메뉴 건너뛰기




Volumn 8, Issue 2, 1997, Pages 65-71

Chinese hamster ovary cell mutants affecting cholesterol metabolism

Author keywords

[No Author keywords available]

Indexed keywords

ACYL COENZYME A; BINDING PROTEIN; CELL ENZYME; CHOLESTEROL; CHOLESTEROL ACYLTRANSFERASE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; HYDROXYMETHYLGLUTARYL COENZYME A SYNTHASE; MEMBRANE LIPID; MEMBRANE PROTEIN; SQUALENE SYNTHASE; STEROL; STEROL 14ALPHA DEMETHYLASE; UNCLASSIFIED DRUG;

EID: 0030972259     PISSN: 09579672     EISSN: None     Source Type: Journal    
DOI: 10.1097/00041433-199704000-00003     Document Type: Review
Times cited : (29)

References (79)
  • 1
    • 0024996833 scopus 로고
    • Evidence for allelic exclusion in Chinese hamster ovary cells
    • Holliday R, Ho T: Evidence for allelic exclusion in Chinese hamster ovary cells. New Biologist 1990, 2:719-726.
    • (1990) New Biologist , vol.2 , pp. 719-726
    • Holliday, R.1    Ho, T.2
  • 2
    • 0025827425 scopus 로고
    • Mutations and epimutations in mammalian cells
    • Holliday R: Mutations and epimutations in mammalian cells. Mutation Res 1991, 250:351-363.
    • (1991) Mutation Res , vol.250 , pp. 351-363
    • Holliday, R.1
  • 3
    • 0017165502 scopus 로고
    • Isolation and characterization of an unsaturated fatty acid requiring mutant of cultured mammalian cells
    • Chang TY, Vagelos PR: Isolation and characterization of an unsaturated fatty acid requiring mutant of cultured mammalian cells. Proc Natl Acad Sci USA 1976, 73:24-28.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 24-28
    • Chang, T.Y.1    Vagelos, P.R.2
  • 5
    • 0018746012 scopus 로고
    • Inhibition of cholesterol synthesis with compactin renders growth of cultured cells dependent on the low density lipoprotein receptor
    • Goldstein JL, Helgeson JAS, Brown MS: Inhibition of cholesterol synthesis with compactin renders growth of cultured cells dependent on the low density lipoprotein receptor. J Biol Chem 1979, 254: 5403-5409.
    • (1979) J Biol Chem , vol.254 , pp. 5403-5409
    • Goldstein, J.L.1    Helgeson, J.A.S.2    Brown, M.S.3
  • 6
    • 0019215066 scopus 로고
    • Regulation of cytosolic acetoacetyl coenzyme A thiolase, 3-hydroxy-3-methylglutaryl coenzyme A synthase, 3-hydroxy-3-methylglutaryl coenzyme A reductase, and mevalonate kinase by low density lipoprotein and by 25-hydroxycholesterol in Chinese hamster ovary cells
    • Chang TY, Limanek JS: Regulation of cytosolic acetoacetyl coenzyme A thiolase, 3-hydroxy-3-methylglutaryl coenzyme A synthase, 3-hydroxy-3-methylglutaryl coenzyme A reductase, and mevalonate kinase by low density lipoprotein and by 25-hydroxycholesterol in Chinese hamster ovary cells. J Biol Chem 1980, 255:7787-7795.
    • (1980) J Biol Chem , vol.255 , pp. 7787-7795
    • Chang, T.Y.1    Limanek, J.S.2
  • 7
    • 0023881297 scopus 로고
    • Somatic cell genetics and the study of cholesterol metabolism
    • Leonard S, Sinensky M: Somatic cell genetics and the study of cholesterol metabolism. Biochim Biophys Acta 1988, 47:101-112.
    • (1988) Biochim Biophys Acta , vol.47 , pp. 101-112
    • Leonard, S.1    Sinensky, M.2
  • 8
    • 0028169450 scopus 로고
    • Isolation of three classes of conditional lethal Chinese hamster ovary cell mutants with temperature-dependent defects in low density lipoprotein receptor
    • Hobbie L, Fisher AS, Lee S, Flint A, Krieger M: Isolation of three classes of conditional lethal Chinese hamster ovary cell mutants with temperature-dependent defects in low density lipoprotein receptor. J Biol Chem 1994, 269:20958-20970.
    • (1994) J Biol Chem , vol.269 , pp. 20958-20970
    • Hobbie, L.1    Fisher, A.S.2    Lee, S.3    Flint, A.4    Krieger, M.5
  • 9
    • 17544372313 scopus 로고    scopus 로고
    • A single point mutation in epsilon-COP results in temperature-sensitive, lethal defects in membrane transport in a Chinese hamster ovary cell mutant
    • Guo Q, Penman M, Trigatti BL, Krieger M: A single point mutation in epsilon-COP results in temperature-sensitive, lethal defects in membrane transport in a Chinese hamster ovary cell mutant. J Biol Chem 1996, 271:11191-11196.
    • (1996) J Biol Chem , vol.271 , pp. 11191-11196
    • Guo, Q.1    Penman, M.2    Trigatti, B.L.3    Krieger, M.4
  • 10
    • 0025005876 scopus 로고
    • Sterol-mediated regulation of mevalonic acid synthesis. Accumulation of 4-carboxysterols as the predominant sterols synthesized in a Chinese hamster ovary cell cholesterol auxotroph (mutant 215)
    • Plemenitas A, Havel CM, Watson JA: Sterol-mediated regulation of mevalonic acid synthesis. Accumulation of 4-carboxysterols as the predominant sterols synthesized in a Chinese hamster ovary cell cholesterol auxotroph (mutant 215). J Biol Chem 1990, 265:17012-17017.
    • (1990) J Biol Chem , vol.265 , pp. 17012-17017
    • Plemenitas, A.1    Havel, C.M.2    Watson, J.A.3
  • 11
    • 0020030243 scopus 로고
    • Further characterization of a Chinese hamster ovary cell mutant defective in lanosterol demethylation
    • Berry DJ, Chang TY: Further characterization of a Chinese hamster ovary cell mutant defective in lanosterol demethylation. Biochemistry 1982, 21:573-580.
    • (1982) Biochemistry , vol.21 , pp. 573-580
    • Berry, D.J.1    Chang, T.Y.2
  • 12
    • 0018214846 scopus 로고
    • A mammalian cell mutant requiring cholesterol and unsaturated fatty acid for growth
    • Limanek JS, Chin J, Chang TY: A mammalian cell mutant requiring cholesterol and unsaturated fatty acid for growth. Proc Natl Acad Sci U S A 1978, 75:5452-5456.
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 5452-5456
    • Limanek, J.S.1    Chin, J.2    Chang, T.Y.3
  • 13
    • 0019888174 scopus 로고
    • Evidence for coordinate expression of 3-hydroxy-3-methylglutaryl coenzyme A. Reductase and low density lipoprotein binding activity
    • Chin J, Chang TY: Evidence for coordinate expression of 3-hydroxy-3-methylglutaryl coenzyme A. Reductase and low density lipoprotein binding activity. J Biol Chem 1981, 256:6304-6310.
    • (1981) J Biol Chem , vol.256 , pp. 6304-6310
    • Chin, J.1    Chang, T.Y.2
  • 14
    • 0019965819 scopus 로고
    • Further characterization of a Chinese hamster ovary cell mutant requiring cholesterol and unsaturated fatty acid for growth
    • Chin J, Chang TY: Further characterization of a Chinese hamster ovary cell mutant requiring cholesterol and unsaturated fatty acid for growth. Biochemistry 1982, 21:3196-3202.
    • (1982) Biochemistry , vol.21 , pp. 3196-3202
    • Chin, J.1    Chang, T.Y.2
  • 15
    • 0027261368 scopus 로고
    • Loss of transcriptional activation of three sterol-regulated genes in mutant hamster cells
    • Evans MJ, Metherall JE: Loss of transcriptional activation of three sterol-regulated genes in mutant hamster cells. Mol Cell Biol 1993, 13:5175-5185.
    • (1993) Mol Cell Biol , vol.13 , pp. 5175-5185
    • Evans, M.J.1    Metherall, J.E.2
  • 16
    • 0029833547 scopus 로고    scopus 로고
    • Role of 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
    • Jackson SM, Ericsson J, Metherall JE, Edwards PA: Role of 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. J Lipid Res 1996, 37:1712-1721.
    • (1996) J Lipid Res , vol.37 , pp. 1712-1721
    • Jackson, S.M.1    Ericsson, J.2    Metherall, J.E.3    Edwards, P.A.4
  • 17
    • 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 EA, Rawson RB, Hua X, Brown MS, Goldstein JL: Sterol-regulated release of SREBP-2 from cell membranes requires two sequential cleavages, one within a transmembrane segment. Cell 1996, 85:1037-1046. This paper elegantly demonstrates that the release of SREBP-2 from the ER membrane requires two sequential proteolytic cleavages. The first cleavage is regulated by sterols while the second cleavage, which can occur only after the first cleavage, is not regulated by sterols. Mutant M-19 and SRD-6 cells are normal at the first cleavage step but defective at the second cleavage step, thus enabling the authors to detect accumulation of a critical intermediate of SREBP-2 after the first cleavage.
    • (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
  • 18
    • 0028087833 scopus 로고
    • Somatic cell genetic and biochemical characterization of cell lines resulting from human genomic DNA transfection of Chinese hamster ovary cell mutants defective in sterol-dependent activation of sterol synthesis and LDL receptor expression
    • Hasan MT, Chang CCY, Chang TY: Somatic cell genetic and biochemical characterization of cell lines resulting from human genomic DNA transfection of Chinese hamster ovary cell mutants defective in sterol-dependent activation of sterol synthesis and LDL receptor expression. Somatic Cell Mol Genet 1994, 20:183-194.
    • (1994) Somatic Cell Mol Genet , vol.20 , pp. 183-194
    • Hasan, M.T.1    Chang, C.C.Y.2    Chang, T.Y.3
  • 19
    • 0021090221 scopus 로고
    • Analysis of the coordinate expression of HMG-CoA synthase and reductase activities in Chinese hamster ovary fibroblasts
    • Schnitzer-Polokoff R, Torget R, Logel J, Sinensky M: Analysis of the coordinate expression of HMG-CoA synthase and reductase activities in Chinese hamster ovary fibroblasts. Arch Biochem Biophys 1983, 227:71-80.
    • (1983) Arch Biochem Biophys , vol.227 , pp. 71-80
    • Schnitzer-Polokoff, R.1    Torget, R.2    Logel, J.3    Sinensky, M.4
  • 20
    • 0027167918 scopus 로고
    • Nuclear protein that binds sterol regulatory element of low density lipoprotein receptor promoter. II. Purification and characterization
    • Wang X, Briggs MR, Hua X, Yokoyama C, Goldstein JL, Brown MS: Nuclear protein that binds sterol regulatory element of low density lipoprotein receptor promoter. II. Purification and characterization. J Biol Chem 1993, 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
  • 21
    • 0027490174 scopus 로고
    • SREBP-1, a basic-helix-loop-helix-leucine zipper protein that controls transcription of the low density lipoprotein receptor gene
    • Yokoyama C, Wang X, Briggs MR, Admon A, Wu J, Hua X, Goldstein JL, Brown MS: SREBP-1, a basic-helix-loop-helix-leucine zipper protein that controls transcription of the low density lipoprotein receptor gene. Cell 1993, 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
  • 22
    • 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 MR, Brown MS, Goldstein JL, Wang X: 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 U S A 1993, 90:11603-11607.
    • (1993) Proc Natl Acad Sci U S A , 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
  • 23
    • 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 MJ, Ho YK, Goldstein JL, Brown MS: Assignment of the membrane attachment, DNA binding, and transcriptional activation domains of sterol regulatory element binding protein-1 (SREBP-1). J Biol Chem 1994, 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
  • 24
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein JL, Brown MS: Regulation of the mevalonate pathway. Nature 1990, 343:425-430.
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 25
    • 0029100908 scopus 로고
    • Molecular cloning and functional analysis of the promoter of the human squalene synthase gene
    • ••] shows that SREBPs are important in transcriptional activation of many sterol-sensitive genes.
    • (1995) J Biol Chem , vol.270 , pp. 21958-21965
    • Guan, G.1    Jiang, G.2    Koch, R.L.3    Shechter, I.4
  • 29
    • 0029797604 scopus 로고    scopus 로고
    • Overproduction of cholesterol and fatty acids causes massive liver enlargement in transgenic mice expressing truncated SREBP-1a
    • Shimano H, Horton JD, Hammer RE, Shimomura I, Brown MS, Goldstein JL: Overproduction of cholesterol and fatty acids causes massive liver enlargement in transgenic mice expressing truncated SREBP-1a. J Clin Invest 1996, 98:1575-1584. This paper demonstrates the effect of overexpressing truncated SREBP-1a on cholesterol synthesis and fatty acid synthesis in livers of intact animals.
    • (1996) J Clin Invest , vol.98 , pp. 1575-1584
    • Shimano, H.1    Horton, J.D.2    Hammer, R.E.3    Shimomura, I.4    Brown, M.S.5    Goldstein, J.L.6
  • 30
    • 0026742623 scopus 로고
    • Red 25, a protein that binds specifically to the sterol regulatory region in the promoter for HMG-CoA reductase
    • Osborne TF, Bennett O, Rhee K: Red 25, a protein that binds specifically to the sterol regulatory region in the promoter for HMG-CoA reductase. J Biol Chem 1992, 267:18973-18982
    • (1992) J Biol Chem , vol.267 , pp. 18973-18982
    • Osborne, T.F.1    Bennett, O.2    Rhee, K.3
  • 31
    • 0028820299 scopus 로고
    • Hairpin orientation of sterol regulatory element binding protein-2 in cell membranes as determined by protease protection
    • Hua X, Sakai J, Brown MS, Goldstein JL: Hairpin orientation of sterol regulatory element binding protein-2 in cell membranes as determined by protease protection. J Biol Chem 1995, 270:29422-29427.
    • (1995) J Biol Chem , vol.270 , pp. 29422-29427
    • Hua, X.1    Sakai, J.2    Brown, M.S.3    Goldstein, J.L.4
  • 32
    • 0020044109 scopus 로고
    • Isolation and characterization of a mammalian cell mutant defective in 3-hydroxy-3-methylglutaryl coenzyme A synthase
    • Schnitzer-Polokoff R, von Gunten C, Torget R, Sinensky M: Isolation and characterization of a mammalian cell mutant defective in 3-hydroxy-3-methylglutaryl coenzyme A synthase. J Biol Chem 1982, 257:472-476.
    • (1982) J Biol Chem , vol.257 , pp. 472-476
    • Schnitzer-Polokoff, R.1    Von Gunten, C.2    Torget, R.3    Sinensky, M.4
  • 33
    • 0021059302 scopus 로고
    • Mutant clone of Chinese hamster ovary cells lacking 3-hydroxy-3-methylglutaryl coenzyme A reductase
    • Mosley ST, Brown MS, Anderson RGW, Goldstein JL: Mutant clone of Chinese hamster ovary cells lacking 3-hydroxy-3-methylglutaryl coenzyme A reductase. J Biol Chem 1983, 258:13875-13881.
    • (1983) J Biol Chem , vol.258 , pp. 13875-13881
    • Mosley, S.T.1    Brown, M.S.2    Anderson, R.G.W.3    Goldstein, J.L.4
  • 34
    • 0022537701 scopus 로고
    • Isolation of animal cell mutants deficient in plasmalogen biosynthesis and peroxisome assembly
    • Zoeller RA, Raetz CRH: Isolation of animal cell mutants deficient in plasmalogen biosynthesis and peroxisome assembly. Proc Natl Acad Sci U S A 1986, 83:5170-5174.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 5170-5174
    • Zoeller, R.A.1    Raetz, C.R.H.2
  • 35
    • 0025255898 scopus 로고
    • A rapid selection for animal cell mutants with defective peroxisomes
    • Allen LA, Zoeller RA, Raetz CR: A rapid selection for animal cell mutants with defective peroxisomes. Biochim Biophys Acta 1990, 1034:132-141.
    • (1990) Biochim Biophys Acta , vol.1034 , pp. 132-141
    • Allen, L.A.1    Zoeller, R.A.2    Raetz, C.R.3
  • 37
    • 0023871216 scopus 로고
    • A mammalian mutant cell lacking detectable lanosterol 14-alpha methyl demethylase activity
    • Chen HW, Leonard DA, Fischer RT, Trzaskos JM: A mammalian mutant cell lacking detectable lanosterol 14-alpha methyl demethylase activity. J Biol Chem 1988, 263:1248-1254.
    • (1988) J Biol Chem , vol.263 , pp. 1248-1254
    • Chen, H.W.1    Leonard, D.A.2    Fischer, R.T.3    Trzaskos, J.M.4
  • 38
    • 0026702230 scopus 로고
    • Squalene synthase-deficient mutant of Chinese hamster ovary cells
    • Bradfute DL, Silva CJ, Simoni RD: Squalene synthase-deficient mutant of Chinese hamster ovary cells. J Biol Chem 1992, 267:18308-18314.
    • (1992) J Biol Chem , vol.267 , pp. 18308-18314
    • Bradfute, D.L.1    Silva, C.J.2    Simoni, R.D.3
  • 39
    • 0018744385 scopus 로고
    • Defective regulation of HMG-CoA reductase in a somatic cell mutant
    • Sinensky M, Duwe G, Pinkerton F: Defective regulation of HMG-CoA reductase in a somatic cell mutant. J Biol Chem 1979, 254:4482-4486.
    • (1979) J Biol Chem , vol.254 , pp. 4482-4486
    • Sinensky, M.1    Duwe, G.2    Pinkerton, F.3
  • 40
    • 0018386317 scopus 로고
    • Sterol synthesis in variant Chinese hamster lung cells selected for resistance to 25-hydroxycholesterol
    • Chen HW, Cavenee WK, Kandutsch AA: Sterol synthesis in variant Chinese hamster lung cells selected for resistance to 25-hydroxycholesterol. J Biol Chem 1979, 254:715-720.
    • (1979) J Biol Chem , vol.254 , pp. 715-720
    • Chen, H.W.1    Cavenee, W.K.2    Kandutsch, A.A.3
  • 41
    • 0020420324 scopus 로고
    • Revertants of Chinese hamster ovary cell mutant resistant to suppression by analog of cholesterol-isolation and partial characterization
    • Chang TY, Chang CCY: Revertants of Chinese hamster ovary cell mutant resistant to suppression by analog of cholesterol-isolation and partial characterization. Biochemistry 1982, 21:5316-5323.
    • (1982) Biochemistry , vol.21 , pp. 5316-5323
    • Chang, T.Y.1    Chang, C.C.Y.2
  • 42
    • 0023882098 scopus 로고
    • Isolation and characterization of Chinese hamster ovary cell mutants deficient in acyl-coenzyme A: Cholesterol acyltransferase activity
    • Cadigan KM, Heider JG, Chang TY: Isolation and characterization of Chinese hamster ovary cell mutants deficient in acyl-coenzyme A: cholesterol acyltransferase activity. J Biol Chem 1988, 263:274-282.
    • (1988) J Biol Chem , vol.263 , pp. 274-282
    • Cadigan, K.M.1    Heider, J.G.2    Chang, T.Y.3
  • 43
    • 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 MT, Chang TY: Somatic cell genetic analysis of two classes of CHO cell mutants expressing opposite phenotypes in sterol-dependent regulation of cholesterol metabolism. Somatic Cell Mol Genet 1994, 20:481-491.
    • (1994) Somatic Cell Mol Genet , vol.20 , pp. 481-491
    • Hasan, M.T.1    Chang, T.Y.2
  • 44
    • 0024971244 scopus 로고
    • Loss of transcriptional repression of three sterol-regulated genes in mutant hamster cells
    • Metherall JE, Goldstein JL, Luskey KL, Brown MS: Loss of transcriptional repression of three sterol-regulated genes in mutant hamster cells. J Biol Chem 1989, 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
  • 45
    • 0025816877 scopus 로고
    • Genetic distinction between sterol-mediated transcriptional and posttranscriptional control of 3-hydroxy-3-methylglutaryl-coenzyme A reductase
    • Dawson PA, Metherall JE, Ridgway ND, Brown MS, Goldstein JL: Genetic distinction between sterol-mediated transcriptional and posttranscriptional control of 3-hydroxy-3-methylglutaryl-coenzyme A reductase. J Biol Chem 1991, 266:9128-9134.
    • (1991) J Biol Chem , vol.266 , pp. 9128-9134
    • Dawson, P.A.1    Metherall, J.E.2    Ridgway, N.D.3    Brown, M.S.4    Goldstein, J.L.5
  • 46
    • 0025741305 scopus 로고
    • A 25-hydroxycholesterol-resistant cell line deficient in acyl-coA : Cholesterol acyltransferase
    • Metherall JE, Ridgway ND, Dawson PA, Goldstein JL, Brown MS: A 25-hydroxycholesterol-resistant cell line deficient in acyl-coA : cholesterol acyltransferase. J Biol Chem 1991, 266:12734-12740.
    • (1991) J Biol Chem , vol.266 , pp. 12734-12740
    • Metherall, J.E.1    Ridgway, N.D.2    Dawson, P.A.3    Goldstein, J.L.4    Brown, M.S.5
  • 48
    • 0028133279 scopus 로고
    • Sterol-resistant transcription in CHO cells caused by gene rearrangement that truncates SREBP-2
    • Yang J, Sato R, Goldstein JL, Brown MS: Sterol-resistant transcription in CHO cells caused by gene rearrangement that truncates SREBP-2. Genes Dev 1994, 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
  • 49
    • 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, Brown MS, Ho YK, Goldstein JL: 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 1995, 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
  • 50
    • 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 JL, Brown MS: Complementation of mutation in acyl-CoA: cholesterol acyltransferase (ACAT) fails to restore sterol regulation in ACAT-defective sterol-resistant hamster cells. J Biol Chem 1996, 271:14642-14648.
    • (1996) J Biol Chem , vol.271 , pp. 14642-14648
    • Cao, G.1    Goldstein, J.L.2    Brown, M.S.3
  • 51
    • 0030298339 scopus 로고    scopus 로고
    • Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein
    • Hua X, Nohturfft A, Goldstein JL, Brown MS: Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein. Cell 1996, 87:415-426. An ingenious expression cloning strategy was designed to clone the mutant gene in 25-RA cells. A new gene encoding the protein called SREBP cleavage-activating protein (SCAP) was discovered. Sterol resistance in 25-RA cells was traced to a gain-of-function point mutation in the protein coding region of SCAP. SCAP may be a regulator of the site 1 protease for cleaving SREBPs.
    • (1996) Cell , vol.87 , pp. 415-426
    • Hua, X.1    Nohturfft, A.2    Goldstein, J.L.3    Brown, M.S.4
  • 52
    • 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
    • Nohturfft A, Hua X, Brown MS, Goldstein JL: 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 U S A 1996, 93:13709-13714.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 13709-13714
    • Nohturfft, A.1    Hua, X.2    Brown, M.S.3    Goldstein, J.L.4
  • 53
    • 0026720521 scopus 로고
    • Immunological evidence for eight spans in the membrane domains of HMG-CoA reductase: Implications for enzyme degradation in the endoplasmic reticulum
    • Roitelman J, Olender EH, Bar-Nun S, Dunn WA Jr, Simoni RD: Immunological evidence for eight spans in the membrane domains of HMG-CoA reductase: implications for enzyme degradation in the endoplasmic reticulum. J Cell Biol 1992, 117:959-973.
    • (1992) J Cell Biol , vol.117 , pp. 959-973
    • Roitelman, J.1    Olender, E.H.2    Bar-Nun, S.3    Dunn Jr., W.A.4    Simoni, R.D.5
  • 54
    • 0029833547 scopus 로고    scopus 로고
    • Role of 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
    • Jackson SM, Ericsson J, Metherall JE, Edwards PA: Role of 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. J Lipid Res 1996, 37:1712-1721.
    • (1996) J Lipid Res , vol.37 , pp. 1712-1721
    • Jackson, S.M.1    Ericsson, J.2    Metherall, J.E.3    Edwards, P.A.4
  • 55
    • 0027648820 scopus 로고
    • ADD1: A novel helix-loop-helix transcription factor associated with adipocyte determination and differentiation
    • Tontonoz P, Kim JB, Graves RA, Spiegelman BM: ADD1: a novel helix-loop-helix transcription factor associated with adipocyte determination and differentiation. Mol Cell Biol 1993, 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
  • 56
    • 0028963743 scopus 로고
    • Dual DNA binding specificity of ADD1/SREBP controlled by a single amino acid in the basic helix-loop-helix domain
    • Kim JB, Spotts GD, Halvorsen Y, Shih H, Ellenberger T, Towle HC, Spiegelman BM: Dual DNA binding specificity of ADD1/SREBP controlled by a single amino acid in the basic helix-loop-helix domain. Mol Cell Biol 1995, 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
  • 57
    • 0029928511 scopus 로고    scopus 로고
    • Compartmental isolation of cholesterol participating in the cytoplasmic cholesteryl ester cycle in Chinese hamster ovary 25-RA cells
    • Klansek JJ, Warner GJ, Johnson WJ, Glick JM: Compartmental isolation of cholesterol participating in the cytoplasmic cholesteryl ester cycle in Chinese hamster ovary 25-RA cells. J Biol Chem 1996, 271:4923-4929. Using indirect means, this paper elegantly demonstrates a distinct intracellular cholesterol pool participating in the cytoplasmic cholesteryl ester cycle in 25-RA cells.
    • (1996) J Biol Chem , vol.271 , pp. 4923-4929
    • Klansek, J.J.1    Warner, G.J.2    Johnson, W.J.3    Glick, J.M.4
  • 58
    • 0026482522 scopus 로고
    • Expression of 7 alpha-hydroxylase in non-hepatic cells results in liver phenotypic resistance of the low density lipoprotein receptor to cholesterol repression
    • Dueland STJ, Nenseter MS, MacPhee AA, Davis RA: Expression of 7 alpha-hydroxylase in non-hepatic cells results in liver phenotypic resistance of the low density lipoprotein receptor to cholesterol repression. J Biol Chem 1992, 267:22695-22698.
    • (1992) J Biol Chem , vol.267 , pp. 22695-22698
    • Dueland, S.T.J.1    Nenseter, M.S.2    MacPhee, A.A.3    Davis, R.A.4
  • 59
    • 0019870058 scopus 로고
    • Isolation and characterization of cells resistant to ML236B (compactin) with increased levels of HMG-CoA reductase
    • Ryan J, Hardeman EC, Endo A, Simoni RD: Isolation and characterization of cells resistant to ML236B (compactin) with increased levels of HMG-CoA reductase. J Biol Chem 1981, 256:6762-6768.
    • (1981) J Biol Chem , vol.256 , pp. 6762-6768
    • Ryan, J.1    Hardeman, E.C.2    Endo, A.3    Simoni, R.D.4
  • 60
    • 0141646834 scopus 로고
    • Appearance of crystalloid endoplasmic reticulum in compactin-resistant Chinese hamster cells with a 500-fold increase in HMG-CoA reductase
    • Chin DJ, Luskey KL, Anderson RGW, Faust JR, Goldstein JL, Brown MS: Appearance of crystalloid endoplasmic reticulum in compactin-resistant Chinese hamster cells with a 500-fold increase in HMG-CoA reductase. Proc Natl Acad Sci U S A 1982, 80:1185-1189.
    • (1982) Proc Natl Acad Sci U S A , vol.80 , pp. 1185-1189
    • Chin, D.J.1    Luskey, K.L.2    Anderson, R.G.W.3    Faust, J.R.4    Goldstein, J.L.5    Brown, M.S.6
  • 61
    • 0023654088 scopus 로고
    • Expression of specific high capacity mevalonate transport in a CHO cell variant
    • Faust JA, Krieger M: Expression of specific high capacity mevalonate transport in a CHO cell variant. J Biol Chem 1987, 262:1996-2004.
    • (1987) J Biol Chem , vol.262 , pp. 1996-2004
    • Faust, J.A.1    Krieger, M.2
  • 62
    • 0026463075 scopus 로고
    • cDNA cloning of MEV, a mutant protein that facilitates cellular uptake of mevalonate, and identification of the point mutation responsible for its gain of function
    • Kim C, Goldstein JL, Brown MS: cDNA cloning of MEV, a mutant protein that facilitates cellular uptake of mevalonate, and identification of the point mutation responsible for its gain of function. J Biol Chem 1992, 267:23113-23121.
    • (1992) J Biol Chem , vol.267 , pp. 23113-23121
    • Kim, C.1    Goldstein, J.L.2    Brown, M.S.3
  • 63
    • 0023002621 scopus 로고
    • Inhibition of acyl coenzyme A: Cholesterol acyltransferase in J774 macrophages enhances down-regulation of the LDL receptor and HMG-CoA reductase and prevents LDL-induced cholesterol accumulation
    • Tabas I, Weiland DA, Tall AR: Inhibition of acyl coenzyme A: cholesterol acyltransferase in J774 macrophages enhances down-regulation of the LDL receptor and HMG-CoA reductase and prevents LDL-induced cholesterol accumulation. J Biol Chem 1986, 261:3147-3155.
    • (1986) J Biol Chem , vol.261 , pp. 3147-3155
    • Tabas, I.1    Weiland, D.A.2    Tall, A.R.3
  • 64
    • 0024383782 scopus 로고
    • Isolation of Chinese hamster ovary cell lines expressing human acyl-coenzyme A : Cholesterol acyltransferase activity
    • Cadigan KM, Chang CCY, Chang TY: Isolation of Chinese hamster ovary cell lines expressing human acyl-coenzyme A : cholesterol acyltransferase activity. J Cell Biol 1989, 108:2201-2210.
    • (1989) J Cell Biol , vol.108 , pp. 2201-2210
    • Cadigan, K.M.1    Chang, C.C.Y.2    Chang, T.Y.3
  • 65
    • 0027527733 scopus 로고
    • Molecular cloning and functional expression of human acyl-coenzyme A : Cholesterol acyltransferase cDNA in mutant Chinese hamster ovary cells
    • Chang CCY, Huh HY, Cadigan KM, Chang TY: Molecular cloning and functional expression of human acyl-coenzyme A : cholesterol acyltransferase cDNA in mutant Chinese hamster ovary cells. J Biol Chem 1993, 268:20747-20755.
    • (1993) J Biol Chem , vol.268 , pp. 20747-20755
    • Chang, C.C.Y.1    Huh, H.Y.2    Cadigan, K.M.3    Chang, T.Y.4
  • 66
    • 0028865098 scopus 로고
    • Tissue-specific expression and cholesterol regulation of acyl coenzyme A : Cholesterol acyltransferase (ACAT) in mice: molecular cloning of mouse ACAT cDNA, chromosomal localization, and regulation of ACAT in vivo and in vitro
    • Uelmen PJ, Oka K, Sullivan M, Chang CCY, Chang TY, Chan L: Tissue-specific expression and cholesterol regulation of acyl coenzyme A : cholesterol acyltransferase (ACAT) in mice: molecular cloning of mouse ACAT cDNA, chromosomal localization, and regulation of ACAT in vivo and in vitro. J Biol Chem 1995, 270:26192-26201.
    • (1995) J Biol Chem , vol.270 , pp. 26192-26201
    • Uelmen, P.J.1    Oka, K.2    Sullivan, M.3    Chang, C.C.Y.4    Chang, T.Y.5    Chan, L.6
  • 67
    • 0028800470 scopus 로고
    • Regulation and localization of acyl coenzyme A: Cholesterol acyltransferase (ACAT) in cultured mammalian cells with specific antibodies
    • Chang CCY, Chen J, Thomas MA, Cheng D, Del Priore VA, Newton RS, Pape ME, Chang TY: Regulation and localization of acyl coenzyme A: cholesterol acyltransferase (ACAT) in cultured mammalian cells with specific antibodies. J Biol Chem 1995, 270:29532-29540.
    • (1995) J Biol Chem , vol.270 , pp. 29532-29540
    • Chang, C.C.Y.1    Chen, J.2    Thomas, M.A.3    Cheng, D.4    Del Priore, V.A.5    Newton, R.S.6    Pape, M.E.7    Chang, T.Y.8
  • 68
    • 0028928737 scopus 로고
    • Activation of acyl coenzyme A: Cholesterol acyltransferase by cholesterol or by oxysterol in a cell-free system
    • Cheng D, Chang CCY, Qu XM, Chang TY: Activation of acyl coenzyme A: cholesterol acyltransferase by cholesterol or by oxysterol in a cell-free system. J Biol Chem 1995, 270:685-695.
    • (1995) J Biol Chem , vol.270 , pp. 685-695
    • Cheng, D.1    Chang, C.C.Y.2    Qu, X.M.3    Chang, T.Y.4
  • 70
    • 0025173761 scopus 로고
    • Isolation and characterization of Chinese hamster ovary cell mutants defective in intracellular low density lipoprotein-cholesterol trafficking
    • Cadigan KM, Spillane DM, Chang TY: Isolation and characterization of Chinese hamster ovary cell mutants defective in intracellular low density lipoprotein-cholesterol trafficking. J Cell Biol 1990, 110:295-308.
    • (1990) J Cell Biol , vol.110 , pp. 295-308
    • Cadigan, K.M.1    Spillane, D.M.2    Chang, T.Y.3
  • 71
    • 0026738867 scopus 로고
    • Isolation and characterization of Chinese hamster ovary cells defective in the intracellular metabolism of low density lipoprotein-derived cholesterol
    • Dahl NK, Reed KL, Daunais MA, Faust JR, Liscum L: Isolation and characterization of Chinese hamster ovary cells defective in the intracellular metabolism of low density lipoprotein-derived cholesterol. J Biol Chem 1992, 267:4889-4896.
    • (1992) J Biol Chem , vol.267 , pp. 4889-4896
    • Dahl, N.K.1    Reed, K.L.2    Daunais, M.A.3    Faust, J.R.4    Liscum, L.5
  • 72
    • 0028021083 scopus 로고
    • A second complementation class of cholesterol transport mutants with a variant Niemann-Pick type C phenotype
    • Dahl NK, Daunais MA, Liscum L: A second complementation class of cholesterol transport mutants with a variant Niemann-Pick type C phenotype. J Lipid Res 1994, 35:1839-1849.
    • (1994) J Lipid Res , vol.35 , pp. 1839-1849
    • Dahl, N.K.1    Daunais, M.A.2    Liscum, L.3
  • 73
    • 8244246637 scopus 로고
    • Isolation and characterization of CHO cell lines possessing abnormal LDL-derived cholesterol trafficking
    • Spillane DM: Isolation and characterization of CHO cell lines possessing abnormal LDL-derived cholesterol trafficking [PhD thesis]. Dartmouth College; 1993.
    • (1993) Dartmouth College
    • Spillane, D.M.1
  • 74
    • 0028854617 scopus 로고
    • Translocation of both lysosomal LDL-derived cholesterol and plasma membrane cholesterol to the endoplasmic reticulum for esterification may require common cellular factors present in the acidic compartment(s)
    • Spillane DM, Reagan JW, Kennedy NJ, Schneider DL, Chang TY: Translocation of both lysosomal LDL-derived cholesterol and plasma membrane cholesterol to the endoplasmic reticulum for esterification may require common cellular factors present in the acidic compartment(s). Biochim Biophys Acta 1995, 1254:283-294.
    • (1995) Biochim Biophys Acta , vol.1254 , pp. 283-294
    • Spillane, D.M.1    Reagan, J.W.2    Kennedy, N.J.3    Schneider, D.L.4    Chang, T.Y.5
  • 77
    • 0023608155 scopus 로고
    • Low density lipoprotein (LDL)-mediated supression of cholesterol synthesis and LDL uptake is defective in Niemann-Pick fibroblasts
    • Liscum L, Faust JR: Low density lipoprotein (LDL)-mediated supression of cholesterol synthesis and LDL uptake is defective in Niemann-Pick fibroblasts. J Biol Chem 1987, 262:17002-17008.
    • (1987) J Biol Chem , vol.262 , pp. 17002-17008
    • Liscum, L.1    Faust, J.R.2
  • 78
    • 0026739685 scopus 로고
    • Intracellular cholesterol transport
    • Liscum L, Dahl NK: Intracellular cholesterol transport. J Lipid Res 1992, 33:1239-1254.
    • (1992) J Lipid Res , vol.33 , pp. 1239-1254
    • Liscum, L.1    Dahl, N.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.