메뉴 건너뛰기




Volumn 55, Issue 3, 2014, Pages 431-442

FoxO4 interacts with the sterol regulatory factor SREBP2 and the hypoxia inducible factor HIF2α at the CYP51 promoter

Author keywords

Cholesterol; Dihydrolanosterol; Forkhead transcription factor 4; Hypoxia inducible factor 2 ; Lanosterol 14 demethylase; Sterol regulatory element binding protein 2

Indexed keywords

DIHYDROLANOSTEROL; FORKHEAD TRANSCRIPTION FACTOR 4; HYPOXIA INDUCIBLE FACTOR 2ALPHA; LANOSTEROL; RECOMBINANT PROTEIN; STEROL 14ALPHA DEMETHYLASE; STEROL REGULATORY ELEMENT BINDING PROTEIN 2; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

EID: 84894718404     PISSN: 00222275     EISSN: 15397262     Source Type: Journal    
DOI: 10.1194/jlr.M043521     Document Type: Article
Times cited : (12)

References (38)
  • 1
    • 0029974620 scopus 로고    scopus 로고
    • The ubiquitously expressed human CYP51 encodes lanosterol 14 alphademethylase, a cytochrome P450 whose expression is regulated by oxysterols
    • Strömstedt, M., D. Rozman, and M. R. Waterman. 1996. The ubiquitously expressed human CYP51 encodes lanosterol 14 alphademethylase, a cytochrome P450 whose expression is regulated by oxysterols. Arch. Biochem. Biophys. 329: 73-81.
    • (1996) Arch. Biochem. Biophys. , vol.329 , pp. 73-81
    • Strömstedt, M.1    Rozman, D.2    Waterman, M.R.3
  • 2
    • 18544378347 scopus 로고    scopus 로고
    • Insigmediated degradation of HMG CoA reductase stimulated by lanosterol, an intermediate in the synthesis of cholesterol
    • Song, B. L., N. B. Javitt, and R. A. DeBose-Boyd. 2005. Insigmediated degradation of HMG CoA reductase stimulated by lanosterol, an intermediate in the synthesis of cholesterol. Cell Metab. 1: 179-189.
    • (2005) Cell Metab. , vol.1 , pp. 179-189
    • Song, B.L.1    Javitt, N.B.2    DeBose-Boyd, R.A.3
  • 3
    • 77952691826 scopus 로고    scopus 로고
    • Effects of FoxO4 overexpression on cholesterol biosynthesis, triacylglycerol accumulation, and glucose uptake
    • Zhu, J., K. Mounzih, E. F. Chehab, N. Mitro, E. Saez, and F. F. Chehab. 2010. Effects of FoxO4 overexpression on cholesterol biosynthesis, triacylglycerol accumulation, and glucose uptake. J. Lipid Res. 51: 1312-1324.
    • (2010) J. Lipid Res. , vol.51 , pp. 1312-1324
    • Zhu, J.1    Mounzih, K.2    Chehab, E.F.3    Mitro, N.4    Saez, E.5    Chehab, F.F.6
  • 4
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E. G., and W. J. Dyer. 1959. A rapid method of total lipid extraction and purification. Can. J. Biochem. Physiol. 37: 911-917.
    • (1959) Can. J. Biochem. Physiol. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 5
    • 0036528246 scopus 로고    scopus 로고
    • Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein
    • DOI 10.1016/S1535-6108(02)00043-0
    • Kondo, K., J. Klco, E. Nakamura, M. Lechpammer, and W. G. Kaelin, Jr. 2002. Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein. Cancer Cell. 1: 237-246. (Pubitemid 41039148)
    • (2002) Cancer Cell , vol.1 , Issue.3 , pp. 237-246
    • Kondo, K.1    Klco, J.2    Nakamura, E.3    Lechpammer, M.4    Kaelin Jr., W.G.5
  • 6
    • 33947250323 scopus 로고    scopus 로고
    • The hypoxia-inducible factor 2alpha N-terminal and C-terminal transactivation domains cooperate to promote renal tumorigenesis in vivo
    • DOI 10.1128/MCB.01514-06
    • Yan, Q., S. Bartz, M. Mao, L. Li, and W. G. Kaelin, Jr. 2007. The hypoxia-inducible factor 2alpha N-terminal and C-terminal transactivation domains cooperate to promote renal tumorigenesis in vivo. Mol. Cell. Biol. 27: 2092-2102. (Pubitemid 46418467)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.6 , pp. 2092-2102
    • Yan, Q.1    Bartz, S.2    Mao, M.3    Li, A.4    Kaelin Jr., W.G.5
  • 7
    • 0030010388 scopus 로고    scopus 로고
    • Correction of the sterility defect in homozygous obese female mice by treatment with the human recombinant leptin
    • DOI 10.1038/ng0396-318
    • Chehab, F. F., M. E. Lim, and R. Lu. 1996. Correction of the sterility defect in homozygous obese female mice by treatment with the human recombinant leptin. Nat. Genet. 12: 318-320. (Pubitemid 26080094)
    • (1996) Nature Genetics , vol.12 , Issue.3 , pp. 318-320
    • Chehab, F.F.1    Lim, M.E.2    Lu, R.3
  • 8
    • 5044229684 scopus 로고    scopus 로고
    • Differential vulnerability of immature murine neurons to oxygen-glucose deprivation
    • DOI 10.1016/j.expneurol.2004.07.010, PII S0014488604002961
    • Jiang, X., D. Mu, C. Manabat, A. A. Koshy, S. Christen, M. G. Tauber, Z. S. Vexler, and D. M. Ferriero. 2004. Differential vulnerability of immature murine neurons to oxygen-glucose deprivation. Exp. Neurol. 190: 224-232. (Pubitemid 39335721)
    • (2004) Experimental Neurology , vol.190 , Issue.1 , pp. 224-232
    • Jiang, X.1    Mu, D.2    Manabat, C.3    Koshy, A.A.4    Christen, S.5    Tauber, M.G.6    Vexler, Z.S.7    Ferriero, D.M.8
  • 9
    • 0036020505 scopus 로고    scopus 로고
    • A cAMP-responsive element binding site is essential for sterol regulation of the human lanosterol 14alpha-demethylase gene (CYP51)
    • DOI 10.1210/me.2001-0262
    • Halder, S. K., M. Fink, M. R. Waterman, and D. Rozman. 2002. A cAMP-responsive element binding site is essential for sterol regulation of the human lanosterol 14alpha-demethylase gene (CYP51). Mol. Endocrinol. 16: 1853-1863. (Pubitemid 34828092)
    • (2002) Molecular Endocrinology , vol.16 , Issue.8 , pp. 1853-1863
    • Halder, S.K.1    Fink, M.2    Waterman, M.R.3    Rozman, D.4
  • 10
    • 0033304572 scopus 로고    scopus 로고
    • Cyclic adenosine 3',5'- Monophosphate(cAMP)/cAMP-responsive element modulator (CREM)-dependent regulation of cholesterogenic lanosterol 14alpha-demethylase (CYP51) in spermatids
    • Rozman, D., M. Fink, G. M. Fimia, P. Sassone-Corsi, and M. R. Waterman. 1999. Cyclic adenosine 3′,5′-monophosphate(cAMP)/cAMP-responsive element modulator (CREM)-dependent regulation of cholesterogenic lanosterol 14alpha-demethylase (CYP51) in spermatids. Mol. Endocrinol. 13: 1951-1962. (Pubitemid 30645267)
    • (1999) Molecular Endocrinology , vol.13 , Issue.11 , pp. 1951-1962
    • Rozman, D.1    Fink, M.2    Fimia, G.M.3    Sassone-Corsi, P.4    Waterman, M.R.5
  • 11
    • 0034234693 scopus 로고    scopus 로고
    • Characterization of the mouse lanosterol 14alpha-demethylase (CYP51), a new member of the evolutionarily most conserved cytochrome P450 family
    • DOI 10.1006/abbi.2000.1859
    • Debeljak, N., S. Horvat, K. Vouk, M. Lee, and D. Rozman. 2000. Characterization of the mouse lanosterol 14alpha-demethylase (CYP51), a new member of the evolutionarily most conserved cytochrome P450 family. Arch. Biochem. Biophys. 379: 37-45. (Pubitemid 30432218)
    • (2000) Archives of Biochemistry and Biophysics , vol.379 , Issue.1 , pp. 37-45
    • Debeljak, N.1    Horvat, S.2    Vouk, K.3    Lee, M.4    Rozman, D.5
  • 12
    • 84879588228 scopus 로고    scopus 로고
    • Controlling cholesterol synthesis beyond 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR)
    • Sharpe, L. J., and A. J. Brown. 2013. Controlling cholesterol synthesis beyond 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR). J. Biol. Chem. 288: 18707-18715.
    • (2013) J. Biol. Chem. , vol.288 , pp. 18707-18715
    • Sharpe, L.J.1    Brown, A.J.2
  • 13
    • 79953756678 scopus 로고    scopus 로고
    • Genome-wide localization of SREBP-2 in hepatic chromatin predicts a role in autophagy
    • Seo, Y. K., T. I. Jeon, H. K. Chong, J. Biesinger, X. Xie, and T. F. Osborne. 2011. Genome-wide localization of SREBP-2 in hepatic chromatin predicts a role in autophagy. Cell Metab. 13: 367-375.
    • (2011) Cell Metab. , vol.13 , pp. 367-375
    • Seo, Y.K.1    Jeon, T.I.2    Chong, H.K.3    Biesinger, J.4    Xie, X.5    Osborne, T.F.6
  • 14
    • 1942533543 scopus 로고    scopus 로고
    • Aryl Hydrocarbon Nuclear Translocator (ARNT) Promotes Oxygen-independent Stabilization of Hypoxia-inducible Factor-1alpha by Modulating an Hsp90-dependent Regulatory Pathway
    • DOI 10.1074/jbc.M313342200
    • Isaacs, J. S., Y. J. Jung, and L. Neckers. 2004. Aryl hydrocarbon nuclear translocator (ARNT) promotes oxygen-independent stabilization of hypoxia-inducible factor-1alpha by modulating an Hsp90-dependent regulatory pathway. J. Biol. Chem. 279: 16128-16135. (Pubitemid 38509304)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.16 , pp. 16128-16135
    • Isaacs, J.S.1    Jung, Y.-J.2    Neckers, L.3
  • 16
    • 85047682984 scopus 로고    scopus 로고
    • Regulation of oxygen homeostasis by hypoxia-inducible factor 1
    • Semenza, G. L. 2009. Regulation of oxygen homeostasis by hypoxia-inducible factor 1. Physiology (Bethesda). 24: 97-106.
    • (2009) Physiology (Bethesda) , vol.24 , pp. 97-106
    • Semenza, G.L.1
  • 17
    • 0346101770 scopus 로고    scopus 로고
    • Insig-dependent Ubiquitination and Degradation of Mammalian 3-Hydroxy-3-methylglutaryl-CoA Reductase Stimulated by Sterols and Geranylgeraniol
    • DOI 10.1074/jbc.M310053200
    • Sever, N., B. L. Song, D. Yabe, J. L. Goldstein, M. S. Brown, and R. A. DeBose-Boyd. 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)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.52 , pp. 52479-52490
    • Sever, N.1    Song, B.-L.2    Yabe, D.3    Goldstein, J.L.4    Brown, M.S.5    DeBose-Boydb, R.A.6
  • 18
    • 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
    • DOI 10.1074/jbc.M704976200
    • Nguyen, A. D., J. G. McDonald, R. K. Bruick, and R. A. DeBose-Boyd. 2007. Hypoxia stimulates degradation of 3-hydroxy-3-methyl-glutaryl-coenzyme A reductase through accumulation of lanosterol and hypoxia-inducible factor-mediated induction of insigs. J. Biol. Chem. 282: 27436-27446. (Pubitemid 47501948)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.37 , pp. 27436-27446
    • Nguyen, A.D.1    McDonald, J.G.2    Bruick, R.K.3    DeBose-Boyd, R.A.4
  • 19
    • 0034006016 scopus 로고    scopus 로고
    • HIF-1: Mediator of physiological and pathophysiological responses to hypoxia
    • Semenza, G. L. 2000. HIF-1: mediator of physiological and pathophysiological responses to hypoxia. J. Appl. Physiol. 88: 1474-1480. (Pubitemid 30217451)
    • (2000) Journal of Applied Physiology , vol.88 , Issue.4 , pp. 1474-1480
    • Semenza, G.L.1
  • 20
    • 67650531089 scopus 로고    scopus 로고
    • Genome-wide association of hypoxia-inducible factor (HIF)-1alpha and HIF-2alpha DNA binding with expression profiling of hypoxia-inducible transcripts
    • Mole, D. R., C. Blancher, R. R. Copley, P. J. Pollard, J. M. Gleadle, J. Ragoussis, and P. J. Ratcliffe. 2009. Genome-wide association of hypoxia-inducible factor (HIF)-1alpha and HIF-2alpha DNA binding with expression profiling of hypoxia-inducible transcripts. J. Biol. Chem. 284: 16767-16775.
    • (2009) J. Biol. Chem. , vol.284 , pp. 16767-16775
    • Mole, D.R.1    Blancher, C.2    Copley, R.R.3    Pollard, P.J.4    Gleadle, J.M.5    Ragoussis, J.6    Ratcliffe, P.J.7
  • 22
    • 0345491599 scopus 로고    scopus 로고
    • Differential Roles of Hypoxia-Inducible Factor 1alpha (HIF-1alpha) and HIF-2alpha in Hypoxic Gene Regulation
    • DOI 10.1128/MCB.23.24.9361-9374.2003
    • Hu, C. J., L. Y. Wang, L. A. Chodosh, B. Keith, and M. C. Simon. 2003. Differential roles of hypoxia-inducible factor 1alpha (HIF-1alpha) and HIF-2alpha in hypoxic gene regulation. Mol. Cell. Biol. 23: 9361-9374. (Pubitemid 37499822)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.24 , pp. 9361-9374
    • Hu, C.-J.1    Wang, L.-Y.2    Chodosh, L.A.3    Keith, B.4    Simon, M.C.5
  • 23
    • 78349272461 scopus 로고    scopus 로고
    • HIF-1 and HIF-2 transcription factors-similar but not identical
    • Loboda, A., A. Jozkowicz, and J. Dulak. 2010. HIF-1 and HIF-2 transcription factors-similar but not identical. Mol. Cells. 29: 435-442.
    • (2010) Mol. Cells. , vol.29 , pp. 435-442
    • Loboda, A.1    Jozkowicz, A.2    Dulak, J.3
  • 24
    • 35848938945 scopus 로고    scopus 로고
    • The N-terminal transactivation domain confers target gene specificity of hypoxia-inducible factors HIF-1alpha and HIF-2alpha
    • DOI 10.1091/mbc.E06-05-0419
    • Hu, C. J., A. Sataur, L. Wang, H. Chen, and M. C. Simon. 2007. The N-terminal transactivation domain confers target gene specificity of hypoxia-inducible factors HIF-1alpha and HIF-2alpha. Mol. Biol. Cell. 18: 4528-4542. (Pubitemid 350060179)
    • (2007) Molecular Biology of the Cell , vol.18 , Issue.11 , pp. 4528-4542
    • Hu, C.-J.1    Sataur, A.2    Wang, L.3    Chen, H.4    Simon, M.C.5
  • 25
    • 66749129781 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor 2alpha signaling by the stress-responsive deacetylase sirtuin 1
    • Dioum, E. M., R. Chen, M. S. Alexander, Q. Zhang, R. T. Hogg, R. D. Gerard, and J. A. Garcia. 2009. Regulation of hypoxia-inducible factor 2alpha signaling by the stress-responsive deacetylase sirtuin 1. Science. 324: 1289-1293.
    • (2009) Science. , vol.324 , pp. 1289-1293
    • Dioum, E.M.1    Chen, R.2    Alexander, M.S.3    Zhang, Q.4    Hogg, R.T.5    Gerard, R.D.6    Garcia, J.A.7
  • 28
    • 37249040886 scopus 로고    scopus 로고
    • Histone deacetylase 3 down-regulates cholesterol synthesis through repression of lanosterol synthase gene expression
    • DOI 10.1074/jbc.M701719200
    • Villagra, A., N. Ulloa, X. Zhang, Z. Yuan, E. Sotomayor, and E. Seto. 2007. Histone deacetylase 3 down-regulates cholesterol synthesis through repression of lanosterol synthase gene expression. J. Biol. Chem. 282: 35457-35470. (Pubitemid 350277091)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.49 , pp. 35457-35470
    • Villagra, A.1    Ulloa, N.2    Zhang, X.3    Yuan, Z.4    Sotomayor, E.5    Seto, E.6
  • 29
    • 84884134120 scopus 로고    scopus 로고
    • Hepatic SREBP-2 and cholesterol biosynthesis are regulated by FoxO3 and Sirt6
    • Tao, R., X. Xiong, R. A. DePinho, C. X. Deng, and X. C. Dong. 2013. Hepatic SREBP-2 and cholesterol biosynthesis are regulated by FoxO3 and Sirt6. J. Lipid Res. 54: 2745-2753.
    • (2013) J. Lipid Res. , vol.54 , pp. 2745-2753
    • Tao, R.1    Xiong, X.2    DePinho, R.A.3    Deng, C.X.4    Dong, X.C.5
  • 30
    • 84860215808 scopus 로고    scopus 로고
    • Circadian expression of steroidogenic cytochromes P450 in the mouse adrenal gland-involvement of cAMP-responsive element modulator in epigenetic regulation of Cyp17a1
    • Kosir, R., U. P. Zmrzljak, T. Bele, J. Acimovic, M. Perse, G. Majdic, C. Prehn, J. Adamski, and D. Rozman. 2012. Circadian expression of steroidogenic cytochromes P450 in the mouse adrenal gland-involvement of cAMP-responsive element modulator in epigenetic regulation of Cyp17a1. FEBS J. 279: 1584-1593.
    • (2012) FEBS J. , vol.279 , pp. 1584-1593
    • Kosir, R.1    Zmrzljak, U.P.2    Bele, T.3    Acimovic, J.4    Perse, M.5    Majdic, G.6    Prehn, C.7    Adamski, J.8    Rozman, D.9
  • 32
    • 41849086320 scopus 로고    scopus 로고
    • FOXO-binding partners: It takes two to tango
    • van der Vos, K. E., and P. J. Coffer. 2008. FOXO-binding partners: it takes two to tango. Oncogene. 27: 2289-2299.
    • (2008) Oncogene. , vol.27 , pp. 2289-2299
    • Van Der Vos, K.E.1    Coffer, P.J.2
  • 33
    • 22944451474 scopus 로고    scopus 로고
    • Phenotypic modulation of smooth muscle cells through interaction of Foxo4 and Myocardin
    • DOI 10.1016/j.devcel.2005.05.017, PII S1534580705002133
    • Liu, Z. P., Z. Wang, H. Yanagisawa, and E. N. Olson. 2005. Phenotypic modulation of smooth muscle cells through interaction of Foxo4 and myocardin. Dev. Cell. 9: 261-270. (Pubitemid 41051744)
    • (2005) Developmental Cell , vol.9 , Issue.2 , pp. 261-270
    • Liu, Z.-P.1    Wang, Z.2    Yanagisawa, H.3    Olson, E.N.4
  • 34
    • 1642332084 scopus 로고    scopus 로고
    • Integration of smad and forkhead pathways in the control of neuroepithelial and glioblastoma cell proliferation
    • DOI 10.1016/S0092-8674(04)00298-3, PII S0092867404002983
    • Seoane, J., H. V. Le, L. Shen, S. A. Anderson, and J. Massague. 2004. Integration of Smad and forkhead pathways in the control of neuroepithelial and glioblastoma cell proliferation. Cell. 117: 211-223. (Pubitemid 38496241)
    • (2004) Cell , vol.117 , Issue.2 , pp. 211-223
    • Seoane, J.1    Le, H.-V.2    Shen, L.3    Anderson, S.A.4    Massague, J.5
  • 35
    • 0037216526 scopus 로고    scopus 로고
    • AKT-independent protection of prostate cancer cells from apoptosis mediated through complex formation between the androgen receptor and FKHR
    • DOI 10.1128/MCB.23.1.104-118.2003
    • Li, P., H. Lee, S. Guo, T. G. Unterman, G. Jenster, and W. Bai. 2003. AKT-independent protection of prostate cancer cells from apoptosis mediated through complex formation between the androgen receptor and FKHR. Mol. Cell. Biol. 23: 104-118. (Pubitemid 36008505)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.1 , pp. 104-118
    • Li, P.1    Lee, H.2    Guo, S.3    Unterman, T.G.4    Jenster, G.5    Bail, W.6
  • 36
    • 34147101043 scopus 로고    scopus 로고
    • Insulin-like growth factor 1/insulin signaling activates androgen signaling through direct interactions of Foxo1 with androgen receptor
    • DOI 10.1074/jbc.M610447200
    • Fan, W., T. Yanase, H. Morinaga, T. Okabe, M. Nomura, H. Daitoku, A. Fukamizu, S. Kato, R. Takayanagi, and H. Nawata. 2007. Insulin-like growth factor 1/insulin signaling activates androgen signaling through direct interactions of Foxo1 with androgen receptor. J. Biol. Chem. 282: 7329-7338. (Pubitemid 47093686)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.10 , pp. 7329-7338
    • Fan, W.1    Yanase, T.2    Morinaga, H.3    Okabe, T.4    Nomura, M.5    Daitoku, H.6    Fukamizu, A.7    Kato, S.8    Takayanagi, R.9    Nawata, H.10
  • 37
    • 0035823576 scopus 로고    scopus 로고
    • Ligand-dependent interaction of estrogen receptor-alpha with members of the forkhead transcription factor family
    • Schuur, E. R., A. V. Loktev, M. Sharma, Z. Sun, R. A. Roth, and R. J. Weigel. 2001. Ligand-dependent interaction of estrogen receptor-alpha with members of the forkhead transcription factor family. J. Biol. Chem. 276: 33554-33560.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33554-33560
    • Schuur, E.R.1    Loktev, A.V.2    Sharma, M.3    Sun, Z.4    Roth, R.A.5    Weigel, R.J.6
  • 38
    • 34347384383 scopus 로고    scopus 로고
    • Constitutively ctive FOXO1a and a DNA-binding domain mutant exhibit distinct co-regulatory functions to enhance progesterone receptor A activity
    • DOI 10.1677/JME-07-0017
    • Rudd, M. D., I. Gonzalez-Robayna, I. Hernandez-Gonzalez, N. L. Weigel, W. E. Bingman 3rd, and J. S. Richards. 2007. Constitutively active FOXO1a and a DNA-binding domain mutant exhibit distinct co-regulatory functions to enhance progesterone receptor A activity. J. Mol. Endocrinol. 38: 673-690. (Pubitemid 47019067)
    • (2007) Journal of Molecular Endocrinology , vol.38 , Issue.5-6 , pp. 673-690
    • Rudd, M.D.1    Gonzales-Robayna, I.2    Henandez-Gonzalez, I.3    Weigel, N.L.4    Bingman III, W.E.5    Richards, J.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.