메뉴 건너뛰기




Volumn 37, Issue 8, 1996, Pages 1712-1721

Role for sterol regulatory element binding protein in the regulation of farnesyl diphosphate synthase and in the control of cellular levels of cholesterol and triglyceride: Evidence from sterol regulation-defective cells

Author keywords

SRD 2; SRD 6; SREBP

Indexed keywords

BINDING PROTEIN; CHOLESTEROL; MESSENGER RNA; PLASMID DNA; SQUALENE SYNTHASE; TRIACYLGLYCEROL;

EID: 0029833547     PISSN: 00222275     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (33)

References (33)
  • 1
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein, J. L., and M. S. Brown. 1990. Regulation of the mevalonate pathway. Nature. 343: 425-430.
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 2
    • 0026629306 scopus 로고
    • Molecular cloning and promoter analysis of the rat liver farnesyl diphosphate synthase gene
    • Spear, D. H., S. Y. Kutsunai, C. C. Correll, and P. A. Edwards. 1992. Molecular cloning and promoter analysis of the rat liver farnesyl diphosphate synthase gene. J. Biol. Chem. 267: 14462-14469.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14462-14469
    • Spear, D.H.1    Kutsunai, S.Y.2    Correll, C.C.3    Edwards, P.A.4
  • 3
    • 0029100908 scopus 로고
    • Molecular cloning and functional analysis of the promoter of the human squalene synthase gene
    • Guan, G., G. Jiang, R. L. Koch, and I. Shechter. 1995. Molecular cloning and functional analysis of the promoter of the human squalene synthase gene. J. Biol. Chem. 270: 21958-21965.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21958-21965
    • Guan, G.1    Jiang, G.2    Koch, R.L.3    Shechter, I.4
  • 4
    • 0028225462 scopus 로고
    • SREBP-1, a membrane bound transcription factor released by sterol-regulated proteolysis
    • Wang, X., R. Sato, M. S. Brown, X. Hua, and J. L. Goldstein. 1994. SREBP-1, a membrane bound transcription factor released by sterol-regulated proteolysis. Cell. 77: 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
  • 5
    • 0027167918 scopus 로고
    • Nuclear protein that binds to sterol regulatory element of low density lipoprotein receptor promoter. II. Purification and characterization
    • Wang, X., M. R. Briggs, X. Hua, C. Yokoyama, J. L. Goldstein, and M. S. Brown. 1993. Nuclear protein that binds to sterol regulatory element of low density lipoprotein receptor promoter. II. Purification and characterization. J. Biol. Chem. 268: 14497-14504.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14497-14504
    • Wang, X.1    Briggs, M.R.2    Hua, X.3    Yokoyama, C.4    Goldstein, J.L.5    Brown, M.S.6
  • 6
    • 0027139362 scopus 로고
    • SREBP-2, a second basic-helix-loop-helix-leucine zipper protein that stimulates transcription by binding to a sterol regulatory element
    • Hua, X., C. Yokoyama, J. Wu, M. R. Briggs, M. S. Brown, and J. L. Goldstein. 1993. SREBP-2, a second basic-helix-loop-helix-leucine zipper protein that stimulates transcription by binding to a sterol regulatory element. Proc. Natl. Acad. Sci. USA. 90: 11603-11607.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 11603-11607
    • Hua, X.1    Yokoyama, C.2    Wu, J.3    Briggs, M.R.4    Brown, M.S.5    Goldstein, J.L.6
  • 7
    • 0027490174 scopus 로고
    • SREBP-1, a basic-helix-loop-helix-leucine zipper protein that controis transcription of the low density lipoprotein receptor gene
    • Yokoyama, C., X. Wang, M. R. Briggs, A. Adman, J. Wu, X. Hua, J. L. Goldstein, and M. S. Brown. 1993. SREBP-1, a basic-helix-loop-helix-leucine zipper protein that controis transcription of the low density lipoprotein receptor gene. Cell. 75: 187-197.
    • (1993) Cell , vol.75 , pp. 187-197
    • Yokoyama, C.1    Wang, X.2    Briggs, M.R.3    Adman, A.4    Wu, J.5    Hua, X.6    Goldstein, J.L.7    Brown, M.S.8
  • 8
    • 0027648820 scopus 로고
    • ADD1: A novel helix-loop-helix transcription factor associated with adipocyte determination and differentiation
    • Tontonoz, P., J. B. Kim, R. A. Graves, and B. M. Spiegelman. 1993. ADD1: a novel helix-loop-helix transcription factor associated with adipocyte determination and differentiation. Mol. Cell. Biol. 13: 4753-4759.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4753-4759
    • Tontonoz, P.1    Kim, J.B.2    Graves, R.A.3    Spiegelman, B.M.4
  • 9
    • 0028963743 scopus 로고
    • Dual DNA binding specificity of ADD1/SREBP controlled by a single amino acid in the basic helix-loop-helix domain
    • Kim, J. B., G. D. Spotts, Y. Halvorsen, H. Shih, T. Ellenberger, H. C. Towle, and B. M. Spiegelman. 1995. Dual DNA binding specificity of ADD1/SREBP controlled by a single amino acid in the basic helix-loop-helix domain. Mol. Cell. Biol. 15: 2582-2588.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2582-2588
    • Kim, J.B.1    Spotts, G.D.2    Halvorsen, Y.3    Shih, H.4    Ellenberger, T.5    Towle, H.C.6    Spiegelman, B.M.7
  • 11
    • 0028260459 scopus 로고
    • Farnesyl diphosphate synthase is localized in peroxisomes
    • Krisans, S. K., J. Ericsson, P. A. Edwards, and G-A. Keller. 1994. Farnesyl diphosphate synthase is localized in peroxisomes. J. Biol. Chem. 269: 14165-14169.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14165-14169
    • Krisans, S.K.1    Ericsson, J.2    Edwards, P.A.3    Keller, G.-A.4
  • 12
    • 0000680126 scopus 로고
    • Prenyl transferases and isomerases
    • J. W. Porter and S. L. Spurgeon, editors. J. Wiley and Sons, New York
    • Poulter, C. D., and H. C. Rilling. 1991. Prenyl transferases and isomerases. In Biosynthesis of Isoprenoid Compounds. J. W. Porter and S. L. Spurgeon, editors. J. Wiley and Sons, New York. Vol. 1. 162-224.
    • (1991) Biosynthesis of Isoprenoid Compounds , vol.1 , pp. 162-224
    • Poulter, C.D.1    Rilling, H.C.2
  • 13
    • 0025649688 scopus 로고
    • Posttranslational modification of proteins by isoprenoids in mammalian cells
    • Maltese, W. A. 1990. Posttranslational modification of proteins by isoprenoids in mammalian cells. FASEB J. 4: 3319-3328.
    • (1990) FASEB J. , vol.4 , pp. 3319-3328
    • Maltese, W.A.1
  • 14
    • 0028307290 scopus 로고
    • Identification of farnesol as the non-sterol derivative of mevalonic acid required for the accelerated degradation of 3-hydroxy-3-methylglutaryl coenzyme a reductase
    • Correll, C. C., L. Ng, and P. A. Edwards. 1994. Identification of farnesol as the non-sterol derivative of mevalonic acid required for the accelerated degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase. J. Biol. Chem. 269: 17390-17393.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17390-17393
    • Correll, C.C.1    Ng, L.2    Edwards, P.A.3
  • 15
    • 0028285272 scopus 로고
    • Non-sterol compounds that regulate cholesterogenesis
    • Bradfute, D. L., and R. D. Simoni. 1994. Non-sterol compounds that regulate cholesterogenesis. J. Biol. Chem. 269: 6645-6650.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6645-6650
    • Bradfute, D.L.1    Simoni, R.D.2
  • 16
    • 0028223422 scopus 로고
    • Mevalonate-mediated suppression of 3-hydroxy-3-methyl-glutaryl coenzyme a reductase function in α-toxin-perforated cells
    • Giron, M. D., C. M. Havel, and J. A. Watson. 1994. Mevalonate-mediated suppression of 3-hydroxy-3-methyl-glutaryl coenzyme A reductase function in α-toxin-perforated cells. Proc. Natl. Acad. Sci. USA. 91: 6398-6402.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6398-6402
    • Giron, M.D.1    Havel, C.M.2    Watson, J.A.3
  • 18
    • 0029073751 scopus 로고
    • Natural and synthetic non-peptide antigens recognized by human γ,δ T cells
    • Tanaka, Y., C. T. Morita, Y. Tanaka, E. Nieves, M. B. Brenner, and B. R. Bloom. 1995. Natural and synthetic non-peptide antigens recognized by human γ,δ T cells. Nature. 375: 155-158.
    • (1995) Nature , vol.375 , pp. 155-158
    • Tanaka, Y.1    Morita, C.T.2    Tanaka, Y.3    Nieves, E.4    Brenner, M.B.5    Bloom, B.R.6
  • 19
    • 0028149049 scopus 로고
    • Identification of a 6-base pair element involved in the sterol-mediated transcriptional regulation of farnesyl diphosphate synthase
    • Spear, D. H., J. Ericsson, S. M. Jackson, and P. A. Edwards. 1994. Identification of a 6-base pair element involved in the sterol-mediated transcriptional regulation of farnesyl diphosphate synthase. J. Biol. Chem. 269: 25212-25218.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25212-25218
    • Spear, D.H.1    Ericsson, J.2    Jackson, S.M.3    Edwards, P.A.4
  • 20
    • 0029099287 scopus 로고
    • NF-Y has a novel role in sterol-dependent transcription of two cholesterogenic genes
    • Jackson, S. M., J. Ericsson, T. F. Osborne, and P. A. Edwards. 1995. NF-Y has a novel role in sterol-dependent transcription of two cholesterogenic genes. J. Biol. Chem. 270: 21445-21448.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21445-21448
    • Jackson, S.M.1    Ericsson, J.2    Osborne, T.F.3    Edwards, P.A.4
  • 21
    • 0030070645 scopus 로고    scopus 로고
    • Sterol regulatory element binding protein binds to a cis element in the promoter of the farnesyl diphosphate synthase gene
    • Ericsson, J., S. M. Jackson, B. Lee, and P. A. Edwards. 1996. Sterol regulatory element binding protein binds to a cis element in the promoter of the farnesyl diphosphate synthase gene. Proc. Natl. Acad. Sci. USA. 93: 945-950.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 945-950
    • Ericsson, J.1    Jackson, S.M.2    Lee, B.3    Edwards, P.A.4
  • 22
    • 0024971244 scopus 로고
    • Loss of transcriptional repression of three sterol-regulated genes in mutant hamster cells
    • Metherall, J. E., J. L. Goldstein, K. L. Juskey, and M. S. Brown. 1989. Loss of transcriptional repression of three sterol-regulated genes in mutant hamster cells. J. Biol. Chem. 264: 15634-15641.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15634-15641
    • Metherall, J.E.1    Goldstein, J.L.2    Juskey, K.L.3    Brown, M.S.4
  • 23
    • 0027261368 scopus 로고
    • Loss of transcriptional activation of three sterol-regulated genes in mutant hamster cells
    • Evans, M. J., and J. E. Metherall. 1993. Loss of transcriptional activation of three sterol-regulated genes in mutant hamster cells. Mol. Cell. Biol. 13: 5175-5185.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5175-5185
    • Evans, M.J.1    Metherall, J.E.2
  • 24
    • 0029025754 scopus 로고
    • Three different rearrangements in a single intron truncate sterol regulatory element binding protein-2 and produce sterol-resistant phenotype in three cell lines: Role of introns in protein evolution
    • Yang, J., M. S. Brown, Y. K. Ho, and J. L. Goldstein. 1995. Three different rearrangements in a single intron truncate sterol regulatory element binding protein-2 and produce sterol-resistant phenotype in three cell lines: role of introns in protein evolution. J. Biol. Chem. 270: 12152-12161.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12152-12161
    • Yang, J.1    Brown, M.S.2    Ho, Y.K.3    Goldstein, J.L.4
  • 25
    • 0025816877 scopus 로고
    • Genetic distinction between sterol-mediated transcriptional and posttranscriptional control of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
    • Dawson P. A., J. E. Metherall, N. D. Ridgeway, M. S. Brown, and J. L. Goldstein. 1991. Genetic distinction between sterol-mediated transcriptional and posttranscriptional control of 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J. Biol. Chem. 266: 9128-9134.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9128-9134
    • Dawson, P.A.1    Metherall, J.E.2    Ridgeway, N.D.3    Brown, M.S.4    Goldstein, J.L.5
  • 26
    • 0028646168 scopus 로고
    • Two separate sites contribute to AP-1 activation of the promoter for 3-hydroxy-3-methylglutaryl coenzyme A synthase
    • Vallett, S. M., and T. F. Osborne. 1994. Two separate sites contribute to AP-1 activation of the promoter for 3-hydroxy-3-methylglutaryl coenzyme A synthase. Nucleic. Acids Res. 22:5184-5189.
    • (1994) Nucleic. Acids Res. , vol.22 , pp. 5184-5189
    • Vallett, S.M.1    Osborne, T.F.2
  • 27
    • 0026342986 scopus 로고
    • Characterization and distribution of cis-prenyl transferase participating in liver microsomal polyisoprenoid biosynthesis
    • Ericsson, J., A. Thelin, T. Chojnacki, and G. Dallner. 1991. Characterization and distribution of cis-prenyl transferase participating in liver microsomal polyisoprenoid biosynthesis. Eur. J. Biochem. 202: 789-796.
    • (1991) Eur. J. Biochem. , vol.202 , pp. 789-796
    • Ericsson, J.1    Thelin, A.2    Chojnacki, T.3    Dallner, G.4
  • 28
    • 0022556123 scopus 로고
    • Enzymatic methods for quantification of lipoprotein lipids
    • Warnick, G. R. 1986. Enzymatic methods for quantification of lipoprotein lipids. Methods Enzymol. 129: 101-123.
    • (1986) Methods Enzymol. , vol.129 , pp. 101-123
    • Warnick, G.R.1
  • 29
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 31
    • 0023409390 scopus 로고
    • Molecular cloning and sequence of a cholesterol-repressible enzyme related to prenyltransferase in the isoprene biosynthetic pathway
    • Clarke, C. F., R. Tanaka, K. Svenson, M. Walmsley, A. M. Fogelman, and P. A. Edwards. 1987. Molecular cloning and sequence of a cholesterol-repressible enzyme related to prenyltransferase in the isoprene biosynthetic pathway. Mol. Cell. Biol. 7: 3138-3146.
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 3138-3146
    • Clarke, C.F.1    Tanaka, R.2    Svenson, K.3    Walmsley, M.4    Fogelman, A.M.5    Edwards, P.A.6
  • 32
    • 0026733829 scopus 로고
    • Biosynthesis of trans,trans,trans-geranylgeranyl diphosphate by the cytosolic fraction from rat tissues
    • Runquist, M., J. Ericsson, A. Thelin, T. Chojnacki, and G. Dallner. 1992. Biosynthesis of trans,trans,trans-geranylgeranyl diphosphate by the cytosolic fraction from rat tissues. Biochem. Biophys. Res. Commun. 186:157-165.
    • (1992) Biochem. Biophys. Res. Commun. , vol.186 , pp. 157-165
    • Runquist, M.1    Ericsson, J.2    Thelin, A.3    Chojnacki, T.4    Dallner, G.5
  • 33
    • 0027768770 scopus 로고
    • Effect of site-directed mutagenesis of conserved aspartate and arginine residues upon farnesyl diphosphate synthae activity
    • Joly, A., and P. A. Edwards. 1993. Effect of site-directed mutagenesis of conserved aspartate and arginine residues upon farnesyl diphosphate synthae activity. J. Biol. Chem. 268: 26983-26989.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26983-26989
    • Joly, A.1    Edwards, P.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.