; OXYSTEROL; SONIC HEDGEHOG PROTEIN; STEROL; STEROL REGULATORY ELEMENT BINDING PROTEIN;

EID: 53149118574     PISSN: 01637827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plipres.2008.04.002     Document Type: Review
Times cited : (187)

References (144)
  • 1
    • 0034529050 scopus 로고    scopus 로고
    • How cells handle cholesterol
    • Simons K., and Ikonen E. How cells handle cholesterol. Science 290 (2000) 1721-1726
    • (2000) Science , vol.290 , pp. 1721-1726
    • Simons, K.1    Ikonen, E.2
  • 2
    • 0030941803 scopus 로고    scopus 로고
    • The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor
    • Brown M.S., and Goldstein J.L. The SREBP pathway: regulation of cholesterol metabolism by proteolysis of a membrane-bound transcription factor. Cell 89 (1997) 331-340
    • (1997) Cell , vol.89 , pp. 331-340
    • Brown, M.S.1    Goldstein, J.L.2
  • 3
    • 0018079091 scopus 로고
    • Biological activity of some oxygenated sterols
    • Kandutsch A.A., Chen H.W., and Heiniger H.J. Biological activity of some oxygenated sterols. Science 201 (1978) 498-501
    • (1978) Science , vol.201 , pp. 498-501
    • Kandutsch, A.A.1    Chen, H.W.2    Heiniger, H.J.3
  • 4
    • 33646864114 scopus 로고    scopus 로고
    • Membrane and protein interactions of oxysterols
    • Massey J.B. Membrane and protein interactions of oxysterols. Curr Opin Lipidol 17 (2006) 296-301
    • (2006) Curr Opin Lipidol , vol.17 , pp. 296-301
    • Massey, J.B.1
  • 5
    • 0004208435 scopus 로고
    • Reinhold Publishing Corporation, New York
    • Fieser L.F., and Fieser M. Steroids (1959), Reinhold Publishing Corporation, New York
    • (1959) Steroids
    • Fieser, L.F.1    Fieser, M.2
  • 6
    • 0013417965 scopus 로고
    • Examen des graisses d'homme, de mouton, de boeuf, de jaguar et d'oie
    • Chevreul M.E. Examen des graisses d'homme, de mouton, de boeuf, de jaguar et d'oie. Ann Chim Phys 2 (1816) 33
    • (1816) Ann Chim Phys , vol.2 , pp. 33
    • Chevreul, M.E.1
  • 8
    • 0032890337 scopus 로고    scopus 로고
    • Oxysterols and atherosclerosis
    • Brown A.J., and Jessup W. Oxysterols and atherosclerosis. Atherosclerosis 142 (1999) 1-28
    • (1999) Atherosclerosis , vol.142 , pp. 1-28
    • Brown, A.J.1    Jessup, W.2
  • 9
    • 37649021073 scopus 로고    scopus 로고
    • Oxysterols: novel biologic roles for the 21st century
    • Javitt N.B. Oxysterols: novel biologic roles for the 21st century. Steroids 73 (2008) 149-157
    • (2008) Steroids , vol.73 , pp. 149-157
    • Javitt, N.B.1
  • 10
    • 0342316532 scopus 로고    scopus 로고
    • Oxysterols: modulators of cholesterol metabolism and other processes
    • Schroepfer Jr. G.J. Oxysterols: modulators of cholesterol metabolism and other processes. Physiol Rev 80 (2000) 361-554
    • (2000) Physiol Rev , vol.80 , pp. 361-554
    • Schroepfer Jr., G.J.1
  • 11
    • 33846084357 scopus 로고    scopus 로고
    • Oxysterols in biological systems: sources, metabolism and pathophysiological relevance
    • van Reyk D.M., Brown A.J., Hult'en L.M., Dean R.T., and Jessup W. Oxysterols in biological systems: sources, metabolism and pathophysiological relevance. Redox Rep 11 (2006) 255-262
    • (2006) Redox Rep , vol.11 , pp. 255-262
    • van Reyk, D.M.1    Brown, A.J.2    Hult'en, L.M.3    Dean, R.T.4    Jessup, W.5
  • 12
    • 0035914368 scopus 로고    scopus 로고
    • Antiepileptic drugs increase plasma levels of 4β-hydroxycholesterol in humans: evidence for involvement of cytochrome p450 3A4
    • Bodin K., Bretillon L., Aden Y., Bertilsson L., Broome U., Einarsson C., et al. Antiepileptic drugs increase plasma levels of 4β-hydroxycholesterol in humans: evidence for involvement of cytochrome p450 3A4. J Biol Chem 276 (2001) 38685-38689
    • (2001) J Biol Chem , vol.276 , pp. 38685-38689
    • Bodin, K.1    Bretillon, L.2    Aden, Y.3    Bertilsson, L.4    Broome, U.5    Einarsson, C.6
  • 13
    • 33947706821 scopus 로고    scopus 로고
    • Rediscovery of cerebrosterol
    • Björkhem I. Rediscovery of cerebrosterol. Lipids 42 (2007) 5-15
    • (2007) Lipids , vol.42 , pp. 5-15
    • Björkhem, I.1
  • 14
    • 0036250159 scopus 로고    scopus 로고
    • 25R,26-Hydroxycholesterol revisited: synthesis, metabolism, and biologic roles
    • Javitt N.B. 25R,26-Hydroxycholesterol revisited: synthesis, metabolism, and biologic roles. J Lipid Res 43 (2002) 665-670
    • (2002) J Lipid Res , vol.43 , pp. 665-670
    • Javitt, N.B.1
  • 15
    • 0015918862 scopus 로고
    • Oxidation of 20α-hydroxycholesterol by adrenal cortex mitochondria
    • Wilson L.D., and Harding B.W. Oxidation of 20α-hydroxycholesterol by adrenal cortex mitochondria. J Biol Chem 248 (1973) 9-14
    • (1973) J Biol Chem , vol.248 , pp. 9-14
    • Wilson, L.D.1    Harding, B.W.2
  • 16
    • 0021328050 scopus 로고
    • The catalytic cycle of cytochrome P-450scc and intermediates in the conversion of cholesterol to pregnenolone
    • Hume R., Kelly R.W., Taylor P.L., and Boyd G.S. The catalytic cycle of cytochrome P-450scc and intermediates in the conversion of cholesterol to pregnenolone. Eur J Biochem 140 (1984) 583-591
    • (1984) Eur J Biochem , vol.140 , pp. 583-591
    • Hume, R.1    Kelly, R.W.2    Taylor, P.L.3    Boyd, G.S.4
  • 17
    • 0034672672 scopus 로고    scopus 로고
    • Oxysterol biosynthetic enzymes
    • Russell D.W. Oxysterol biosynthetic enzymes. Biochim Biophys Acta 1529 (2000) 126-135
    • (2000) Biochim Biophys Acta , vol.1529 , pp. 126-135
    • Russell, D.W.1
  • 18
    • 38349112601 scopus 로고    scopus 로고
    • Effectors of rapid homeostatic responses of endoplasmic reticulum cholesterol and HMG-CoA reductase
    • Lange Y., Ory D.S., Ye J., Lanier M.H., Hsu F.-F., and Steck T.L. Effectors of rapid homeostatic responses of endoplasmic reticulum cholesterol and HMG-CoA reductase. J Biol Chem 283 (2008) 1445-1455
    • (2008) J Biol Chem , vol.283 , pp. 1445-1455
    • Lange, Y.1    Ory, D.S.2    Ye, J.3    Lanier, M.H.4    Hsu, F.-F.5    Steck, T.L.6
  • 19
    • 30344442114 scopus 로고    scopus 로고
    • Physiologic interactions between macrophages and Leydig cells
    • Hutson J.C. Physiologic interactions between macrophages and Leydig cells. Exp Biol Med 231 (2006) 1-7
    • (2006) Exp Biol Med , vol.231 , pp. 1-7
    • Hutson, J.C.1
  • 20
    • 0343890977 scopus 로고
    • Synthesis and destruction of cholesterol in the organism
    • Schoenheimer R., and Breusch F. Synthesis and destruction of cholesterol in the organism. J Biol Chem 103 (1933) 439-448
    • (1933) J Biol Chem , vol.103 , pp. 439-448
    • Schoenheimer, R.1    Breusch, F.2
  • 21
    • 0001517301 scopus 로고
    • Cholesterol metabolism I. Effect of dietary cholesterol on the synthesis of cholesterol in dog tissue in vitro
    • Gould R.G., Taylor C.B., Hangerman J.S., Warner I., and Campbell D.J. Cholesterol metabolism I. Effect of dietary cholesterol on the synthesis of cholesterol in dog tissue in vitro. J Biol Chem 201 (1952) 519-528
    • (1952) J Biol Chem , vol.201 , pp. 519-528
    • Gould, R.G.1    Taylor, C.B.2    Hangerman, J.S.3    Warner, I.4    Campbell, D.J.5
  • 22
    • 33746064276 scopus 로고
    • Cholesterol synthesis by liver IV. Suppression by steroid administration.
    • Tomkins G.M., Sheppard H., and Chaikoff I.L. Cholesterol synthesis by liver IV. Suppression by steroid administration. J Biol Chem 203 (1953) 781-786
    • (1953) J Biol Chem , vol.203 , pp. 781-786
    • Tomkins, G.M.1    Sheppard, H.2    Chaikoff, I.L.3
  • 23
    • 0015714737 scopus 로고
    • Inhibition of sterol synthesis in cultured mouse cells by 7α-hydroxycholesterol, 7β-hydroxycholesterol, and 7-ketocholesterol
    • Kandutsch A.A., and Chen H.W. Inhibition of sterol synthesis in cultured mouse cells by 7α-hydroxycholesterol, 7β-hydroxycholesterol, and 7-ketocholesterol. J Biol Chem 248 (1973) 8408-8417
    • (1973) J Biol Chem , vol.248 , pp. 8408-8417
    • Kandutsch, A.A.1    Chen, H.W.2
  • 24
    • 0017103628 scopus 로고
    • The low-density lipoprotein pathway in human fibroblasts: relation between cell surface receptor binding and endocytosis of low-density lipoprotein
    • Brown M.S., Ho Y.K., and Goldstein J.L. The low-density lipoprotein pathway in human fibroblasts: relation between cell surface receptor binding and endocytosis of low-density lipoprotein. Ann NY Acad Sci 275 (1976) 244-257
    • (1976) Ann NY Acad Sci , vol.275 , pp. 244-257
    • Brown, M.S.1    Ho, Y.K.2    Goldstein, J.L.3
  • 25
    • 0017358485 scopus 로고
    • Consequences of blocked sterol synthesis in cultured cells DNA synthesis and membrane composition
    • Kandutsch A.A., and Chen H.W. Consequences of blocked sterol synthesis in cultured cells DNA synthesis and membrane composition. J Biol Chem 252 (1977) 409-415
    • (1977) J Biol Chem , vol.252 , pp. 409-415
    • Kandutsch, A.A.1    Chen, H.W.2
  • 26
    • 0017646560 scopus 로고
    • 7-Ketocholeserol Its effects on hepatic cholesterogenesis and its hepatic metabolism in vivo and in vitro
    • Erickson S.K., Cooper A.D., Matsui S.M., and Gould R.G. 7-Ketocholeserol Its effects on hepatic cholesterogenesis and its hepatic metabolism in vivo and in vitro. J Biol Chem 252 (1977) 5186-5193
    • (1977) J Biol Chem , vol.252 , pp. 5186-5193
    • Erickson, S.K.1    Cooper, A.D.2    Matsui, S.M.3    Gould, R.G.4
  • 27
    • 0021747172 scopus 로고
    • Correlation between oxysterol binding to a cytosolic binding protein and potency in the repression of hydroxymethylglutaryl coenzyme A reductase
    • Taylor F.R., Saucier S.E., Shown E.P., Parish E.J., and Kandutsch A.A. Correlation between oxysterol binding to a cytosolic binding protein and potency in the repression of hydroxymethylglutaryl coenzyme A reductase. J Biol Chem 259 (1984) 12382-12387
    • (1984) J Biol Chem , vol.259 , pp. 12382-12387
    • Taylor, F.R.1    Saucier, S.E.2    Shown, E.P.3    Parish, E.J.4    Kandutsch, A.A.5
  • 28
    • 11144233997 scopus 로고    scopus 로고
    • Oxysterols and oxysterol binding proteins: role in lipid metabolism and atherosclerosis
    • Olkkonen V.M., and Lehto M. Oxysterols and oxysterol binding proteins: role in lipid metabolism and atherosclerosis. Ann Med 36 (2004) 562-572
    • (2004) Ann Med , vol.36 , pp. 562-572
    • Olkkonen, V.M.1    Lehto, M.2
  • 29
    • 34547439826 scopus 로고    scopus 로고
    • The mammalian oxysterol-binding protein-related proteins (ORPs) bind 25-hydroxycholesterol in an evolutionarily conserved pocket
    • Suchanek M., Hynynen R., Wohlfahrt G., Lehto M., Johansson M., Saarinen H., et al. The mammalian oxysterol-binding protein-related proteins (ORPs) bind 25-hydroxycholesterol in an evolutionarily conserved pocket. Biochem J 405 (2007) 473-480
    • (2007) Biochem J , vol.405 , pp. 473-480
    • Suchanek, M.1    Hynynen, R.2    Wohlfahrt, G.3    Lehto, M.4    Johansson, M.5    Saarinen, H.6
  • 30
    • 23844453427 scopus 로고    scopus 로고
    • Inhibition of cholesterol biosynthesis by 25-hydroxycholesterol is independent of OSBP
    • Nishimura T., Inoue T., Shibata N., Sekine A., Takabe W., Noguchi N., et al. Inhibition of cholesterol biosynthesis by 25-hydroxycholesterol is independent of OSBP. Genes Cells 10 (2005) 793-801
    • (2005) Genes Cells , vol.10 , pp. 793-801
    • Nishimura, T.1    Inoue, T.2    Shibata, N.3    Sekine, A.4    Takabe, W.5    Noguchi, N.6
  • 31
    • 10644239801 scopus 로고    scopus 로고
    • Cholesterol and 25-hydroxycholesterol inhibit activation of SREBPs by different mechanisms, both involving SCAP and Insigs
    • Adams C.M., Reitz J., De Brabander J.K., Feramisco J.D., Li L., Brown M.S., et al. Cholesterol and 25-hydroxycholesterol inhibit activation of SREBPs by different mechanisms, both involving SCAP and Insigs. J Biol Chem 279 (2004) 52772-52780
    • (2004) J Biol Chem , vol.279 , pp. 52772-52780
    • Adams, C.M.1    Reitz, J.2    De Brabander, J.K.3    Feramisco, J.D.4    Li, L.5    Brown, M.S.6
  • 32
    • 0036671360 scopus 로고    scopus 로고
    • Cholesterol addition to ER membranes alters conformation of SCAP, the SREBP escort protein that regulates cholesterol metabolism
    • Brown A.J., Sun L., Feramisco J.D., Brown M.S., and Goldstein J.L. Cholesterol addition to ER membranes alters conformation of SCAP, the SREBP escort protein that regulates cholesterol metabolism. Mol Cell 10 (2002) 237-245
    • (2002) Mol Cell , vol.10 , pp. 237-245
    • Brown, A.J.1    Sun, L.2    Feramisco, J.D.3    Brown, M.S.4    Goldstein, J.L.5
  • 33
    • 0035063045 scopus 로고    scopus 로고
    • Key regulatory oxysterols in liver: analysis as delta4-3-ketone derivatives by HPLC and response to physiological perturbations
    • Zhang Z., Li D., Blanchard D.E., Lear S.R., Erickson S.K., and Spencer T.A. Key regulatory oxysterols in liver: analysis as delta4-3-ketone derivatives by HPLC and response to physiological perturbations. J Lipid Res 42 (2001) 649-658
    • (2001) J Lipid Res , vol.42 , pp. 649-658
    • Zhang, Z.1    Li, D.2    Blanchard, D.E.3    Lear, S.R.4    Erickson, S.K.5    Spencer, T.A.6
  • 35
    • 0019939669 scopus 로고
    • Inhibition of hepatic cholesterol synthesis in mice by sterols with shortened and stereochemically varied side chains
    • Erickson K.A., and Nes W.R. Inhibition of hepatic cholesterol synthesis in mice by sterols with shortened and stereochemically varied side chains. Proc Natl Acad Sci USA 79 (1982) 4873-4877
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 4873-4877
    • Erickson, K.A.1    Nes, W.R.2
  • 36
    • 11944268807 scopus 로고
    • Role of oxysterols in the regulation of cholesterol homeostasis: a critical evaluation
    • Lund E., and Björkhem I. Role of oxysterols in the regulation of cholesterol homeostasis: a critical evaluation. Acc Chem Res 28 (1995) 241-250
    • (1995) Acc Chem Res , vol.28 , pp. 241-250
    • Lund, E.1    Björkhem, I.2
  • 37
  • 38
    • 0032511035 scopus 로고    scopus 로고
    • Markedly reduced bile acid synthesis but maintained levels of cholesterol and vitamin D metabolites in mice with disrupted sterol 27-hydroxylase gene
    • Rosen H., Reshef A., Maeda N., Lippoldt A., Shpizen S., Triger L., et al. Markedly reduced bile acid synthesis but maintained levels of cholesterol and vitamin D metabolites in mice with disrupted sterol 27-hydroxylase gene. J Biol Chem 273 (1998) 14805-14812
    • (1998) J Biol Chem , vol.273 , pp. 14805-14812
    • Rosen, H.1    Reshef, A.2    Maeda, N.3    Lippoldt, A.4    Shpizen, S.5    Triger, L.6
  • 39
    • 0036736781 scopus 로고    scopus 로고
    • Do oxysterols control cholesterol homeostasis?
    • Björkhem I. Do oxysterols control cholesterol homeostasis?. J Clin Invest 110 (2002) 725-730
    • (2002) J Clin Invest , vol.110 , pp. 725-730
    • Björkhem, I.1
  • 41
    • 0036096897 scopus 로고    scopus 로고
    • Oxysterols: friends, foes, or just fellow passengers?
    • Björkhem I., and Diczfalusy U. Oxysterols: friends, foes, or just fellow passengers?. Arterioscler Thromb Vasc Biol 22 (2002) 734-742
    • (2002) Arterioscler Thromb Vasc Biol , vol.22 , pp. 734-742
    • Björkhem, I.1    Diczfalusy, U.2
  • 42
    • 0027190308 scopus 로고
    • Nuclear protein that binds sterol regulatory element of low density lipoprotein receptor promoter I. Identification of the protein and delineation of its target nucleotide sequence
    • Briggs M.R., Yokoyama C., Wang X., Brown M.S., and Goldstein J.L. Nuclear protein that binds sterol regulatory element of low density lipoprotein receptor promoter I. Identification of the protein and delineation of its target nucleotide sequence. J Biol Chem 268 (1993) 14490-14496
    • (1993) J Biol Chem , vol.268 , pp. 14490-14496
    • Briggs, M.R.1    Yokoyama, C.2    Wang, X.3    Brown, M.S.4    Goldstein, J.L.5
  • 43
    • 0028225462 scopus 로고
    • SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis
    • Wang X., Sato R., Brown M.S., Hua X., and Goldstein J.L. SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis. Cell 77 (1994) 53-62
    • (1994) Cell , vol.77 , pp. 53-62
    • Wang, X.1    Sato, R.2    Brown, M.S.3    Hua, X.4    Goldstein, J.L.5
  • 44
  • 45
    • 0141591549 scopus 로고    scopus 로고
    • Cholesterol-induced conformational change in SCAP enhanced by Insig proteins and mimicked by cationic amphiphiles
    • Adams C.M., Goldstein J.L., and Brown M.S. Cholesterol-induced conformational change in SCAP enhanced by Insig proteins and mimicked by cationic amphiphiles. Proc Natl Acad Sci U S A 100 (2003) 10647-10652
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 10647-10652
    • Adams, C.M.1    Goldstein, J.L.2    Brown, M.S.3
  • 46
    • 3242668095 scopus 로고    scopus 로고
    • Direct binding of cholesterol to the purified membrane region of SCAP: mechanism for a sterol-sensing domain
    • Radhakrishnan A., Sun L.P., Kwon H.J., Brown M.S., and Goldstein J.L. Direct binding of cholesterol to the purified membrane region of SCAP: mechanism for a sterol-sensing domain. Mol Cell 15 (2004) 259-268
    • (2004) Mol Cell , vol.15 , pp. 259-268
    • Radhakrishnan, A.1    Sun, L.P.2    Kwon, H.J.3    Brown, M.S.4    Goldstein, J.L.5
  • 47
    • 34249848111 scopus 로고    scopus 로고
    • Sterol-regulated transport of SREBPs from endoplasmic reticulum to golgi: oxysterols block transport by binding to Insig
    • Radhakrishnan A., Ikeda Y., Kwon H.J., Brown M.S., and Goldstein J.L. Sterol-regulated transport of SREBPs from endoplasmic reticulum to golgi: oxysterols block transport by binding to Insig. Proc Natl Acad Sci USA 104 (2007) 6511-6518
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 6511-6518
    • Radhakrishnan, A.1    Ikeda, Y.2    Kwon, H.J.3    Brown, M.S.4    Goldstein, J.L.5
  • 48
    • 0037245750 scopus 로고    scopus 로고
    • Accelerated degradation of HMG CoA reductase mediated by binding of insig-1 to its sterol-sensing domain
    • Sever N., Yang T., Brown M.S., Goldstein J.L., and DeBose-Boyd R.A. Accelerated degradation of HMG CoA reductase mediated by binding of insig-1 to its sterol-sensing domain. Mol Cell 11 (2003) 25-33
    • (2003) Mol Cell , vol.11 , pp. 25-33
    • Sever, N.1    Yang, T.2    Brown, M.S.3    Goldstein, J.L.4    DeBose-Boyd, R.A.5
  • 49
    • 0031042762 scopus 로고    scopus 로고
    • Unique requirements for retinoid-dependent transcriptional activation by the orphan receptor LXR
    • Willy P.J., and Mangelsdorf D.J. Unique requirements for retinoid-dependent transcriptional activation by the orphan receptor LXR. Genes Dev 11 (1997) 289-298
    • (1997) Genes Dev , vol.11 , pp. 289-298
    • Willy, P.J.1    Mangelsdorf, D.J.2
  • 50
    • 34248647293 scopus 로고    scopus 로고
    • Liver X receptors and cholesterol homoeostasis: spotlight on the adrenal gland
    • Cummins C.L., and Mangelsdorf D.J. Liver X receptors and cholesterol homoeostasis: spotlight on the adrenal gland. Biochem Soc Trans 34 (2006) 1110-1113
    • (2006) Biochem Soc Trans , vol.34 , pp. 1110-1113
    • Cummins, C.L.1    Mangelsdorf, D.J.2
  • 52
    • 14444285707 scopus 로고    scopus 로고
    • Activation of the nuclear receptor LXR by oxysterols defines a new hormone response pathway
    • Lehmann J.M., Kliewer S.A., Moore L.B., Smith-Oliver T.A., Oliver B.B., Su J.L., et al. Activation of the nuclear receptor LXR by oxysterols defines a new hormone response pathway. J Biol Chem 272 (1997) 3137-3140
    • (1997) J Biol Chem , vol.272 , pp. 3137-3140
    • Lehmann, J.M.1    Kliewer, S.A.2    Moore, L.B.3    Smith-Oliver, T.A.4    Oliver, B.B.5    Su, J.L.6
  • 54
    • 0141737105 scopus 로고    scopus 로고
    • Crystal structure of the heterodimeric complex of LXRalpha and RXRbeta ligand-binding domains in a fully agonistic conformation
    • Svensson S., Ostberg T., Jacobsson M., Norstrom C., Stefansson K., Hallen D., et al. Crystal structure of the heterodimeric complex of LXRalpha and RXRbeta ligand-binding domains in a fully agonistic conformation. Embo J 22 (2003) 4625-4633
    • (2003) Embo J , vol.22 , pp. 4625-4633
    • Svensson, S.1    Ostberg, T.2    Jacobsson, M.3    Norstrom, C.4    Stefansson, K.5    Hallen, D.6
  • 55
    • 33748792007 scopus 로고    scopus 로고
    • Sterol intermediates from cholesterol biosynthetic pathway as liver X receptor ligands
    • Yang C., McDonald J.G., Patel A., Zhang Y., Umetani M., Xu F., et al. Sterol intermediates from cholesterol biosynthetic pathway as liver X receptor ligands. J Biol Chem 281 (2006) 27816-27826
    • (2006) J Biol Chem , vol.281 , pp. 27816-27826
    • Yang, C.1    McDonald, J.G.2    Patel, A.3    Zhang, Y.4    Umetani, M.5    Xu, F.6
  • 56
    • 33845587711 scopus 로고    scopus 로고
    • Enzymatic reduction of oxysterols impairs LXR signaling in cultured cells and the livers of mice
    • Chen W., Chen G., Head D.L., Mangelsdorf D.J., and Russell D.W. Enzymatic reduction of oxysterols impairs LXR signaling in cultured cells and the livers of mice. Cell Metab 5 (2007) 73-79
    • (2007) Cell Metab , vol.5 , pp. 73-79
    • Chen, W.1    Chen, G.2    Head, D.L.3    Mangelsdorf, D.J.4    Russell, D.W.5
  • 57
    • 38149138153 scopus 로고    scopus 로고
    • Endogenous 24(S),25-epoxycholesterol fine-tunes acute control of cellular cholesterol homeostasis
    • Wong J., Quinn C.M., Gelissen I.C., and Brown A.J. Endogenous 24(S),25-epoxycholesterol fine-tunes acute control of cellular cholesterol homeostasis. J Biol Chem 283 (2008) 700-707
    • (2008) J Biol Chem , vol.283 , pp. 700-707
    • Wong, J.1    Quinn, C.M.2    Gelissen, I.C.3    Brown, A.J.4
  • 58
    • 12144291619 scopus 로고    scopus 로고
    • Statins downregulate ATP-binding-cassette transporter A1 gene expression in macrophages
    • Sone H., Shimano H., Shu M., Nakakuki M., Takahashi A., Sakai M., et al. Statins downregulate ATP-binding-cassette transporter A1 gene expression in macrophages. Biochem Biophys Res Commun 316 (2004) 790-794
    • (2004) Biochem Biophys Res Commun , vol.316 , pp. 790-794
    • Sone, H.1    Shimano, H.2    Shu, M.3    Nakakuki, M.4    Takahashi, A.5    Sakai, M.6
  • 59
    • 38049081038 scopus 로고    scopus 로고
    • The effect of statins on ABCA1 and ABCG1 expression in human macrophages is influenced by cellular cholesterol levels and extent of differentiation
    • Wong J., Quinn C.M., Gelissen I.C., Jessup W., and Brown A.J. The effect of statins on ABCA1 and ABCG1 expression in human macrophages is influenced by cellular cholesterol levels and extent of differentiation. Atherosclerosis 196 (2008) 180-189
    • (2008) Atherosclerosis , vol.196 , pp. 180-189
    • Wong, J.1    Quinn, C.M.2    Gelissen, I.C.3    Jessup, W.4    Brown, A.J.5
  • 60
    • 10644229420 scopus 로고    scopus 로고
    • Statins inhibit synthesis of an oxysterol ligand for the liver X receptor in human macrophages with consequences for cholesterol flux
    • Wong J., Quinn C.M., and Brown A.J. Statins inhibit synthesis of an oxysterol ligand for the liver X receptor in human macrophages with consequences for cholesterol flux. Arterioscler Thromb Vasc Biol 24 (2004) 2365-2371
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , pp. 2365-2371
    • Wong, J.1    Quinn, C.M.2    Brown, A.J.3
  • 61
    • 33845748205 scopus 로고    scopus 로고
    • SREBP-2 positively regulates transcription of the cholesterol efflux gene, ABCA1 by generating oxysterol ligands for LXR
    • Wong J., Quinn C.M., and Brown A.J. SREBP-2 positively regulates transcription of the cholesterol efflux gene, ABCA1 by generating oxysterol ligands for LXR. Biochem J 400 (2006) 485-491
    • (2006) Biochem J , vol.400 , pp. 485-491
    • Wong, J.1    Quinn, C.M.2    Brown, A.J.3
  • 62
    • 0019420840 scopus 로고
    • Biosynthesis of 24,25-epoxycholesterol from squalene 2,3;22,23-dioxide
    • Nelson J.A., Steckbeck S.R., and Spencer T.A. Biosynthesis of 24,25-epoxycholesterol from squalene 2,3;22,23-dioxide. J Biol Chem 256 (1981) 1067-1068
    • (1981) J Biol Chem , vol.256 , pp. 1067-1068
    • Nelson, J.A.1    Steckbeck, S.R.2    Spencer, T.A.3
  • 63
    • 0022346351 scopus 로고
    • 24(S),25-Epoxycholesterol, evidence consistent with a role in the regulation of hepatic cholesterogenesis
    • Spencer T.A., Gayen A.K., Phirwa S., Nelson J.A., Taylor F.R., Kandutsch A.A., et al. 24(S),25-Epoxycholesterol, evidence consistent with a role in the regulation of hepatic cholesterogenesis. J Biol Chem 260 (1985) 13391-13394
    • (1985) J Biol Chem , vol.260 , pp. 13391-13394
    • Spencer, T.A.1    Gayen, A.K.2    Phirwa, S.3    Nelson, J.A.4    Taylor, F.R.5    Kandutsch, A.A.6
  • 64
    • 0035976936 scopus 로고    scopus 로고
    • The hypocholesterolemic agent LY295427 reverses suppression of sterol regulatory element-binding protein processing mediated by oxysterols
    • Janowski B.A., Shan B., and Russell D.W. The hypocholesterolemic agent LY295427 reverses suppression of sterol regulatory element-binding protein processing mediated by oxysterols. J Biol Chem 276 (2001) 45408-45416
    • (2001) J Biol Chem , vol.276 , pp. 45408-45416
    • Janowski, B.A.1    Shan, B.2    Russell, D.W.3
  • 65
    • 0142120095 scopus 로고    scopus 로고
    • Enhanced synthesis of the oxysterol 24(S),25-epoxycholesterol in macrophages by inhibitors of 2,3-oxidosqualene:lanosterol cyclase: a novel mechanism for the attenuation of foam cell formation
    • Rowe A.H., Argmann C.A., Edwards J.Y., Sawyez C.G., Morand O.H., Hegele R.A., et al. Enhanced synthesis of the oxysterol 24(S),25-epoxycholesterol in macrophages by inhibitors of 2,3-oxidosqualene:lanosterol cyclase: a novel mechanism for the attenuation of foam cell formation. Circ Res 93 (2003) 717-725
    • (2003) Circ Res , vol.93 , pp. 717-725
    • Rowe, A.H.1    Argmann, C.A.2    Edwards, J.Y.3    Sawyez, C.G.4    Morand, O.H.5    Hegele, R.A.6
  • 66
    • 3142654791 scopus 로고    scopus 로고
    • Ubiquitination of 3-hydroxy-3-methylglutaryl CoA reductase in permeabilized cells mediated by cytosolic E1 and a putative membrane-bound ubiquitin ligase
    • Song B.-L., and DeBose-Boyd R.A. Ubiquitination of 3-hydroxy-3-methylglutaryl CoA reductase in permeabilized cells mediated by cytosolic E1 and a putative membrane-bound ubiquitin ligase. J Biol Chem 279 (2004) 28798-28806
    • (2004) J Biol Chem , vol.279 , pp. 28798-28806
    • Song, B.-L.1    DeBose-Boyd, R.A.2
  • 67
    • 36249006573 scopus 로고    scopus 로고
    • Primary human astrocytes produce 24(S),25-epoxycholesterol with implications for brain cholesterol homeostasis
    • Wong J., Quinn C.M., Guillemin G., and Brown A.J. Primary human astrocytes produce 24(S),25-epoxycholesterol with implications for brain cholesterol homeostasis. J Neurochem 103 (2007) 1764-1773
    • (2007) J Neurochem , vol.103 , pp. 1764-1773
    • Wong, J.1    Quinn, C.M.2    Guillemin, G.3    Brown, A.J.4
  • 68
    • 34247381583 scopus 로고    scopus 로고
    • Synthesis of the oxysterol, 24(S), 25-epoxycholesterol, parallels cholesterol production and may protect against cellular accumulation of newly-synthesized cholesterol
    • Wong J., Quinn C.M., and Brown A.J. Synthesis of the oxysterol, 24(S), 25-epoxycholesterol, parallels cholesterol production and may protect against cellular accumulation of newly-synthesized cholesterol. Lipids Health Dis 6 (2007) 10
    • (2007) Lipids Health Dis , vol.6 , pp. 10
    • Wong, J.1    Quinn, C.M.2    Brown, A.J.3
  • 69
    • 0027968653 scopus 로고
    • Effects of a 2,3-oxidosqualene-lanosterol cyclase inhibitor, 2,3:22,23-dioxidosqualene and 24,25-epoxycholesterol on the regulation of cholesterol biosynthesis in human hepatoma cell line HepG2
    • Dollis D., and Schuber F. Effects of a 2,3-oxidosqualene-lanosterol cyclase inhibitor, 2,3:22,23-dioxidosqualene and 24,25-epoxycholesterol on the regulation of cholesterol biosynthesis in human hepatoma cell line HepG2. Biochem Pharmacol 48 (1994) 49-57
    • (1994) Biochem Pharmacol , vol.48 , pp. 49-57
    • Dollis, D.1    Schuber, F.2
  • 70
    • 0030064188 scopus 로고    scopus 로고
    • Effects of a novel 2,3-oxidosqualene cyclase inhibitor on the regulation of cholesterol biosynthesis in HepG2 cells
    • Mark M., Muller P., Maier R., and Eisele B. Effects of a novel 2,3-oxidosqualene cyclase inhibitor on the regulation of cholesterol biosynthesis in HepG2 cells. J Lipid Res 37 (1996) 148-158
    • (1996) J Lipid Res , vol.37 , pp. 148-158
    • Mark, M.1    Muller, P.2    Maier, R.3    Eisele, B.4
  • 71
    • 34247139296 scopus 로고    scopus 로고
    • Selective up-regulation of LXR-regulated genes ABCA1, ABCG1, and APOE in macrophages through increased endogenous synthesis of 24(S),25-epoxycholesterol
    • Beyea M.M., Heslop C.L., Sawyez C.G., Edwards J.Y., Markle J.G., Hegele R.A., et al. Selective up-regulation of LXR-regulated genes ABCA1, ABCG1, and APOE in macrophages through increased endogenous synthesis of 24(S),25-epoxycholesterol. J Biol Chem 282 (2007) 5207-5216
    • (2007) J Biol Chem , vol.282 , pp. 5207-5216
    • Beyea, M.M.1    Heslop, C.L.2    Sawyez, C.G.3    Edwards, J.Y.4    Markle, J.G.5    Hegele, R.A.6
  • 72
    • 0042972934 scopus 로고    scopus 로고
    • The endoplasmic reticulum is the site of cholesterol-induced cytotoxicity in macrophages
    • Feng B., Yao P.M., Li Y., Devlin C.M., Zhang D., Harding H.P., et al. The endoplasmic reticulum is the site of cholesterol-induced cytotoxicity in macrophages. Nat Cell Biol 5 (2003) 781-792
    • (2003) Nat Cell Biol , vol.5 , pp. 781-792
    • Feng, B.1    Yao, P.M.2    Li, Y.3    Devlin, C.M.4    Zhang, D.5    Harding, H.P.6
  • 73
    • 0026627805 scopus 로고
    • Post-transcriptional regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by 24(S),25-oxidolanosterol
    • Panini S.R., Delate T.A., and Sinensky M. Post-transcriptional regulation of 3-hydroxy-3-methylglutaryl coenzyme A reductase by 24(S),25-oxidolanosterol. J Biol Chem 267 (1992) 12647-12654
    • (1992) J Biol Chem , vol.267 , pp. 12647-12654
    • Panini, S.R.1    Delate, T.A.2    Sinensky, M.3
  • 74
    • 35148813852 scopus 로고    scopus 로고
    • Studies on the cholesterol-free mouse: strong activation of LXR-regulated hepatic genes when replacing cholesterol with desmosterol
    • Heverin M., Meaney S., Brafman A., Shafir M., Olin M., Shafaati M., et al. Studies on the cholesterol-free mouse: strong activation of LXR-regulated hepatic genes when replacing cholesterol with desmosterol. Arterioscler Thromb Vasc Biol 27 (2007) 2191-2197
    • (2007) Arterioscler Thromb Vasc Biol , vol.27 , pp. 2191-2197
    • Heverin, M.1    Meaney, S.2    Brafman, A.3    Shafir, M.4    Olin, M.5    Shafaati, M.6
  • 75
    • 0015606662 scopus 로고
    • Desmosterol levels in human foetal brain - a reassessment
    • Dennick R.G., Dean P.D., and Abramovich D.A. Desmosterol levels in human foetal brain - a reassessment. J Neurochem 20 (1973) 1293-1294
    • (1973) J Neurochem , vol.20 , pp. 1293-1294
    • Dennick, R.G.1    Dean, P.D.2    Abramovich, D.A.3
  • 76
    • 18544378347 scopus 로고    scopus 로고
    • Insig-mediated degradation of HMG CoA reductase stimulated by lanosterol, an intermediate in the synthesis of cholesterol
    • Song B.-L., Javitt N.B., and DeBose-Boyd R.A. Insig-mediated degradation of HMG CoA reductase stimulated by lanosterol, an intermediate in the synthesis of cholesterol. Cell Metab 1 (2005) 179-189
    • (2005) Cell Metab , vol.1 , pp. 179-189
    • Song, B.-L.1    Javitt, N.B.2    DeBose-Boyd, R.A.3
  • 77
    • 34848866023 scopus 로고    scopus 로고
    • Hypoxia stimulates degradation of 3-hydroxy-3-methylglutaryl-coenzyme A Reductase through accumulation of lanosterol and hypoxia-inducible factor-mediated induction of Insigs
    • Nguyen A.D., McDonald J.G., Bruick R.K., and DeBose-Boyd R.A. Hypoxia stimulates degradation of 3-hydroxy-3-methylglutaryl-coenzyme A Reductase through accumulation of lanosterol and hypoxia-inducible factor-mediated induction of Insigs. J Biol Chem 282 (2007) 27436-27446
    • (2007) J Biol Chem , vol.282 , pp. 27436-27446
    • Nguyen, A.D.1    McDonald, J.G.2    Bruick, R.K.3    DeBose-Boyd, R.A.4
  • 78
    • 17644401005 scopus 로고    scopus 로고
    • SREBP pathway responds to sterols and functions as an oxygen sensor in fission yeast
    • Hughes A.L., Todd B.L., and Espenshade P.J. SREBP pathway responds to sterols and functions as an oxygen sensor in fission yeast. Cell 120 (2005) 831-842
    • (2005) Cell , vol.120 , pp. 831-842
    • Hughes, A.L.1    Todd, B.L.2    Espenshade, P.J.3
  • 79
    • 34548245574 scopus 로고    scopus 로고
    • 4-Methyl sterols regulate fission yeast SREBP-Scap under low oxygen and cell stress
    • Hughes A.L., Lee C.-Y.S., Bien C.M., and Espenshade P.J. 4-Methyl sterols regulate fission yeast SREBP-Scap under low oxygen and cell stress. J Biol Chem 282 (2007) 24388-24396
    • (2007) J Biol Chem , vol.282 , pp. 24388-24396
    • Hughes, A.L.1    Lee, C.-Y.S.2    Bien, C.M.3    Espenshade, P.J.4
  • 80
    • 34547121206 scopus 로고    scopus 로고
    • Hypoxia in cancer: significance and impact on clinical outcome
    • Vaupel P., and Mayer A. Hypoxia in cancer: significance and impact on clinical outcome. Cancer Metastasis Rev 26 (2007) 225-240
    • (2007) Cancer Metastasis Rev , vol.26 , pp. 225-240
    • Vaupel, P.1    Mayer, A.2
  • 81
    • 38949134571 scopus 로고    scopus 로고
    • Oxidative stress in obstructive sleep apnea: putative pathways to the cardiovascular complications
    • Yamauchi M., and Kimura H. Oxidative stress in obstructive sleep apnea: putative pathways to the cardiovascular complications. Antioxid Redox Signal 10 (2008) 755-769
    • (2008) Antioxid Redox Signal , vol.10 , pp. 755-769
    • Yamauchi, M.1    Kimura, H.2
  • 82
    • 2442557294 scopus 로고    scopus 로고
    • Brain cholesterol: long secret life behind a barrier
    • Björkhem I., and Meaney S. Brain cholesterol: long secret life behind a barrier. Arterioscler Thromb Vasc Biol 24 (2004) 806-815
    • (2004) Arterioscler Thromb Vasc Biol , vol.24 , pp. 806-815
    • Björkhem, I.1    Meaney, S.2
  • 83
    • 0030008367 scopus 로고    scopus 로고
    • Sterol efflux is impaired from macrophage foam cells selectively enriched with 7-ketocholesterol
    • Gelissen I.C., Brown A.J., Mander E.L., Kritharides L., Dean R.T., and Jessup W. Sterol efflux is impaired from macrophage foam cells selectively enriched with 7-ketocholesterol. J Biol Chem 271 (1996) 17852-17860
    • (1996) J Biol Chem , vol.271 , pp. 17852-17860
    • Gelissen, I.C.1    Brown, A.J.2    Mander, E.L.3    Kritharides, L.4    Dean, R.T.5    Jessup, W.6
  • 84
    • 0031848338 scopus 로고    scopus 로고
    • Cholesterol homeostasis in human brain: turnover of 24S-hydroxycholesterol and evidence for a cerebral origin of most of this oxysterol in the circulation
    • Björkhem I., Lütjohann D., Diczfalusy U., Stahle L., Ahlborg G., and Wahren J. Cholesterol homeostasis in human brain: turnover of 24S-hydroxycholesterol and evidence for a cerebral origin of most of this oxysterol in the circulation. J Lipid Res 39 (1998) 1594-1600
    • (1998) J Lipid Res , vol.39 , pp. 1594-1600
    • Björkhem, I.1    Lütjohann, D.2    Diczfalusy, U.3    Stahle, L.4    Ahlborg, G.5    Wahren, J.6
  • 86
    • 0032770376 scopus 로고    scopus 로고
    • Elimination of cholesterol as cholestenoic acid in human lung by sterol 27-hydroxylase: evidence that most of this steroid in the circulation is of pulmonary origin
    • Babiker A., Andersson O., Lindblom D., van der Linden J., Wiklund B., Lütjohann D., et al. Elimination of cholesterol as cholestenoic acid in human lung by sterol 27-hydroxylase: evidence that most of this steroid in the circulation is of pulmonary origin. J Lipid Res 40 (1999) 1417-1425
    • (1999) J Lipid Res , vol.40 , pp. 1417-1425
    • Babiker, A.1    Andersson, O.2    Lindblom, D.3    van der Linden, J.4    Wiklund, B.5    Lütjohann, D.6
  • 87
    • 0028068796 scopus 로고
    • Atherosclerosis and sterol 27-hydroxylase: evidence for a role of this enzyme in elimination of cholesterol from human macrophages
    • Björkhem I., Andersson O., Diczfalusy U., Sevastik B., Xiu R.J., Duan C., et al. Atherosclerosis and sterol 27-hydroxylase: evidence for a role of this enzyme in elimination of cholesterol from human macrophages. Proc Natl Acad Sci USA 91 (1994) 8592-8596
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8592-8596
    • Björkhem, I.1    Andersson, O.2    Diczfalusy, U.3    Sevastik, B.4    Xiu, R.J.5    Duan, C.6
  • 88
    • 33748420211 scopus 로고    scopus 로고
    • ABCA1 mediates high-affinity uptake of 25-hydroxycholesterol by membrane vesicles and rapid efflux of oxysterol by intact cells
    • Tam S.-P., Mok L., Chimini G., Vasa M., and Deeley R.G. ABCA1 mediates high-affinity uptake of 25-hydroxycholesterol by membrane vesicles and rapid efflux of oxysterol by intact cells. Am J Physiol Cell Physiol 291 (2006) 490-502
    • (2006) Am J Physiol Cell Physiol , vol.291 , pp. 490-502
    • Tam, S.-P.1    Mok, L.2    Chimini, G.3    Vasa, M.4    Deeley, R.G.5
  • 89
    • 34047127402 scopus 로고    scopus 로고
    • Expression of ATP binding cassette-transporter ABCG1 prevents cell death by transporting cytotoxic 7β-hydroxycholesterol
    • Engel T., Kannenberg F., Fobker M., Nofer J.-R., Bode G., Lueken A., et al. Expression of ATP binding cassette-transporter ABCG1 prevents cell death by transporting cytotoxic 7β-hydroxycholesterol. FEBS Letters 581 (2007) 1673-1680
    • (2007) FEBS Letters , vol.581 , pp. 1673-1680
    • Engel, T.1    Kannenberg, F.2    Fobker, M.3    Nofer, J.-R.4    Bode, G.5    Lueken, A.6
  • 90
    • 35448980715 scopus 로고    scopus 로고
    • High-density lipoprotein protects macrophages from oxidized low-density lipoprotein-induced apoptosis by promoting efflux of 7-ketocholesterol via ABCG1
    • Terasaka N., Wang N., Yvan-Charvet L., and Tall A.R. High-density lipoprotein protects macrophages from oxidized low-density lipoprotein-induced apoptosis by promoting efflux of 7-ketocholesterol via ABCG1. Proc Natl Acad Sci USA 104 (2007) 15093-15098
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 15093-15098
    • Terasaka, N.1    Wang, N.2    Yvan-Charvet, L.3    Tall, A.R.4
  • 91
    • 0028816863 scopus 로고
    • Determination of cholesterol oxidation products in human plasma by isotope dilution-mass spectrometry
    • Dzeletovic S., Breuer O., Lund E., and Diczfalusy U. Determination of cholesterol oxidation products in human plasma by isotope dilution-mass spectrometry. Anal Biochem 225 (1995) 73-80
    • (1995) Anal Biochem , vol.225 , pp. 73-80
    • Dzeletovic, S.1    Breuer, O.2    Lund, E.3    Diczfalusy, U.4
  • 92
    • 0034623160 scopus 로고    scopus 로고
    • Sterol 27-hydroxylase acts on 7-ketocholesterol in human atherosclerotic lesions and macrophages in culture
    • Brown A.J., Watts G.F., Burnett J.R., Dean R.T., and Jessup W. Sterol 27-hydroxylase acts on 7-ketocholesterol in human atherosclerotic lesions and macrophages in culture. J Biol Chem 275 (2000) 27627-27633
    • (2000) J Biol Chem , vol.275 , pp. 27627-27633
    • Brown, A.J.1    Watts, G.F.2    Burnett, J.R.3    Dean, R.T.4    Jessup, W.5
  • 93
    • 0034892932 scopus 로고    scopus 로고
    • Metabolism of an oxysterol, 7-ketocholesterol, by sterol 27-hydroxylase in HepG2 cells
    • Lyons M.A., and Brown A.J. Metabolism of an oxysterol, 7-ketocholesterol, by sterol 27-hydroxylase in HepG2 cells. Lipids 36 (2001) 701-711
    • (2001) Lipids , vol.36 , pp. 701-711
    • Lyons, M.A.1    Brown, A.J.2
  • 94
    • 33744904197 scopus 로고    scopus 로고
    • Expression and localization of sterol 27-hydroxylase (CYP27A1) in monkey retina
    • Lee J.W., Fuda H., Javitt N.B., Strott C.A., and Rodriguez I.R. Expression and localization of sterol 27-hydroxylase (CYP27A1) in monkey retina. Exp Eye Res 83 (2006) 465-469
    • (2006) Exp Eye Res , vol.83 , pp. 465-469
    • Lee, J.W.1    Fuda, H.2    Javitt, N.B.3    Strott, C.A.4    Rodriguez, I.R.5
  • 96
    • 2442513350 scopus 로고    scopus 로고
    • Rapid hepatic metabolism of 7-ketocholesterol by 11β-hydroxysteroid dehydrogenase type 1: species-specific differences between the rat, human and hamster enzyme
    • Schweizer R.A.S., Zurcher M., Balazs Z., Dick B., and Odermatt A. Rapid hepatic metabolism of 7-ketocholesterol by 11β-hydroxysteroid dehydrogenase type 1: species-specific differences between the rat, human and hamster enzyme. J Biol Chem 279 (2004) 18415-18424
    • (2004) J Biol Chem , vol.279 , pp. 18415-18424
    • Schweizer, R.A.S.1    Zurcher, M.2    Balazs, Z.3    Dick, B.4    Odermatt, A.5
  • 97
    • 34547118363 scopus 로고    scopus 로고
    • In vivo interconversion of 7β-hydroxycholesterol and 7-ketocholesterol, potential surrogate markers for oxidative stress
    • Larsson H., Bottiger Y., Iuliano L., and Diczfalusy U. In vivo interconversion of 7β-hydroxycholesterol and 7-ketocholesterol, potential surrogate markers for oxidative stress. Free Radical Biol Med 43 (2007) 695-701
    • (2007) Free Radical Biol Med , vol.43 , pp. 695-701
    • Larsson, H.1    Bottiger, Y.2    Iuliano, L.3    Diczfalusy, U.4
  • 98
  • 99
    • 0034895787 scopus 로고    scopus 로고
    • Expression and characterization of the human 3β-hydroxysteroid sulfotransferases (SULT2B1a and SULT2B1b)
    • Meloche C.A., and Falany C.N. Expression and characterization of the human 3β-hydroxysteroid sulfotransferases (SULT2B1a and SULT2B1b). J Steroid Biochem Mol Biol 77 (2001) 261-269
    • (2001) J Steroid Biochem Mol Biol , vol.77 , pp. 261-269
    • Meloche, C.A.1    Falany, C.N.2
  • 100
    • 0037387277 scopus 로고    scopus 로고
    • Conservation of the hydroxysteroid sulfotransferase SULT2B1 gene structure in the mouse: pre- and post-natal expression, kinetic analysis of isoforms, and comparison with prototypical SULT2A1
    • Shimizu C., Fuda H., Yanai H., and Strott C.A. Conservation of the hydroxysteroid sulfotransferase SULT2B1 gene structure in the mouse: pre- and post-natal expression, kinetic analysis of isoforms, and comparison with prototypical SULT2A1. Endocrinology 144 (2003) 1186-1193
    • (2003) Endocrinology , vol.144 , pp. 1186-1193
    • Shimizu, C.1    Fuda, H.2    Yanai, H.3    Strott, C.A.4
  • 101
    • 33846886738 scopus 로고    scopus 로고
    • PXR induces CYP27A1 and regulates cholesterol metabolism in the intestine
    • Li T., Chen W., and Chiang J.Y.L. PXR induces CYP27A1 and regulates cholesterol metabolism in the intestine. J Lipid Res 48 (2007) 373-384
    • (2007) J Lipid Res , vol.48 , pp. 373-384
    • Li, T.1    Chen, W.2    Chiang, J.Y.L.3
  • 102
  • 103
    • 0035372651 scopus 로고    scopus 로고
    • Auto-oxidized cholesterol sulfates are antagonistic ligands of liver X receptors: implications for the development and treatment of atherosclerosis
    • Song C., Hiipakka R.A., and Liao S. Auto-oxidized cholesterol sulfates are antagonistic ligands of liver X receptors: implications for the development and treatment of atherosclerosis. Steroids 66 (2001) 473-479
    • (2001) Steroids , vol.66 , pp. 473-479
    • Song, C.1    Hiipakka, R.A.2    Liao, S.3
  • 104
    • 0014573241 scopus 로고
    • Steroids in newborns and infants C19 and C21 steroids in faeces from infants
    • Gustafsson J.A., Shackleton C.H., and Sjovall J. Steroids in newborns and infants C19 and C21 steroids in faeces from infants. Eur J Biochem 10 (1969) 302-311
    • (1969) Eur J Biochem , vol.10 , pp. 302-311
    • Gustafsson, J.A.1    Shackleton, C.H.2    Sjovall, J.3
  • 105
    • 0030906963 scopus 로고    scopus 로고
    • High levels of (24S)-24-hydroxycholesterol 3-sulfate, 24-glucuronide in the serum and urine of children with severe cholestatic liver disease
    • Meng L.J., Griffiths W.J., Nazer H., Yang Y., and Sjovall J. High levels of (24S)-24-hydroxycholesterol 3-sulfate, 24-glucuronide in the serum and urine of children with severe cholestatic liver disease. J Lipid Res 38 (1997) 926-934
    • (1997) J Lipid Res , vol.38 , pp. 926-934
    • Meng, L.J.1    Griffiths, W.J.2    Nazer, H.3    Yang, Y.4    Sjovall, J.5
  • 106
    • 15444348784 scopus 로고    scopus 로고
    • ACAT-2, a second mammalian acyl-CoA:cholesterol acyltransferase its cloning, expression, and characterization
    • Cases S., Novak S., Zheng Y.-W., Myers H.M., Lear S.R., Sande E., et al. ACAT-2, a second mammalian acyl-CoA:cholesterol acyltransferase its cloning, expression, and characterization. J Biol Chem 273 (1998) 26755-26764
    • (1998) J Biol Chem , vol.273 , pp. 26755-26764
    • Cases, S.1    Novak, S.2    Zheng, Y.-W.3    Myers, H.M.4    Lear, S.R.5    Sande, E.6
  • 108
    • 0016691608 scopus 로고
    • Cholesterol ester formation in cultured human fibroblasts Stimulation by oxygenated sterols
    • Brown M.S., Dana S.E., and Goldstein J.L. Cholesterol ester formation in cultured human fibroblasts Stimulation by oxygenated sterols. J Biol Chem 250 (1975) 4025-4027
    • (1975) J Biol Chem , vol.250 , pp. 4025-4027
    • Brown, M.S.1    Dana, S.E.2    Goldstein, J.L.3
  • 109
    • 0030977396 scopus 로고    scopus 로고
    • Quantitation of the pool of cholesterol associated with acyl-CoA:cholesterol acyltransferase in human fibroblasts
    • Lange Y., and Steck T.L. Quantitation of the pool of cholesterol associated with acyl-CoA:cholesterol acyltransferase in human fibroblasts. J Biol Chem 272 (1997) 13103-13108
    • (1997) J Biol Chem , vol.272 , pp. 13103-13108
    • Lange, Y.1    Steck, T.L.2
  • 110
    • 33744732467 scopus 로고    scopus 로고
    • Involvement of Akt in ER-to-Golgi transport of SCAP/SREBP: a link between a key cell proliferative pathway and membrane synthesis
    • Du X., Kristiana I., Wong J., and Brown A.J. Involvement of Akt in ER-to-Golgi transport of SCAP/SREBP: a link between a key cell proliferative pathway and membrane synthesis. Mol Biol Cell 17 (2006) 2735-2745
    • (2006) Mol Biol Cell , vol.17 , pp. 2735-2745
    • Du, X.1    Kristiana, I.2    Wong, J.3    Brown, A.J.4
  • 111
    • 8744222698 scopus 로고    scopus 로고
    • Effects of 25-hydroxycholesterol on cholesterol esterification and SREBP processing are dissociable: Implications for cholesterol movement to the regulatory pool in the endoplasmic reticulum
    • Du X., Pham Y.H., and Brown A.J. Effects of 25-hydroxycholesterol on cholesterol esterification and SREBP processing are dissociable: Implications for cholesterol movement to the regulatory pool in the endoplasmic reticulum. J Biol Chem 279 (2004) 47010-47016
    • (2004) J Biol Chem , vol.279 , pp. 47010-47016
    • Du, X.1    Pham, Y.H.2    Brown, A.J.3
  • 112
    • 20444396178 scopus 로고    scopus 로고
    • Niemann-Pick type C disease and intracellular cholesterol trafficking
    • Chang T.-Y., Reid P.C., Sugii S., Ohgami N., Cruz J.C., and Chang C.C.Y. Niemann-Pick type C disease and intracellular cholesterol trafficking. J Biol Chem 280 (2005) 20917-20920
    • (2005) J Biol Chem , vol.280 , pp. 20917-20920
    • Chang, T.-Y.1    Reid, P.C.2    Sugii, S.3    Ohgami, N.4    Cruz, J.C.5    Chang, C.C.Y.6
  • 114
    • 0023608155 scopus 로고
    • Low density lipoprotein (LDL)-mediated suppression of cholesterol synthesis and LDL uptake is defective in Niemann-Pick type C fibroblasts
    • Liscum L., and Faust J.R. Low density lipoprotein (LDL)-mediated suppression of cholesterol synthesis and LDL uptake is defective in Niemann-Pick type C fibroblasts. J Biol Chem 262 (1987) 17002-17008
    • (1987) J Biol Chem , vol.262 , pp. 17002-17008
    • Liscum, L.1    Faust, J.R.2
  • 115
    • 0037815282 scopus 로고    scopus 로고
    • NPC1 and NPC2 regulate cellular cholesterol homeostasis through generation of low density lipoprotein cholesterol-derived oxysterols
    • Frolov A., Zielinski S.E., Crowley J.R., Dudley-Rucker N., Schaffer J.E., and Ory D.S. NPC1 and NPC2 regulate cellular cholesterol homeostasis through generation of low density lipoprotein cholesterol-derived oxysterols. J Biol Chem 278 (2003) 25517-25525
    • (2003) J Biol Chem , vol.278 , pp. 25517-25525
    • Frolov, A.1    Zielinski, S.E.2    Crowley, J.R.3    Dudley-Rucker, N.4    Schaffer, J.E.5    Ory, D.S.6
  • 116
    • 38149069055 scopus 로고    scopus 로고
    • Purified NPC1 protein: I Binding of cholesterol and oxysterols to a 1278-amino acid membrane protein
    • Infante R.E., Abi-Mosleh L., Radhakrishnan A., Dale J.D., Brown M.S., and Goldstein J.L. Purified NPC1 protein: I Binding of cholesterol and oxysterols to a 1278-amino acid membrane protein. J Biol Chem 283 (2007) 1052-1063
    • (2007) J Biol Chem , vol.283 , pp. 1052-1063
    • Infante, R.E.1    Abi-Mosleh, L.2    Radhakrishnan, A.3    Dale, J.D.4    Brown, M.S.5    Goldstein, J.L.6
  • 117
    • 0141459395 scopus 로고    scopus 로고
    • Quantitation of two pathways for cholesterol excretion from the brain in normal mice and mice with neurodegeneration
    • Xie C., Lund E.G., Turley S.D., Russell D.W., and Dietschy J.M. Quantitation of two pathways for cholesterol excretion from the brain in normal mice and mice with neurodegeneration. J Lipid Res 44 (2003) 1780-1789
    • (2003) J Lipid Res , vol.44 , pp. 1780-1789
    • Xie, C.1    Lund, E.G.2    Turley, S.D.3    Russell, D.W.4    Dietschy, J.M.5
  • 118
    • 2942738996 scopus 로고    scopus 로고
    • The Hedgehog response network: sensors, switches, and routers
    • Lum L., and Beachy P.A. The Hedgehog response network: sensors, switches, and routers. Science 304 (2004) 1755-1759
    • (2004) Science , vol.304 , pp. 1755-1759
    • Lum, L.1    Beachy, P.A.2
  • 119
    • 33846448142 scopus 로고    scopus 로고
    • Cholesterol, statins and cancer
    • Brown A.J. Cholesterol, statins and cancer. Clin Exper Pharm Physiol 34 (2007) 135-141
    • (2007) Clin Exper Pharm Physiol , vol.34 , pp. 135-141
    • Brown, A.J.1
  • 120
    • 34247844371 scopus 로고    scopus 로고
    • Oxysterols are novel activators of the hedgehog signaling pathway in pluripotent mesenchymal cells
    • Dwyer J.R., Sever N., Carlson M., Nelson S.F., Beachy P.A., and Parhami F. Oxysterols are novel activators of the hedgehog signaling pathway in pluripotent mesenchymal cells. J Biol Chem 282 (2007) 8959-8968
    • (2007) J Biol Chem , vol.282 , pp. 8959-8968
    • Dwyer, J.R.1    Sever, N.2    Carlson, M.3    Nelson, S.F.4    Beachy, P.A.5    Parhami, F.6
  • 121
    • 33744788672 scopus 로고    scopus 로고
    • Oxysterols stimulate Sonic hedgehog signal transduction and proliferation of medulloblastoma cells
    • Corcoran R.B., and Scott M.P. Oxysterols stimulate Sonic hedgehog signal transduction and proliferation of medulloblastoma cells. Proc Natl Acad Sci USA 103 (2006) 8408-8413
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 8408-8413
    • Corcoran, R.B.1    Scott, M.P.2
  • 122
    • 34547110771 scopus 로고    scopus 로고
    • Patched1 regulates hedgehog signaling at the primary cilium
    • Rohatgi R., Milenkovic L., and Scott M.P. Patched1 regulates hedgehog signaling at the primary cilium. Science 317 (2007) 372-376
    • (2007) Science , vol.317 , pp. 372-376
    • Rohatgi, R.1    Milenkovic, L.2    Scott, M.P.3
  • 123
    • 33746891890 scopus 로고    scopus 로고
    • The primary cilium as the cell's antenna: signaling at a sensory organelle
    • Singla V., and Reiter J.F. The primary cilium as the cell's antenna: signaling at a sensory organelle. Science 313 (2006) 629-633
    • (2006) Science , vol.313 , pp. 629-633
    • Singla, V.1    Reiter, J.F.2
  • 124
    • 33748297599 scopus 로고    scopus 로고
    • Severe facial clefting in Insig-deficient mouse embryos caused by sterol accumulation and reversed by lovastatin
    • Engelking L.J., Evers B.M., Richardson J.A., Goldstein J.L., Brown M.S., and Liang G. Severe facial clefting in Insig-deficient mouse embryos caused by sterol accumulation and reversed by lovastatin. J Clin Invest 116 (2006) 2356-2365
    • (2006) J Clin Invest , vol.116 , pp. 2356-2365
    • Engelking, L.J.1    Evers, B.M.2    Richardson, J.A.3    Goldstein, J.L.4    Brown, M.S.5    Liang, G.6
  • 125
    • 34248343047 scopus 로고    scopus 로고
    • Oxysterols: functional significance in fetal development and the maintenance of normal retinal function
    • Javitt N.B. Oxysterols: functional significance in fetal development and the maintenance of normal retinal function. Curr Opin Lipidol 18 (2007) 283-289
    • (2007) Curr Opin Lipidol , vol.18 , pp. 283-289
    • Javitt, N.B.1
  • 126
    • 33645127044 scopus 로고    scopus 로고
    • Oxysterol 22(R)-hydroxycholesterol induces the expression of the bile salt export pump through nuclear receptor Farsenoid X Receptor but not Liver X Receptor
    • Deng R., Yang D., Yang J., and Yan B. Oxysterol 22(R)-hydroxycholesterol induces the expression of the bile salt export pump through nuclear receptor Farsenoid X Receptor but not Liver X Receptor. J Pharmacol Exp Ther 317 (2006) 317-325
    • (2006) J Pharmacol Exp Ther , vol.317 , pp. 317-325
    • Deng, R.1    Yang, D.2    Yang, J.3    Yan, B.4
  • 128
    • 0032515062 scopus 로고    scopus 로고
    • Oxysterol regulation of steroidogenic acute regulatory protein gene expression structural specificity and transcriptional and posttranscriptional actions.
    • Christenson L.K., McAllister J.M., Martin K.O., Javitt N.B., Osborne T.F., and Strauss III J.F. Oxysterol regulation of steroidogenic acute regulatory protein gene expression structural specificity and transcriptional and posttranscriptional actions. J Biol Chem 273 (1998) 30729-30735
    • (1998) J Biol Chem , vol.273 , pp. 30729-30735
    • Christenson, L.K.1    McAllister, J.M.2    Martin, K.O.3    Javitt, N.B.4    Osborne, T.F.5    Strauss III, J.F.6
  • 130
    • 34948820661 scopus 로고    scopus 로고
    • 27-Hydroxycholesterol is an endogenous SERM that inhibits the cardiovascular effects of estrogen
    • Umetani M., Domoto H., Gormley A.K., Yuhanna I.S., Cummins C.L., Javitt N.B., et al. 27-Hydroxycholesterol is an endogenous SERM that inhibits the cardiovascular effects of estrogen. Nat Med 13 (2007) 1185-1192
    • (2007) Nat Med , vol.13 , pp. 1185-1192
    • Umetani, M.1    Domoto, H.2    Gormley, A.K.3    Yuhanna, I.S.4    Cummins, C.L.5    Javitt, N.B.6
  • 131
    • 0344737604 scopus 로고    scopus 로고
    • Activation of microglial Poly(ADP-Ribose)-Polymerase-1 by cholesterol breakdown products during neuroinflammation: a link between demyelination and neuronal damage
    • Diestel A., Aktas O., Hackel D., Hake I., Meier S., Raine C.S., et al. Activation of microglial Poly(ADP-Ribose)-Polymerase-1 by cholesterol breakdown products during neuroinflammation: a link between demyelination and neuronal damage. J Exp Med 198 (2003) 1729-1740
    • (2003) J Exp Med , vol.198 , pp. 1729-1740
    • Diestel, A.1    Aktas, O.2    Hackel, D.3    Hake, I.4    Meier, S.5    Raine, C.S.6
  • 132
    • 13944273308 scopus 로고    scopus 로고
    • Levels of 7-oxocholesterol in cerebrospinal fluid are more than one thousand times lower than reported in multiple sclerosis
    • Leoni V., Lütjohann D., and Masterman T. Levels of 7-oxocholesterol in cerebrospinal fluid are more than one thousand times lower than reported in multiple sclerosis. J Lipid Res 46 (2005) 191-195
    • (2005) J Lipid Res , vol.46 , pp. 191-195
    • Leoni, V.1    Lütjohann, D.2    Masterman, T.3
  • 133
    • 33745756094 scopus 로고    scopus 로고
    • Cholesterol metabolism in the brain: importance of 24S-hydroxylation
    • Lütjohann D. Cholesterol metabolism in the brain: importance of 24S-hydroxylation. Acta Neurol Scand Suppl 114 (2006) 33-42
    • (2006) Acta Neurol Scand Suppl , vol.114 , pp. 33-42
    • Lütjohann, D.1
  • 134
    • 0029835410 scopus 로고    scopus 로고
    • Cholesterol homeostasis in human brain: Evidence for an age-dependent flux of 24S-hydroxycholesterol from the brain into the circulation
    • Lütjohann D., Breuer O., Ahlborg G., Nennesmo I., Siden A., Diczfalusy U., et al. Cholesterol homeostasis in human brain: Evidence for an age-dependent flux of 24S-hydroxycholesterol from the brain into the circulation. Proc Natl Acad Sci USA 93 (1996) 9799-9804
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9799-9804
    • Lütjohann, D.1    Breuer, O.2    Ahlborg, G.3    Nennesmo, I.4    Siden, A.5    Diczfalusy, U.6
  • 136
    • 0029872744 scopus 로고    scopus 로고
    • Free and esterified oxysterol: formation during copper-oxidation of low density lipoprotein and uptake by macrophages
    • Brown A.J., Dean R.T., and Jessup W. Free and esterified oxysterol: formation during copper-oxidation of low density lipoprotein and uptake by macrophages. J Lipid Res 37 (1996) 320-335
    • (1996) J Lipid Res , vol.37 , pp. 320-335
    • Brown, A.J.1    Dean, R.T.2    Jessup, W.3
  • 137
    • 0031713657 scopus 로고    scopus 로고
    • Dietary oxysterols are incorporated in plasma triglyceride-rich lipoproteins, increase their susceptibility to oxidation and increase aortic cholesterol concentration of rabbits
    • Vine D.F., Mamo J.C.L., Beilin L.J., Mori T.A., and Croft K.D. Dietary oxysterols are incorporated in plasma triglyceride-rich lipoproteins, increase their susceptibility to oxidation and increase aortic cholesterol concentration of rabbits. J Lipid Res 39 (1998) 1995-2004
    • (1998) J Lipid Res , vol.39 , pp. 1995-2004
    • Vine, D.F.1    Mamo, J.C.L.2    Beilin, L.J.3    Mori, T.A.4    Croft, K.D.5
  • 138
    • 0030820068 scopus 로고    scopus 로고
    • 7-Hydroperoxycholesterol and its products in oxidized low density lipoprotein and human atherosclerotic plaque
    • Brown A.J., Leong S.L., Dean R.T., and Jessup W. 7-Hydroperoxycholesterol and its products in oxidized low density lipoprotein and human atherosclerotic plaque. J Lipid Res 38 (1997) 1730-1745
    • (1997) J Lipid Res , vol.38 , pp. 1730-1745
    • Brown, A.J.1    Leong, S.L.2    Dean, R.T.3    Jessup, W.4
  • 139
    • 41249093188 scopus 로고    scopus 로고
    • Extraction and analysis of sterols in biological matrices by high performance liquid chromatography electrospray ionization mass spectrometry
    • McDonald J., Thompson B., McCrum E., and Russell D.W. Extraction and analysis of sterols in biological matrices by high performance liquid chromatography electrospray ionization mass spectrometry. Methods Enzymol 432 (2007) 145-170
    • (2007) Methods Enzymol , vol.432 , pp. 145-170
    • McDonald, J.1    Thompson, B.2    McCrum, E.3    Russell, D.W.4
  • 140
    • 34147118488 scopus 로고    scopus 로고
    • Liquid chromatography-mass spectrometry utilizing multi-stage fragmentation for the identification of oxysterols
    • Karu K., Hornshaw M., Woffendin G., Bodin K., Hamberg M., Alvelius G., et al. Liquid chromatography-mass spectrometry utilizing multi-stage fragmentation for the identification of oxysterols. J Lipid Res 48 (2007) 976-987
    • (2007) J Lipid Res , vol.48 , pp. 976-987
    • Karu, K.1    Hornshaw, M.2    Woffendin, G.3    Bodin, K.4    Hamberg, M.5    Alvelius, G.6
  • 141
    • 0242660992 scopus 로고    scopus 로고
    • Quantitation of receptor ligands by mass spectrometry
    • Lund E.G., and Dizcfaluzy U. Quantitation of receptor ligands by mass spectrometry. Methods Enzymol 364 (2003) 24-37
    • (2003) Methods Enzymol , vol.364 , pp. 24-37
    • Lund, E.G.1    Dizcfaluzy, U.2
  • 143
    • 0001487484 scopus 로고
    • The in vitro production of 25- and 26-hydroxycholesterol and their in vivo metabolism
    • Fredrickson D.S., and Ono K. The in vitro production of 25- and 26-hydroxycholesterol and their in vivo metabolism. Biochim Biophys Acta 22 (1956) 183-184
    • (1956) Biochim Biophys Acta , vol.22 , pp. 183-184
    • Fredrickson, D.S.1    Ono, K.2
  • 144
    • 0029835410 scopus 로고    scopus 로고
    • Cholesterol homeostasis in human brain: evidence for an age-dependent flux of 24S-hydroxycholesterol from the brain into the circulation
    • Lütjohann D., Breuer O., Ahlborg G., Nennesmo I., Siden A., Diczfalusy U., et al. Cholesterol homeostasis in human brain: evidence for an age-dependent flux of 24S-hydroxycholesterol from the brain into the circulation. Proc Natl Acad Sci USA 93 (1996) 9799-9804
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9799-9804
    • Lütjohann, D.1    Breuer, O.2    Ahlborg, G.3    Nennesmo, I.4    Siden, A.5    Diczfalusy, U.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.