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Volumn 87, Issue 3, 1996, Pages 415-426

Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein

Author keywords

[No Author keywords available]

Indexed keywords

ASPARAGINE; ASPARTIC ACID; CHOLESTEROL; COMPLEMENTARY DNA; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; STEROL; TRANSCRIPTION FACTOR;

EID: 0030298339     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)81362-8     Document Type: Article
Times cited : (435)

References (42)
  • 1
    • 0028875426 scopus 로고
    • Sterol regulation of fatty acid synthase promoter: Coordinate feedback regulation of two major lipid pathways
    • Bennett, M.K., Lopez, J.M., Sanchez, H.B., and Osborne, T.F. (1995). Sterol regulation of fatty acid synthase promoter: coordinate feedback regulation of two major lipid pathways. J. Biol. Chem. 270, 25578-25583.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25578-25583
    • Bennett, M.K.1    Lopez, J.M.2    Sanchez, H.B.3    Osborne, T.F.4
  • 2
    • 0027190308 scopus 로고
    • Nuclear protein that binds sterol regulatory element of low density lipoprotein receptor promoter: 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. (1993). Nuclear protein that binds sterol regulatory element of low density lipoprotein receptor promoter: identification of the protein and delineation of its target nucleotide sequence. J. Biol. Chem. 268, 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
  • 3
    • 0022549920 scopus 로고
    • A receptor-mediated pathway for cholesterol homeostasis
    • Brown, M.S., and Goldstein, J.L. (1986). A receptor-mediated pathway for cholesterol homeostasis. Science 232, 34-47.
    • (1986) Science , vol.232 , pp. 34-47
    • Brown, M.S.1    Goldstein, J.L.2
  • 4
    • 15844418021 scopus 로고    scopus 로고
    • Complementation of mutation in acyl-CoA:Cholesterol acyltransferase (ACAT) fails to restore sterol regulation in ACAT-defective sterol-resistant hamster cells
    • Cao, G., Goldstein, J.L., and Brown, M.S. (1996). Complementation of mutation in acyl-CoA:cholesterol acyltransferase (ACAT) fails to restore sterol regulation in ACAT-defective sterol-resistant hamster cells. J. Biol. Chem. 277, 14642-14648.
    • (1996) J. Biol. Chem. , vol.277 , pp. 14642-14648
    • Cao, G.1    Goldstein, J.L.2    Brown, M.S.3
  • 5
    • 0019215066 scopus 로고
    • Regulation of cytosolic acetoacetyl coenzyme Athiolase, 3-hydroxy-3-methylglutaryl coenzyme A synthase, 3-hydroxy-3-methylglutaryl coenzyme A reductase, and mevalonate kinase by low density lipoprotein and by 25-hydroxy-cholesterol in chinese hamster ovary cells
    • Chang, T.-Y., and Limanek, J.S. (1980). Regulation of cytosolic acetoacetyl coenzyme Athiolase, 3-hydroxy-3-methylglutaryl coenzyme A synthase, 3-hydroxy-3-methylglutaryl coenzyme A reductase, and mevalonate kinase by low density lipoprotein and by 25-hydroxy-cholesterol in Chinese hamster ovary cells. J. Biol. Chem. 255, 7787-7795.
    • (1980) J. Biol. Chem. , vol.255 , pp. 7787-7795
    • Chang, T.-Y.1    Limanek, J.S.2
  • 6
    • 0019888174 scopus 로고
    • Evidence for coordinate expression of 3-hydroxy-3-methylglutaryl coenzyme A reductase and low density lipoprotein binding activity
    • Chin, J., and Chang, T.-Y. (1981). Evidence for coordinate expression of 3-hydroxy-3-methylglutaryl coenzyme A reductase and low density lipoprotein binding activity. J. Biol. Chem. 256, 6304-6310.
    • (1981) J. Biol. Chem. , vol.256 , pp. 6304-6310
    • Chin, J.1    Chang, T.-Y.2
  • 8
    • 0018639079 scopus 로고
    • Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease
    • Chirgwin, J.M., Przybyla, A.E., MacDonald, R.J., and Rutter, W.J. (1979). Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18, 5294-5299.
    • (1979) Biochemistry , vol.18 , pp. 5294-5299
    • Chirgwin, J.M.1    Przybyla, A.E.2    MacDonald, R.J.3    Rutter, W.J.4
  • 9
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux, J., Haeberli, P., and Smithies, O. (1984). A comprehensive set of sequence analysis programs for the VAX. Nucl. Acids Res. 12, 387-395.
    • (1984) Nucl. Acids Res. , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 10
    • 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., Jackson, S.M., Lee, B.C., and Edwards, P.A. (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.C.3    Edwards, P.A.4
  • 11
    • 0027261368 scopus 로고
    • Loss of transcriptional activation of three sterol-regulated genes in mutant hamster cells
    • Evans, M.J., and Metherall, J.E. (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
  • 12
    • 0021856440 scopus 로고
    • Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzyme
    • Gil, G., Faust, J.R., Chin, D.J., Goldstein, J.L., and Brown, M.S. (1985). Membrane-bound domain of HMG CoA reductase is required for sterol-enhanced degradation of the enzyme. Cell 41, 249-258.
    • (1985) Cell , vol.41 , pp. 249-258
    • Gil, G.1    Faust, J.R.2    Chin, D.J.3    Goldstein, J.L.4    Brown, M.S.5
  • 13
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein, J.L., and Brown, M.S. (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
  • 14
    • 0000710395 scopus 로고
    • Familial hypercholesterolemia
    • C.R. Scriver, A.L. Beaudet, W.S. Sly, and D. Valle, eds. (New York: McGraw-Hill, Inc.)
    • Goldstein, J.L., Hobbs, H.H., and Brown, M.S. (1995). Familial hypercholesterolemia. In The Metabolic and Molecular Bases of Inherited Disease, C.R. Scriver, A.L. Beaudet, W.S. Sly, and D. Valle, eds. (New York: McGraw-Hill, Inc.), pp. 1981-2030.
    • (1995) The Metabolic and Molecular Bases of Inherited Disease , pp. 1981-2030
    • Goldstein, J.L.1    Hobbs, H.H.2    Brown, M.S.3
  • 15
    • 0028657057 scopus 로고
    • Somatic cell genetic analysis of two classes of CHO cell mutants expressing opposite phenotypes in sterol-dependent regulation of cholesterol metabolism
    • Hasan, M.T., and Chang, T.Y. (1994). Somatic cell genetic analysis of two classes of CHO cell mutants expressing opposite phenotypes in sterol-dependent regulation of cholesterol metabolism. Som. Cell Mol. Genet. 20, 481-491.
    • (1994) Som. Cell Mol. Genet. , vol.20 , pp. 481-491
    • Hasan, M.T.1    Chang, T.Y.2
  • 16
    • 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., Yokoyama, C., Wu, J., Briggs, M.R., Brown, M.S., Goldstein, J.L., and Wang, X. (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    Wang, X.7
  • 17
    • 0028820299 scopus 로고
    • Hairpin orientation of sterol regulatory element binding protein-2 in cell membranes as determined by protease protection
    • Hua, X., Sakai, J., Ho, Y.K., Goldstein, J.L., and Brown, M.S. (1995). Hairpin orientation of sterol regulatory element binding protein-2 in cell membranes as determined by protease protection. J. Biol. Chem. 270, 29422-29427.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29422-29427
    • Hua, X.1    Sakai, J.2    Ho, Y.K.3    Goldstein, J.L.4    Brown, M.S.5
  • 18
    • 0029878960 scopus 로고    scopus 로고
    • Regulated cleavage of sterol regulatory element binding proteins (SREBPs) requires sequences on both sides of the endoplasmic reticulum membrane
    • Hua, X., Sakai, J., Brown, M.S., and Goldstein, J.L. (1996). Regulated cleavage of sterol regulatory element binding proteins (SREBPs) requires sequences on both sides of the endoplasmic reticulum membrane. J. Biol. Chem. 271, 10379-10384.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10379-10384
    • Hua, X.1    Sakai, J.2    Brown, M.S.3    Goldstein, J.L.4
  • 19
    • 0030007427 scopus 로고    scopus 로고
    • ADD1/SREBP1 promotes adipocyte differentiation and gene expression linked to fatty acid metabolism
    • Kim, J.B., and Spiegelman, B.M. (1996). ADD1/SREBP1 promotes adipocyte differentiation and gene expression linked to fatty acid metabolism. Genes Dev. 10, 1096-1107.
    • (1996) Genes Dev. , vol.10 , pp. 1096-1107
    • Kim, J.B.1    Spiegelman, B.M.2
  • 20
    • 0029045589 scopus 로고
    • Molecular dissection of the role of the membrane domain in the regulated degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Kumagai, H., Chun, K.T., and Simoni, R.D. (1995). Molecular dissection of the role of the membrane domain in the regulated degradation of 3-hydroxy-3-methylglutaryl coenzyme A reductase. J. Biol. Chem. 270, 19107-19113.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19107-19113
    • Kumagai, H.1    Chun, K.T.2    Simoni, R.D.3
  • 21
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J., and Doolittle, R.F. (1982). A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 22
    • 0021913335 scopus 로고
    • Domain structure of 3-hydroxy-3-methylglutaryl coenzyme A reductase, a glycoprotein of the endoplasmic reticulum
    • Liscum, L., Finer-Moore, J., Stroud, R.M., Luskey, K.L., Brown, M.S., and Goldstein, J.L. (1985). Domain structure of 3-hydroxy-3-methylglutaryl coenzyme A reductase, a glycoprotein of the endoplasmic reticulum. J. Biol. Chem. 260, 522-530.
    • (1985) J. Biol. Chem. , vol.260 , pp. 522-530
    • Liscum, L.1    Finer-Moore, J.2    Stroud, R.M.3    Luskey, K.L.4    Brown, M.S.5    Goldstein, J.L.6
  • 23
    • 0030020577 scopus 로고    scopus 로고
    • Sterol regulation of acetyl CoA carboxylase: A mechanism for coordinate control of cellular lipid
    • Lopez, J.M., Bennett, M.K., Sanchez, H.B., Rosenfeld, J.M., and Osborne, T.F. (1996). Sterol regulation of acetyl CoA carboxylase: a mechanism for coordinate control of cellular lipid. Proc. Natl. Acad. Sci. USA 93, 1049-1053.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1049-1053
    • Lopez, J.M.1    Bennett, M.K.2    Sanchez, H.B.3    Rosenfeld, J.M.4    Osborne, T.F.5
  • 24
    • 0024971244 scopus 로고
    • Loss of transcriptional repression of three sterol-regulated genes in mutant hamster cells
    • Metherall, J.E., Goldstein, J.L., Luskey, K.L., and Brown, M.S. (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    Luskey, K.L.3    Brown, M.S.4
  • 25
    • 0030608273 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes: The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1
    • in press
    • Nagase, T., Seki, N., Tanaka, A., Ishikawa, K., and Nomura, N. (1996). Prediction of the coding sequences of unidentified human genes: the coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1. DNA Research, in press.
    • (1996) DNA Research
    • Nagase, T.1    Seki, N.2    Tanaka, A.3    Ishikawa, K.4    Nomura, N.5
  • 26
    • 0028076764 scopus 로고
    • The ancient regulatory-protein family of WD repeat proteins
    • Neer, E.J., Schmidt, C.J., Nambudripad, R., and Smith, T.F. (1994). The ancient regulatory-protein family of WD repeat proteins. Nature 377, 297-300.
    • (1994) Nature , vol.377 , pp. 297-300
    • Neer, E.J.1    Schmidt, C.J.2    Nambudripad, R.3    Smith, T.F.4
  • 27
    • 0030472004 scopus 로고    scopus 로고
    • Recurrent G-to-A substitution in a single codon of SREBP cleavage-activating protein (SCAP) causes sterol resistance in three mutant CHO cell lines
    • in press
    • Nohturfft, A., Hua, X., Brown, M.S., and Goldstein, J.L. (1996). Recurrent G-to-A substitution in a single codon of SREBP cleavage-activating protein (SCAP) causes sterol resistance in three mutant CHO cell lines. Proc. Natl. Acad. Sci. USA, in press.
    • (1996) Proc. Natl. Acad. Sci. USA
    • Nohturfft, A.1    Hua, X.2    Brown, M.S.3    Goldstein, J.L.4
  • 28
    • 0026673416 scopus 로고
    • The intracellular targeting and membrane topology of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Olender, E.H., and Simoni, R.D. (1992). The intracellular targeting and membrane topology of 3-hydroxy-3-methylglutaryl-CoA reductase. J. Biol. Chem. 267, 4223-4235.
    • (1992) J. Biol. Chem. , vol.267 , pp. 4223-4235
    • Olender, E.H.1    Simoni, R.D.2
  • 29
    • 0024756969 scopus 로고
    • Rapid and sensitive detection of point mutations and DNA polymorphisms using the polymerase chain reaction
    • Orita, M., Suzuki, Y., Sekiya, T., and Hayashi, K. (1989). Rapid and sensitive detection of point mutations and DNA polymorphisms using the polymerase chain reaction. Genomics 5, 874-879.
    • (1989) Genomics , vol.5 , pp. 874-879
    • Orita, M.1    Suzuki, Y.2    Sekiya, T.3    Hayashi, K.4
  • 30
    • 0026720521 scopus 로고
    • Immunological evidence for eight spans in the membrane domain of 3-hydroxy-3-methylglutaryl coenzyme A reductase: Implications for enzyme degradation in the endoplasmic reticulum
    • Roitelman, J., Olender, E.H., Bar-Nun, S., Dunn, W.A., Jr., and Simoni, R.D. (1992). Immunological evidence for eight spans in the membrane domain of 3-hydroxy-3-methylglutaryl coenzyme A reductase: implications for enzyme degradation in the endoplasmic reticulum. J. Cell Biol. 117, 959-973.
    • (1992) J. Cell Biol. , vol.117 , pp. 959-973
    • Roitelman, J.1    Olender, E.H.2    Bar-Nun, S.3    Dunn, W.A.4    Simoni, R.D.5
  • 31
    • 0030604717 scopus 로고    scopus 로고
    • Sterol-regulated release of SREBP-2 from cell membranes requires two sequential cleavages, one within a transmembrane segment
    • Sakai, J., Duncan, E.A., Rawson, R.B., Hua, X., Brown, M.S., and Goldstein, J.L. (1996). Sterol-regulated release of SREBP-2 from cell membranes requires two sequential cleavages, one within a transmembrane segment. Cell 85, 1037-1046.
    • (1996) Cell , vol.85 , pp. 1037-1046
    • Sakai, J.1    Duncan, E.A.2    Rawson, R.B.3    Hua, X.4    Brown, M.S.5    Goldstein, J.L.6
  • 32
    • 0028360111 scopus 로고
    • Assignment of the membrane attachment, DNA binding, and transcriptional activation domains of sterol regulatory element binding protein-1 (SREBP-1)
    • Sato, R., Yang, J., Wang, X., Evans, M.J., Ho, Y.K., Goldstein, J.L., and Brown, M.S. (1994). Assignment of the membrane attachment, DNA binding, and transcriptional activation domains of sterol regulatory element binding protein-1 (SREBP-1). J. Biol. Chem. 269, 17267-17273.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17267-17273
    • Sato, R.1    Yang, J.2    Wang, X.3    Evans, M.J.4    Ho, Y.K.5    Goldstein, J.L.6    Brown, M.S.7
  • 33
    • 0029797604 scopus 로고    scopus 로고
    • Overproduction of cholesterol and fatty acids causes massive liver enlargement in transgenic mice expressing truncated SREBP-1a
    • in press
    • Shimano, H., Horton, J.D., Hammer, R.E., Shimomura, I., Brown, M.S., and Goldstein, J.L. (1996). Overproduction of cholesterol and fatty acids causes massive liver enlargement in transgenic mice expressing truncated SREBP-1a. J. Clin. Invest., in press.
    • (1996) J. Clin. Invest.
    • Shimano, H.1    Horton, J.D.2    Hammer, R.E.3    Shimomura, I.4    Brown, M.S.5    Goldstein, J.L.6
  • 35
    • 0027305130 scopus 로고
    • Regulation of plasma LDL-cholesterol levels by dietary cholesterol and fatty acids
    • Spady, D.K., Woollett, L.A., and Dietschy, J.M. (1993). Regulation of plasma LDL-cholesterol levels by dietary cholesterol and fatty acids. Annu. Rev. Nutr. 13, 355-381.
    • (1993) Annu. Rev. Nutr. , vol.13 , pp. 355-381
    • Spady, D.K.1    Woollett, L.A.2    Dietschy, J.M.3
  • 36
    • 0011176887 scopus 로고    scopus 로고
    • A direct role for sterol regulatory element binding protein in activation of 3-hydroxy-3-methylglutaryl coenzyme A reductase gene
    • 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.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12247-12253
    • Vallett, S.M.1    Sanchez, H.B.2    Rosenfeld, J.M.3    Osborne, T.F.4
  • 38
    • 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. (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
  • 39
    • 0028295681 scopus 로고
    • 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. Elegans
    • Wilson, R., Ainscough, R., Anderson, K., and others. (1994). 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans. Nature 368, 32-38.
    • (1994) Nature , vol.368 , pp. 32-38
    • Wilson, R.1    Ainscough, R.2    Anderson, K.3
  • 40
    • 0028133279 scopus 로고
    • Sterol-resistant transcription in CHO cells caused by gene rearrangement that truncates SREBP-2
    • Yang, J., Sato, R., Goldstein, J.L., and Brown, M.S. (1994). Sterol-resistant transcription in CHO cells caused by gene rearrangement that truncates SREBP-2. Genes Dev. 8, 1910-1919.
    • (1994) Genes Dev. , vol.8 , pp. 1910-1919
    • Yang, J.1    Sato, R.2    Goldstein, J.L.3    Brown, M.S.4
  • 41
    • 0029025754 scopus 로고
    • Three different rearrangements in a single intron truncate SREBP-2 and produce sterol-resistant phenotype in three cell lines
    • Yang, J., Brown, M.S., Ho, Y.K., and Goldstein, J.L. (1995). Three different rearrangements in a single intron truncate SREBP-2 and produce sterol-resistant phenotype in three cell lines. 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
  • 42
    • 0027490174 scopus 로고
    • SREBP-1, a basic-helix-loop-helix-leucine zipper protein that controls transcription of the ldl receptor gene
    • Yokoyama, C., Wang, X., Briggs, M.R., Admon, A., Wu, J., Hua, X., Goldstein, J.L., and Brown, M.S. (1993). SREBP-1, a basic-helix-loop-helix-leucine zipper protein that controls transcription of the LDL receptor gene. Cell 75, 187-197.
    • (1993) Cell , vol.75 , pp. 187-197
    • Yokoyama, C.1    Wang, X.2    Briggs, M.R.3    Admon, A.4    Wu, J.5    Hua, X.6    Goldstein, J.L.7    Brown, M.S.8


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