Controlling cholesterol synthesis beyond 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR)

Journal of Biological Chemistry

Volumn 288, Issue 26, 2013, Pages 18707-18715

  Sharpe, Laura J ^a,b   Brown, Andrew J ^a  

^a UNIVERSITY OF NEW SOUTH WALES   (Australia)

^b UNIVERSITY OF SYDNEY   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

BLOOD CHOLESTEROL; CARDIO-VASCULAR DISEASE; CHOLESTEROL SYNTHESIS; REGULATORY MECHANISM; STATINS;

CHOLESTEROL;

ENZYMES;

CHOLESTEROL; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; MICRORNA; STEROL; STEROL REGULATORY ELEMENT BINDING PROTEIN;

ALTERNATIVE RNA SPLICING; CHOLESTEROL SYNTHESIS; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME LOCALIZATION; ENZYME METABOLISM; ENZYME REGULATION; FEEDBACK SYSTEM; GENE EXPRESSION; HUMAN; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN MOTIF; PROTEIN PROCESSING; SHORT SURVEY; TRANSCRIPTION REGULATION; UPREGULATION;

CHOLESTEROL; CHOLESTEROL REGULATION; ER-ASSOCIATED DEGRADATION; NSDHL; POST-TRANSLATIONAL MODIFICATION; SQUALENE MONOOXYGENASE; SREBP; STEROL;

ALTERNATIVE SPLICING; ANIMALS; CHOLESTEROL; ENDOPLASMIC RETICULUM; HUMANS; HYDROXYMETHYLGLUTARYL COA REDUCTASES; PROTEIN ISOFORMS; PROTEIN PROCESSING, POST-TRANSLATIONAL; SQUALENE MONOOXYGENASE; STEROL REGULATORY ELEMENT BINDING PROTEINS;

EID: 84879588228     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R113.479808     Document Type: Short Survey

References (86)

1. Schoenheimer, R., and Breusch, F. (1933) Synthesis and destruction of cholesterol in the organism. J. Biol. Chem. 103, 439-448
2. Bloch, K. (1965) The biological synthesis of cholesterol. Science 150, 19-28
3. Jo, Y., and Debose-Boyd, R. A. (2010) Control of cholesterol synthesis through regulated ER-associated degradation of HMG CoA reductase. Crit. Rev. Biochem. Mol. Biol. 45, 185-198
4. Burg, J. S., and Espenshade, P. J. (2011) Regulation of HMG-CoA reductase in mammals and yeast. Prog. Lipid Res. 50, 403-410
5. Thomas, S., and Fell, D. A. (1998) The role of multiple enzyme activation in metabolic flux control. Adv. Enzyme Regul. 38, 65-85 (Pubitemid 28381384)
6. Nagashima, S., Yagyu, H., Ohashi, K., Tazoe, F., Takahashi, M., Ohshiro, T., Bayasgalan, T., Okada, K., Sekiya, M., Osuga, J., and Ishibashi, S. (2012) Liver-specific deletion of 3-hydroxy-3-methylglutaryl coenzyme A reductase causes hepatic steatosis and death. Arterioscler. Thromb. Vasc. Biol. 32, 1824-1831
7. Porter, F. D., and Herman, G. E. (2011) Malformation syndromes caused by disorders of cholesterol synthesis. J. Lipid Res. 52, 6-34
8. Wang, T. J., Zhang, F., Richards, J. B., Kestenbaum, B., van Meurs, J. B., Berry, D., Kiel, D. P., Streeten, E. A., Ohlsson, C., Koller, D. L., Peltonen, L., Cooper, J. D., O'Reilly, P. F., Houston, D. K., Glazer, N. L., Vandenput, L., Peacock, M., Shi, J., Rivadeneira, F., McCarthy, M. I., Anneli, P., de Boer, I. H., Mangino, M., Kato, B., Smyth, D. J., Booth, S. L., Jacques, P. F., Burke, G. L., Goodarzi, M., Cheung, C. L., Wolf, M., Rice, K., Goltzman, D., Hidiroglou, N., Ladouceur, M., Wareham, N. J., Hocking, L. J., Hart, D., Arden, N. K., Cooper, C., Malik, S., Fraser, W. D., Hartikainen, A. L., Zhai, G., Macdonald, H. M., Forouhi, N. G., Loos, R. J., Reid, D. M., Hakim, A., Dennison, E., Liu, Y., Power, C., Stevens, H. E., Jaana, L., Vasan, R. S., Soranzo, N., Bojunga, J., Psaty, B. M., Lorentzon, M., Foroud, T., Harris, T. B., Hofman, A., Jansson, J. O., Cauley, J. A., Uitterlinden, A. G., Gibson, Q., Jarvelin, M. R., Karasik, D., Siscovick, D. S., Econs, M. J., Kritchevsky, S. B., Florez, J. C., Todd, J. A., Dupuis, J., Hypponen, E., and Spector, T. D. (2010) Common genetic determinants of vitamin D insufficiency: a genomewide association study. Lancet 376, 180-188
9. He, M., Kratz, L. E., Michel, J. J., Vallejo, A. N., Ferris, L., Kelley, R. I., Hoover, J. J., Jukic, D., Gibson, K. M., Wolfe, L. A., Ramachandran, D., Zwick, M. E., and Vockley, J. (2011) Mutations in the human SC4MOL gene encoding a methyl sterol oxidase cause psoriasiform dermatitis, microcephaly, and developmental delay. J. Clin. Invest. 121, 976-984
10. Sukhanova, A., Gorin, A., Serebriiskii, I. G., Gabitova, L., Zheng, H., Restifo, D., Egleston, B. L., Cunningham, D., Bagnyukova, T., Liu, H., Nikonova, A., Adams, G. P., Zhou, Y., Yang, D. H., Mehra, R., Burtness, B., Cai, K. Q., Klein-Szanto, A., Kratz, L. E., Kelley, R. I., Weiner, L. M., Herman, G. E., Golemis, E. A., and Astsaturov, I. (2013) Targeting C4-demethylating genes in the cholesterol pathway sensitizes cancer cells to EGF receptor inhibitors via increased EGF receptor degradation. Cancer Discov. 3, 96-111
11. Song, B. L., Javitt, N. B., and DeBose-Boyd, R. A. (2005) Insig-mediated degradation of HMG-CoA reductase stimulated by lanosterol, an intermediate in the synthesis of cholesterol. Cell Metab. 1, 179-189 (Pubitemid 43960599)
12. Lange, Y., Ory, D. S., Ye, J., Lanier, M. H., Hsu, F. F., and Steck, T. L. (2008) Effectors of rapid homeostatic responses of endoplasmic reticulum cholesterol and 3-hydroxy-3-methylglutaryl-CoA reductase. J. Biol. Chem. 283, 1445-1455
13. Leichner, G. S., Avner, R., Harats, D., and Roitelman, J. (2011) Metabolically regulated endoplasmic reticulum-associated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase. Evidence for requirement of a geranylgeranylated protein. J. Biol. Chem. 286, 32150-32161
14. Zhu, J., Mounzih, K., Chehab, E. F., Mitro, N., Saez, E., and Chehab, F. F. (2010) Effects of FoxO4 overexpression on cholesterol biosynthesis, triacylglycerol accumulation, and glucose uptake. J. Lipid Res. 51, 1312-1324
15. Yang, C., McDonald, J. G., Patel, A., Zhang, Y., Umetani, M., Xu, F., Westover, E. J., Covey, D. F., Mangelsdorf, D. J., Cohen, J. C., and Hobbs, H. H. (2006) Sterol intermediates from cholesterol biosynthetic pathway as liver X receptor ligands. J. Biol. Chem. 281, 27816-27826 (Pubitemid 44414494)
16. Spann, N. J., Garmire, L. X., McDonald, J. G., Myers, D. S., Milne, S. B., Shibata, N., Reichart, D., Fox, J. N., Shaked, I., Heudobler, D., Raetz, C. R., Wang, E. W., Kelly, S. L., Sullards, M. C., Murphy, R. C., Merrill, A. H., Jr., Brown, H. A., Dennis, E. A., Li, A. C., Ley, K., Tsimikas, S., Fahy, E., Subramaniam, S., Quehenberger, O., Russell, D. W., and Glass, C. K. (2012) Regulated accumulation of desmosterol integrates macrophage lipid metabolism and inflammatory responses. Cell 151, 138-152
17. Lehmann, J. M., Kliewer, S. A., Moore, L. B., Smith-Oliver, T. A., Oliver, B. B., Su, J.-L., Sundseth, S. S., Winegar, D. A., Blanchard, D. E., Spencer, T. A., and Willson, T. M. (1997) Activation of the nuclear receptor LXR by oxysterols defines a new hormone response pathway. J. Biol. Chem. 272, 3137-3140 (Pubitemid 27066798)
18. Spencer, T. A., Gayen, A. K., Phirwa, S., Nelson, J. A., Taylor, F. R., Kandutsch, A. A., and Erickson, S. K. (1985) 24(S),25-Epoxycholesterol. Evidence consistent with a role in the regulation of hepatic cholesterogenesis. J. Biol. Chem. 260, 13391-13394 (Pubitemid 16192280)
19. Dang, H., Liu, Y., Pang, W., Li, C., Wang, N., Shyy, J. Y.-J., and Zhu, Y. (2009) Suppression of 2,3-oxidosqualene cyclase by high fat diet contributes to liver X receptor-α-mediated improvement of hepatic lipid profile. J. Biol. Chem. 284, 6218-6226
20. Wong, J., Quinn, C. M., Gelissen, I. C., and Brown, A. J. (2008) Endogenous 24(S),25-epoxycholesterol fine-tunes acute control of cellular cholesterol homeostasis. J. Biol. Chem. 283, 700-707
21. Zerenturk, E. J., Kristiana, I., Gill, S., and Brown, A. J. (2012) The endogenous regulator 24(S),25-epoxycholesterol inhibits cholesterol synthesis at DHCR24 (Seladin-1). Biochim. Biophys. Acta 1821, 1269-1277
22. Horton, J. D., Shah, N. A., Warrington, J. A., Anderson, N. N., Park, S. W., Brown, M. S., and Goldstein, J. L. (2003) Combined analysis of oligonucleotide microarray data from transgenic and knockout mice identifies direct SREBP target genes. Proc. Natl. Acad. Sci. U.S.A. 100, 12027-12032 (Pubitemid 37271509)
23. 14-reductase in human cholesterol biosynthesis. Biochim. Biophys. Acta 1761, 677-685
24. 14-reductase (Tm7sf2) in mice does not impair cholesterol biosynthesis. FEBS J. 275, 5034-5047
25. Seo, Y. K., Jeon, T. I., Chong, H. K., Biesinger, J., Xie, X., and Osborne, T. F. (2011) Genome-wide localization of SREBP-2 in hepatic chromatin predicts a role in autophagy. Cell Metab. 13, 367-375
26. 24-reductase (DHCR24) via dual sterol regulatory elements: cooperative induction of key enzymes in lipid synthesis by sterol regulatory element binding proteins. Biochim. Biophys. Acta 1821, 1350-1360
27. Nagai, M., Sakakibara, J., Nakamura, Y., Gejyo, F., and Ono, T. (2002) SREBP-2 and NF-Y are involved in the transcriptional regulation of squalene epoxidase. Biochem. Biophys. Res. Commun. 295, 74-80 (Pubitemid 34743777)
28. Murphy, C., Ledmyr, H., Ehrenborg, E., and Gåfvels, M. (2006) Promoter analysis of the murine squalene epoxidase gene. Identification of a 205 bp homing region regulated by both SREBP'S and NF-Y. Biochim. Biophys. Acta 1761, 1213-1227 (Pubitemid 44512173)
29. Guan, G., Dai, P. H., Osborne, T. F., Kim, J. B., and Shechter, I. (1997) Multiple sequence elements are involved in the transcriptional regulation of the human squalene synthase gene. J. Biol. Chem. 272, 10295-10302 (Pubitemid 27171712)
30. Inoue, J., Sato, R., and Maeda, M. (1998) MultipleDNAelements for sterol regulatory element-binding protein and NF-Y are responsible for sterol-regulated transcription of the genes for human 3-hydroxy-3-methylglutaryl coenzyme A synthase and squalene synthase. J. Biochem. 123, 1191-1198 (Pubitemid 28306004)
31. Magaña, M. M., and Osborne, T. F. (1996) Two tandem binding sites for sterol regulatory element binding proteins are required for sterol regulation of fatty-acid synthase promoter. J. Biol. Chem. 271, 32689-32694
32. Wang, Y., Rogers, P. M., Su, C., Varga, G., Stayrook, K. R., and Burris, T. P. (2008) Regulation of cholesterologenesis by the oxysterol receptor, LXRα. J. Biol. Chem. 283, 26332-26339
33. Wang, Y., Rogers, P. M., Stayrook, K. R., Su, C., Varga, G., Shen, Q., Nagpal, S., and Burris, T. P. (2008) The selective Alzheimer's disease indicator-1 gene (Seladin-1/DHCR24) is a liver X receptor target gene. Mol. Pharmacol. 74, 1716-1721
34. Repa, J. J., Li, H., Frank-Cannon, T. C., Valasek, M. A., Turley, S. D., Tansey, M. G., and Dietschy, J. M. (2007) Liver X receptor activation enhances cholesterol loss from the brain, decreases neuroinflammation, and increases survival of the NPC1 mouse. J. Neurosci. 27, 14470-14480
35. Krycer, J. R., and Brown, A. J. (2011) Cross-talk between the androgen receptor and the liver X receptor. Implications for cholesterol homeostasis. J. Biol. Chem. 286, 20637-20647
36. Luu, W., Sharpe, L. J., Stevenson, J., and Brown, A. J. (2012) Akt acutely activates the cholesterogenic transcription factor SREBP-2. Biochim. Biophys. Acta 1823, 458-464
37. Fernández-Hernando, C., Ramírez, C. M., Goedeke, L., and Suárez, Y. (2013) MicroRNAs in metabolic disease. Arterioscl. Thromb. Vasc. Biol. 33, 178-185
38. Krützfeldt, J., Rajewsky, N., Braich, R., Rajeev, K. G., Tuschl, T., Manoharan, M., and Stoffel, M. (2005) Silencing of microRNAs in vivo with 'antagomirs.' Nature 438, 685-689
39. Esau, C., Davis, S., Murray, S. F., Yu, X. X., Pandey, S. K., Pear, M., Watts, L., Booten, S. L., Graham, M., McKay, R., Subramaniam, A., Propp, S., Lollo, B. A., Freier, S., Bennett, C. F., Bhanot, S., and Monia, B. P. (2006) miR-122 regulation of lipid metabolism revealed by in vivo antisense targeting. Cell Metab. 3, 87-98
40. Medina, M. W., and Krauss, R. M. (2013) Alternative splicing in the regulation of cholesterol homeostasis. Curr. Opin. Lipid. 24, 147-152
41. Medina, M. W., Gao, F., Naidoo, D., Rudel, L. L., Temel, R. E., McDaniel, A. L., Marshall, S. M., and Krauss, R. M. (2011) Coordinately regulated alternative splicing of genes involved in cholesterol biosynthesis and uptake. PLoS ONE 6, e19420
42. de la Grange, P., Dutertre, M., Correa, M., and Auboeuf, D. (2007) A new advance in alternative splicing databases: from catalogue to detailed analysis of regulation of expression and function of human alternative splicing variants. BMC Bioinformatics 8, 180
43. Roitelman, J., and Simoni, R. D. (1992) Distinct sterol and nonsterol signals for the regulated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase. J. Biol. Chem. 267, 25264-25273
44. Nguyen, A. D., McDonald, J. G., Bruick, R. K., and DeBose-Boyd, R. A. (2007) Hypoxia stimulates degradation of 3-hydroxy-3-methylglutarylcoenzyme A reductase through accumulation of lanosterol and hypoxia-inducible factor-mediated induction of insigs. J. Biol. Chem. 282, 27436-27446 (Pubitemid 47501948)
45. Gonzalez, R., Carlson, J. P., and Dempsey, M. E. (1979) Two major regulatory steps in cholesterol synthesis by human renal cancer cells. Arch. Biochem. Biophys. 196, 574-580 (Pubitemid 10230169)
46. Hidaka, Y., Satoh, T., and Kamei, T. (1990) Regulation of squalene epoxidase in HepG2 cells. J. Lipid Res. 31, 2087-2094
47. Gill, S., Stevenson, J., Kristiana, I., and Brown, A. J. (2011) Cholesterol-dependent degradation of squalene monooxygenase, a control point in cholesterol synthesis beyond HMG-CoA reductase. Cell Metab. 13, 260-273
48. Hulce, J. J., Cognetta, A. B., Niphakis, M. J., Tully, S. E., and Cravatt, B. F. (2013) Proteome-wide mapping of cholesterol-interacting proteins in mammalian cells. Nat. Methods 10, 259-264
49. Kristiana, I., Luu, W., Stevenson, J., Cartland, S., Jessup, W., Belani, J. D., Rychnovsky, S. D., and Brown, A. J. (2012) Cholesterol through the looking glass. Ability of its enantiomer also to elicit homeostatic responses. J. Biol. Chem. 287, 33897-33904
50. Clarke, P. R., and Hardie, D. G. (1990) Regulation of HMG-CoA reductase: identification of the site phosphorylated by the AMP-activated protein kinase in vitro and in intact rat liver. EMBO J. 9, 2439-2446
51. Sever, N., Song, B. L., Yabe, D., Goldstein, J. L., Brown, M. S., and DeBose- Boyd, R. A. (2003) Insig-dependent ubiquitination and degradation of mammalian 3-hydroxy-3-methylglutaryl-CoA reductase stimulated by sterols and geranylgeraniol. J. Biol. Chem. 278, 52479-52490 (Pubitemid 38035841)
52. Takano, M., Koyama, Y., Ito, H., Hoshino, S., Onogi, H., Hagiwara, M., Furukawa, K., and Horigome, T. (2004) Regulation of binding of lamin B receptor to chromatin by SR protein kinase and Cdc2 kinase in Xenopus egg extracts. J. Biol. Chem. 279, 13265-13271 (Pubitemid 38445906)
53. Hornbeck, P. V., Kornhauser, J. M., Tkachev, S., Zhang, B., Skrzypek, E., Murray, B., Latham, V., and Sullivan, M. (2012) PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res. 40, D261-D270
54. 24-reductase in mammalian cells. Biochem. J. 366, 109-119
55. Metherall, J. E., Waugh, K., and Li, H. (1996) Progesterone inhibits cholesterol biosynthesis in cultured cells. Accumulation of cholesterol precursors. J. Biol. Chem. 271, 2627-2633
56. Jansen, M., Wang, W., Greco, D., Bellenchi, G. C., di Porzio, U., Brown, A. J., and Ikonen, E. (2013) What dictates the accumulation of desmosterol in the developing brain? FASEB J. 27, 865-870
57. Shimomura, I., Shimano, H., Korn, B. S., Bashmakov, Y., and Horton, J. D. (1998) Nuclear sterol regulatory element-binding proteins activate genes responsible for the entire program of unsaturated fatty acid biosynthesis in transgenic mouse liver. J. Biol. Chem. 273, 35299-35306 (Pubitemid 29028238)
58. Ferguson, J. B., and Bloch, K. (1977) Purification and properties of a soluble protein activator of rat liver squalene epoxidase. J. Biol. Chem. 252, 5381-5385 (Pubitemid 8168413)
59. Ishibashi, T. (2002) Supernatant protein relevant to the activity of membrane-bound enzymes: studies on lathosterol 5-desaturase. Biochem. Biophys. Res. Commun. 292, 1293-1298
60. Mokashi, V., Singh, D. K., and Porter, T. D. (2005) Supernatant protein factor stimulates HMG-CoA reductase in cell culture and in vitro. Arch. Biochem. Biophys. 433, 474-480 (Pubitemid 39592802)
61. Taramino, S., Teske, B., Oliaro-Bosso, S., Bard, M., and Balliano, G. (2010) Divergent interactions involving the oxidosqualene cyclase and the steroid- 3-ketoreductase in the sterol biosynthetic pathway of mammals and yeasts. Biochim. Biophys. Acta 1801, 1232-1237
62. Wu, C., Miloslavskaya, I., Demontis, S., Maestro, R., and Galaktionov, K. (2004) Regulation of cellular response to oncogenic and oxidative stress by Seladin-1. Nature 432, 640-645 (Pubitemid 39626272)
63. Hartman, I. Z., Liu, P., Zehmer, J. K., Luby-Phelps, K., Jo, Y., Anderson, R. G., and DeBose-Boyd, R. A. (2010) Sterol-induced dislocation of 3-hydroxy-3-methylglutaryl coenzyme A reductase from endoplasmic reticulum membranes into the cytosol through a subcellular compartment resembling lipid droplets. J. Biol. Chem. 285, 19288-19298
64. Ohashi, M., Mizushima, N., Kabeya, Y., and Yoshimori, T. (2003) Localization of mammalian NAD(P)H steroid dehydrogenase-like protein on lipid droplets. J. Biol. Chem. 278, 36819-36829 (Pubitemid 37140016)
65. Wan, H. C., Melo, R. C., Jin, Z., Dvorak, A. M., and Weller, P. F. (2007) Roles and origins of leukocyte lipid bodies: proteomic and ultrastructural studies. FASEB J. 21, 167-178 (Pubitemid 46061356)
66. Ta, M. T., Kapterian, T. S., Fei, W., Du, X., Brown, A. J., Dawes, I. W., and Yang, H. (2012) Accumulation of squalene is associated with the clustering of lipid droplets. FEBS J. 279, 4231-4244
67. Xue, T., Zhang, Y., Zhang, L., Yao, L., Hu, X., and Xu, L. X. (2013) Proteomic analysis of two metabolic proteins with potential to translocate to plasma membrane associated with tumor metastasis development and drug targets. J. Proteome Res. 12, 1754-1763
68. Leber, R., Landl, K., Zinser, E., Ahorn, H., Spök, A., Kohlwein, S. D., Turnowsky, F., and Daum, G. (1998) Dual localization of squalene epoxidase, Erg1p, in yeast reflects a relationship between the endoplasmic reticulum and lipid particles. Mol. Biol. Cell 9, 375-386 (Pubitemid 28084132)
69. Lim, L., Jackson-Lewis, V., Wong, L. C., Shui, G. H., Goh, A. X., Kesavapany, S., Jenner, A. M., Fivaz, M., Przedborski, S., and Wenk, M. R. (2012) Lanosterol induces mitochondrial uncoupling and protects dopaminergic neurons from cell death in a model for Parkinson's disease. Cell Death Differ. 19, 416-427
70. Lange, Y., Echevarria, F., and Steck, T. L. (1991) Movement of zymosterol, a precursor of cholesterol, among three membranes in human fibroblasts. J. Biol. Chem. 266, 21439-21443 (Pubitemid 121000204)
71. Lusa, S., Heino, S., and Ikonen, E. (2003) Differential mobilization of newly synthesized cholesterol and biosynthetic sterol precursors from cells. J. Biol. Chem. 278, 19844-19851 (Pubitemid 36799172)
72. McDonald, J. G., Smith, D. D., Stiles, A. R., and Russell, D. W. (2012) A comprehensive method for extraction and quantitative analysis of sterols and secosteroids from human plasma. J. Biol. Chem. 53, 1399-1409
73. Porter, J. R., Burg, J. S., Espenshade, P. J., and Iglesias, P. A. (2012) Identifying a static nonlinear structure in a biological system using noisy, sparse data. J. Theor. Biol. 300, 232-241
74. Belič, A., Pompon, D., Monostory, K., Kelly, D., Kelly, S., and Rozman, D. (2013) An algorithm for rapid computational construction of metabolic networks: a cholesterol biosynthesis example. Comput. Biol. Med. 43, 471-480
75. Mazein, A., Watterson, S., Hsieh, W. Y., Griffiths, W. J., and Ghazal, P. (2013) A comprehensive machine-readable view of the mammalian cholesterol biosynthesis pathway. Biochem. Pharmacol. 10.1016/j.bcp. 2013.03.021
76. Li, J. J. (2009) Triumph of the Heart: The Story of Statins, Oxford University Press, New York
77. Gelissen, I. C., and Brown, A. J. (2011) Drug targets beyond HMG-CoA reductase: why venture beyond the statins? Front. Biol. 6, 197-205
78. Zhang, D. W., Lagace, T. A., Garuti, R., Zhao, Z., McDonald, M., Horton, J. D., Cohen, J. C., and Hobbs, H. H. (2007) Binding of proprotein convertase subtilisin/kexin type 9 to epidermal growth factor-like repeat A of low density lipoprotein receptor decreases receptor recycling and increases degradation. J. Biol. Chem. 282, 18602-18612 (Pubitemid 47100234)
79. Vallett, S. M., Sanchez, H. B., Rosenfeld, J. M., and Osborne, T. F. (1996) A direct role for sterol regulatory element binding protein in activation of 3-hydroxy-3-methylglutaryl coenzyme A reductase gene. J. Biol. Chem. 271, 12247-12253 (Pubitemid 26160886)
80. Ishimoto, K., Tachibana, K., Hanano, I., Yamasaki, D., Nakamura, H., Kawai, M., Urano, Y., Tanaka, T., Hamakubo, T., Sakai, J., Kodama, T., and Doi, T. (2010) Sterol-regulatory-element-binding protein 2 and nuclear factor Y control human farnesyl diphosphate synthase expression and affect cell proliferation in hepatoblastoma cells. Biochem. J. 429, 347-357
81. Rozman, D., Fink, M., Fimia, G. M., Sassone-Corsi, P., and Waterman, M. R. (1999) Cyclic adenosine 3′,5′-monophosphate (cAMP)/cAMP- responsive element modulator (CREM)-dependent regulation of cholesterogenic lanosterol 14α-demethylase (CYP51) in spermatids. Mol. Endocrinol. 13, 1951-1962 (Pubitemid 30645267)
82. Schiavoni, G., Bennati, A. M., Castelli, M., Fazia, M. A., Beccari, T., Servillo, G., and Roberti, R. (2010) Activation of TM7SF2 promoter by SREBP-2 depends on a new sterol regulatory element, a GC-box, and an inverted CCAAT-box. Biochim. Biophys. Acta 1801, 587-592
83. Ohnesorg, T., and Adamski, J. (2005) Promoter analyses of human and mouse 17β-hydroxysteroid dehydrogenase type 7. J. Steroid Biochem. Mol. Biol. 94, 259-261 (Pubitemid 40614539)
84. Misawa, K., Horiba, T., Arimura, N., Hirano, Y., Inoue, J., Emoto, N., Shimano, H., Shimizu, M., and Sato, R. (2003) Sterol regulatory elementbinding protein-2 interacts with hepatocyte nuclear factor-4 to enhance sterol isomerase gene expression in hepatocytes. J. Biol. Chem. 278, 36176-36182 (Pubitemid 37139940)
85. Kim, J. H., Lee, J. N., and Paik, Y. K. (2001) Cholesterol biosynthesis from lanosterol. A concerted role for Sp1 and NF-Y-binding sites for sterolmediated regulation of rat 7-dehydrocholesterol reductase gene expression. J. Biol. Chem. 276, 18153-18160
86. Sakakura, Y., Shimano, H., Sone, H., Takahashi, A., Inoue, N., Toyoshima, H., Suzuki, S., and Yamada, N. (2001) Sterol regulatory element-binding proteins induce an entire pathway of cholesterol synthesis. Biochem. Biophys. Res. Commun. 286, 176-183 (Pubitemid 32917666)