메뉴 건너뛰기




Volumn 369, Issue 3, 2003, Pages 643-650

Inhibition of phosphatidylcholine synthesis induces expression of the endoplasmic reticulum stress and apoptosis-related protein CCAAT/enhancer-binding protein-homologous protein (CHOP/GADD153)

Author keywords

BiP GRP78; CHO mutant MT58; CTP:phosphocholine cytidylyltransferase

Indexed keywords

CELLS; DRUG THERAPY; ENZYMES; SYNTHESIS (CHEMICAL);

EID: 0037330932     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20020285     Document Type: Article
Times cited : (79)

References (58)
  • 1
    • 0028296793 scopus 로고
    • Phosphatidylcholine breakdown and signal transduction
    • Exton, J. H. (1994) Phosphatidylcholine breakdown and signal transduction. Biochim. Biophys. Acta 1212, 26-42
    • (1994) Biochim. Biophys. Acta , vol.1212 , pp. 26-42
    • Exton, J.H.1
  • 2
    • 0024392736 scopus 로고
    • Sphingomyelin synthase and PKC activation
    • Hampton, R. Y. and Morand, O. H. (1989) Sphingomyelin synthase and PKC activation. Science 246, 1050-1054
    • (1989) Science , vol.246 , pp. 1050-1054
    • Hampton, R.Y.1    Morand, O.H.2
  • 3
    • 0028855405 scopus 로고
    • Ceramide: An intracellular signal for apoptosis
    • Hannun, Y. A. and Obeid, L. M. (1995) Ceramide: an intracellular signal for apoptosis. Trends Biochem. Sci. 20, 73-77
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 73-77
    • Hannun, Y.A.1    Obeid, L.M.2
  • 4
    • 0029026637 scopus 로고
    • Eukaryotic phospholipid biosynthesis
    • Kent, C. (1995) Eukaryotic phospholipid biosynthesis. Annu. Rev. Biochem. 64, 315-343
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 315-343
    • Kent, C.1
  • 5
    • 0025610139 scopus 로고
    • Regulation of phosphatidylcholine biosynthesis
    • Kent, C. (1990) Regulation of phosphatidylcholine biosynthesis. Progr. Lipid Res. 29, 87-105
    • (1990) Progr. Lipid Res. , vol.29 , pp. 87-105
    • Kent, C.1
  • 6
    • 0033578749 scopus 로고    scopus 로고
    • Distribution of CTP:Phosphocholine cytidylyltransferase (CCT) isoforms. Identification of a new CCTβ splice variant
    • Lykidis, A., Baburina, I. and Jackowski, S. (1999) Distribution of CTP:phosphocholine cytidylyltransferase (CCT) isoforms. Identification of a new CCTβ splice variant. J. Biol. Chem. 274, 26992-27001
    • (1999) J. Biol. Chem. , vol.274 , pp. 26992-27001
    • Lykidis, A.1    Baburina, I.2    Jackowski, S.3
  • 7
    • 0034284083 scopus 로고    scopus 로고
    • Regulation of CTP:Phosphocholine cytidylyltransferase by amphitropism and relocalization
    • Cornell, R. B. and Northwood, I. C. (2000) Regulation of CTP:phosphocholine cytidylyltransferase by amphitropism and relocalization. Trends Biochem. Sci. 25, 441-447
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 441-447
    • Cornell, R.B.1    Northwood, I.C.2
  • 8
    • 0031553042 scopus 로고    scopus 로고
    • CTP:Phosphocholine cytidylyltransferase
    • Kent, C. (1997) CTP:phosphocholine cytidylyltransferase. Biochim. Biophys. Acta 1348, 79-90
    • (1997) Biochim. Biophys. Acta , vol.1348 , pp. 79-90
    • Kent, C.1
  • 9
    • 0029833954 scopus 로고    scopus 로고
    • Structure of the membrane binding domain of CTP:Phosphocholine cytidylyltransferase
    • Dunne, S. J., Cornell, R. B., Johnson, J. E., Glover, N. R. and Tracey, A. S. (1996) Structure of the membrane binding domain of CTP:phosphocholine cytidylyltransferase. Biochemistry 35, 11975-11984
    • (1996) Biochemistry , vol.35 , pp. 11975-11984
    • Dunne, S.J.1    Cornell, R.B.2    Johnson, J.E.3    Glover, N.R.4    Tracey, A.S.5
  • 10
    • 0028302144 scopus 로고
    • Phosphatidylcholine cycle and regulation of phosphatidylcholine biosynthesis by enzyme translocation
    • Tronchere, H., Record, M., Terce, F. and Chap, H. (1994) Phosphatidylcholine cycle and regulation of phosphatidylcholine biosynthesis by enzyme translocation. Biochim. Biophys. Acta 1212, 137-151
    • (1994) Biochim. Biophys. Acta , vol.1212 , pp. 137-151
    • Tronchere, H.1    Record, M.2    Terce, F.3    Chap, H.4
  • 11
    • 77956689688 scopus 로고    scopus 로고
    • The glycerolipid biosynthesis in eukaryotes
    • Vance, D. E. and Vance, J., eds., Elsevier, Amsterdam
    • Vance, D. E. (1996) The glycerolipid biosynthesis in eukaryotes. In Biochemistry of Lipids, Lipoproteins and Membranes, 3rd edn (Vance, D. E. and Vance, J., eds.), pp. 153-181, Elsevier, Amsterdam
    • (1996) Biochemistry of Lipids, Lipoproteins and Membranes, 3rd Edn , pp. 153-181
    • Vance, D.E.1
  • 12
    • 0025951209 scopus 로고
    • Colony-stimulating factor 1 regulates CTP: Phosphocholine cytidylyltransferase mRNA levels
    • Tessner, T. G., Rock, C. O., Kalmar, G. B., Cornell, R. B. and Jackowski, S. (1991) Colony-stimulating factor 1 regulates CTP: phosphocholine cytidylyltransferase mRNA levels. J. Biol. Chem. 266, 16261-16264
    • (1991) J. Biol. Chem. , vol.266 , pp. 16261-16264
    • Tessner, T.G.1    Rock, C.O.2    Kalmar, G.B.3    Cornell, R.B.4    Jackowski, S.5
  • 13
    • 0031708952 scopus 로고    scopus 로고
    • How cytidylyltransferase uses an amphipathic helix to sense membrane phospholipid composition
    • Cornel, R. B. (1998) How cytidylyltransferase uses an amphipathic helix to sense membrane phospholipid composition Biochem. Soc. Trans. 26, 539-544
    • (1998) Biochem. Soc. Trans. , vol.26 , pp. 539-544
    • Cornel, R.B.1
  • 14
    • 0029786402 scopus 로고    scopus 로고
    • Cell cycle regulation of membrane phospholipid metabolism
    • Jackowski, S. (1996) Cell cycle regulation of membrane phospholipid metabolism. J. Biol. Chem. 271, 20219-20222
    • (1996) J. Biol. Chem. , vol.271 , pp. 20219-20222
    • Jackowski, S.1
  • 15
    • 0031892176 scopus 로고    scopus 로고
    • Apoptosis triggered by 1-O-octadecyl-2-O-methyl-rac-glycero-3-phosphocholine is prevented by increased expression of CTP:Phosphocholine cytidylyltransferase
    • Baburina, I. and Jackowski, S. (1998) Apoptosis triggered by 1-O-octadecyl-2-O-methyl-rac-glycero-3-phosphocholine is prevented by increased expression of CTP:phosphocholine cytidylyltransferase. J. Biol. Chem. 273, 2169-2173
    • (1998) J. Biol. Chem. , vol.273 , pp. 2169-2173
    • Baburina, I.1    Jackowski, S.2
  • 16
    • 15844389625 scopus 로고    scopus 로고
    • A genetic defect in phosphatidylcholine biosynthesis triggers apoptosis in Chinese hamster ovary cells
    • Cui, Z., Houweling, M., Chen, M. H., Record, M., Chap, H., Vance, D. E. and Terce, F. (1996) A genetic defect in phosphatidylcholine biosynthesis triggers apoptosis in Chinese hamster ovary cells. J. Biol. Chem. 271, 14668-14671
    • (1996) J. Biol. Chem. , vol.271 , pp. 14668-14671
    • Cui, Z.1    Houweling, M.2    Chen, M.H.3    Record, M.4    Chap, H.5    Vance, D.E.6    Terce, F.7
  • 17
    • 0028146621 scopus 로고
    • Coordination of membrane phospholipid synthesis with the cell cycle
    • Jackowski, S. (1994) Coordination of membrane phospholipid synthesis with the cell cycle. J. Biol. Chem. 269, 3858-3867
    • (1994) J. Biol. Chem. , vol.269 , pp. 3858-3867
    • Jackowski, S.1
  • 18
    • 0032484590 scopus 로고    scopus 로고
    • The antiproliferative effect of hexadecylphosphocholine toward HL60 cells is prevented by exogenous lysophosphatidylcholine
    • Boggs, K., Rock, C. O. and Jackowski, S. (1998) The antiproliferative effect of hexadecylphosphocholine toward HL60 cells is prevented by exogenous lysophosphatidylcholine. Biochim. Biophys. Acta 1389, 1-12
    • (1998) Biochim. Biophys. Acta , vol.1389 , pp. 1-12
    • Boggs, K.1    Rock, C.O.2    Jackowski, S.3
  • 19
    • 0032079477 scopus 로고    scopus 로고
    • Induction of ceramide-mediated apoptosis by the anticancer phospholipid analog, hexadecylphosphocholine
    • Wieder, T., Orfanos, C. E. and Geiler, C. C. (1998) Induction of ceramide-mediated apoptosis by the anticancer phospholipid analog, hexadecylphosphocholine. J. Biol. Chem. 273, 11025-11031
    • (1998) J. Biol. Chem. , vol.273 , pp. 11025-11031
    • Wieder, T.1    Orfanos, C.E.2    Geiler, C.C.3
  • 20
    • 0033538462 scopus 로고    scopus 로고
    • Inhibition of phosphatidylcholine biosynthesis following induction of apoptosis in HL-60 cells
    • Anthony, M. L., Zhao, M. and Brindle, K. M. (1999) Inhibition of phosphatidylcholine biosynthesis following induction of apoptosis in HL-60 cells. J. Biol. Chem. 274, 19686-19692
    • (1999) J. Biol. Chem. , vol.274 , pp. 19686-19692
    • Anthony, M.L.1    Zhao, M.2    Brindle, K.M.3
  • 21
    • 0032476029 scopus 로고    scopus 로고
    • Competitive inhibition of choline phosphotransferase by geranylgeraniol and farnesol inhibits phosphatidylcholine synthesis and induces apoptosis in human lung adenocarcinoma A549 cells
    • Miquel, K., Pradines, A., Terce, F., Selmi, S. and Favre, G. (1998) Competitive inhibition of choline phosphotransferase by geranylgeraniol and farnesol inhibits phosphatidylcholine synthesis and induces apoptosis in human lung adenocarcinoma A549 cells. J. Biol. Chem 273, 26179-26186
    • (1998) J. Biol. Chem. , vol.273 , pp. 26179-26186
    • Miquel, K.1    Pradines, A.2    Terce, F.3    Selmi, S.4    Favre, G.5
  • 22
    • 0019966917 scopus 로고
    • Animal cells dependent on exogenous phosphatidylcholine for membrane biogenesis
    • Esko, J. D., Nishijima, M. and Raetz, C. R. (1982) Animal cells dependent on exogenous phosphatidylcholine for membrane biogenesis. Proc. Natl. Acad. Sci. U.S.A. 79, 1698-1702
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 1698-1702
    • Esko, J.D.1    Nishijima, M.2    Raetz, C.R.3
  • 23
    • 0019888255 scopus 로고
    • Thermolabile CDP-choline synthetase in an animal cell mutant defective in lecithin formation
    • Esko, J. D., Wermuth, M. M. and Raetz, C. R. (1981) Thermolabile CDP-choline synthetase in an animal cell mutant defective in lecithin formation. J. Biol. Chem. 256, 7388-7393
    • (1981) J. Biol. Chem. , vol.256 , pp. 7388-7393
    • Esko, J.D.1    Wermuth, M.M.2    Raetz, C.R.3
  • 24
    • 0019061277 scopus 로고
    • Autoradiographic detection of animal cell membrane mutants altered in phosphatidylcholine synthesis
    • Esko, J. D. and Raetz, C. R. (1980) Autoradiographic detection of animal cell membrane mutants altered in phosphatidylcholine synthesis. Proc. Natl. Acad. Sci U.S.A. 77, 5192-5196
    • (1980) Proc. Natl. Acad. Sci U.S.A. , vol.77 , pp. 5192-5196
    • Esko, J.D.1    Raetz, C.R.2
  • 25
    • 0028260451 scopus 로고
    • Effect of amino acid limitation on the expression of 19 genes in rat hepatoma cells
    • Marten, N. W., Burke, E. J., Hayden, J. M. and Straus, D. S. (1994) Effect of amino acid limitation on the expression of 19 genes in rat hepatoma cells. FASEB J. 8, 538-544
    • (1994) FASEB J. , vol.8 , pp. 538-544
    • Marten, N.W.1    Burke, E.J.2    Hayden, J.M.3    Straus, D.S.4
  • 26
    • 0030971176 scopus 로고    scopus 로고
    • The molecular response to reductive stress in LLC-PK1 renal epithelial cells: Coordinate transcriptional regulation of gadd153 and grp78 genes by thiols
    • Halleck, M. M., Holbrook, N. J., Skinner, J., Liu, H. and Stevens, J. L. (1997) The molecular response to reductive stress in LLC-PK1 renal epithelial cells: coordinate transcriptional regulation of gadd153 and grp78 genes by thiols. Cell Stress. Chaperones 2, 31-40
    • (1997) Cell Stress. Chaperones , vol.2 , pp. 31-40
    • Halleck, M.M.1    Holbrook, N.J.2    Skinner, J.3    Liu, H.4    Stevens, J.L.5
  • 27
    • 0026843954 scopus 로고
    • Mammalian stress response: Induction of the glucose-regulated protein family
    • Lee, A. S. (1992) Mammalian stress response: induction of the glucose-regulated protein family. Curr. Opin. Cell Biol. 4, 267-273
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 267-273
    • Lee, A.S.1
  • 28
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: Coordination of gene transcriptional and translational controls
    • Kaufman, R. J. (1999) Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev. 13, 1211-1233
    • (1999) Genes Dev. , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 29
    • 0023852783 scopus 로고
    • The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins
    • Kozutsumi, Y., Segal, M., Normington, K., Gething, M. J. and Sambrook, J. (1988) The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins. Nature (London) 332, 462-464
    • (1988) Nature (London) , vol.332 , pp. 462-464
    • Kozutsumi, Y.1    Segal, M.2    Normington, K.3    Gething, M.J.4    Sambrook, J.5
  • 30
    • 0024400060 scopus 로고
    • Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP)
    • Hurtley, S. M., Bole, D. G., Hoover-Litty, H., Helenius, A. and Copeland, C. S. (1989) Interactions of misfolded influenza virus hemagglutinin with binding protein (BiP). J. Cell Biol. 108, 2117-2126
    • (1989) J. Cell Biol. , vol.108 , pp. 2117-2126
    • Hurtley, S.M.1    Bole, D.G.2    Hoover-Litty, H.3    Helenius, A.4    Copeland, C.S.5
  • 31
    • 0034716887 scopus 로고    scopus 로고
    • Tripartite management of unfolded proteins in the endoplasmic reticulum
    • Mori, K. (2000) Tripartite management of unfolded proteins in the endoplasmic reticulum. Cell 101, 451-454
    • (2000) Cell , vol.101 , pp. 451-454
    • Mori, K.1
  • 32
    • 0033408418 scopus 로고    scopus 로고
    • Heat-shock protein 70 antisense oligomers enhance proteasome inhibitor-induced apoptosis
    • Robertson, J. D., Datta, K., Biswal, S. S. and Kehrer, J. P. (1999) Heat-shock protein 70 antisense oligomers enhance proteasome inhibitor-induced apoptosis. Biochem. J. 344, 477-485
    • (1999) Biochem. J. , vol.344 , pp. 477-485
    • Robertson, J.D.1    Datta, K.2    Biswal, S.S.3    Kehrer, J.P.4
  • 33
    • 0030739208 scopus 로고    scopus 로고
    • Role of the human heat shock protein HSP 70 in protection against stress-induced apoptosis
    • Mosser, D. D., Caron, A. W., Bourget, L., Denis-Larose, C. and Massie, B. (1997) Role of the human heat shock protein HSP 70 in protection against stress-induced apoptosis. Mol Cell Biol. 17, 5317-5327
    • (1997) Mol Cell Biol. , vol.17 , pp. 5317-5327
    • Mosser, D.D.1    Caron, A.W.2    Bourget, L.3    Denis-Larose, C.4    Massie, B.5
  • 34
    • 0032476668 scopus 로고    scopus 로고
    • HSP 70 exerts its anti-apoptotic function downstream of caspase-3-like proteases
    • Jaattela, M., Wissing, D., Kokholm, K., Kallunki, T. and Egeblad, M. (1998) HSP 70 exerts its anti-apoptotic function downstream of caspase-3-like proteases. EMBO J. 17, 6124-6134
    • (1998) EMBO J. , vol.17 , pp. 6124-6134
    • Jaattela, M.1    Wissing, D.2    Kokholm, K.3    Kallunki, T.4    Egeblad, M.5
  • 35
  • 36
    • 0026546365 scopus 로고
    • CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcription
    • Ron, D. and Habener, J. F. (1992) CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcription Genes Dev. 6, 439-453
    • (1992) Genes Dev. , vol.6 , pp. 439-453
    • Ron, D.1    Habener, J.F.2
  • 40
    • 0026611735 scopus 로고
    • Brefeldin A, thapsigargin, and AIF4-stimulate the accumulation of GRP78 mRNA in a cycloheximide dependent manner, whilst induction by hypoxia is independent of protein synthesis
    • Price, B. D., Mannheim-Rodman, L. A. and Calderwood, S. K. (1992) Brefeldin A, thapsigargin, and AIF4-stimulate the accumulation of GRP78 mRNA in a cycloheximide dependent manner, whilst induction by hypoxia is independent of protein synthesis. J. Cell Physiol. 152, 545-552
    • (1992) J. Cell Physiol. , vol.152 , pp. 545-552
    • Price, B.D.1    Mannheim-Rodman, L.A.2    Calderwood, S.K.3
  • 41
    • 0030803278 scopus 로고    scopus 로고
    • Fas- or ceramide-induced apoptosis is mediated by a Rac1-regulated activation of Jun N-terminal kinase/p38 kinases and GADD153
    • Brenner, B., Koppenhoefer, U., Weinstock, C., Linderkamp, O., Lang, F. and Gulbins, E. (1997) Fas- or ceramide-induced apoptosis is mediated by a Rac1-regulated activation of Jun N-terminal kinase/p38 kinases and GADD153. J. Biol. Chem. 272, 22173-22181
    • (1997) J. Biol. Chem. , vol.272 , pp. 22173-22181
    • Brenner, B.1    Koppenhoefer, U.2    Weinstock, C.3    Linderkamp, O.4    Lang, F.5    Gulbins, E.6
  • 42
    • 0029938805 scopus 로고    scopus 로고
    • Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP kinase
    • Wang, X. Z. and Ron, D. (1996) Stress-induced phosphorylation and activation of the transcription factor CHOP (GADD153) by p38 MAP kinase. Science 272, 1347-1349
    • (1996) Science , vol.272 , pp. 1347-1349
    • Wang, X.Z.1    Ron, D.2
  • 43
    • 0029928173 scopus 로고    scopus 로고
    • Stress-induced binding of the transcriptional factor CHOP to a novel DNA control element
    • Ubeda, M., Wang, X. Z., Zinszner, H., Wu, I., Habener, J. F. and Ron, D. (1996) Stress-induced binding of the transcriptional factor CHOP to a novel DNA control element. Mol. Cell. Biol. 16, 1479-1489
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1479-1489
    • Ubeda, M.1    Wang, X.Z.2    Zinszner, H.3    Wu, I.4    Habener, J.F.5    Ron, D.6
  • 44
    • 0033830234 scopus 로고    scopus 로고
    • Amino acids control mammalian gene transcription: Activating transcription factor 2 is essential for the amino acid responsiveness of the CHOP promoter
    • Bruhat, A., Jousse, C., Carraro, V., Reimold, A. M., Ferrara, M. and Fafournoux, P. (2000) Amino acids control mammalian gene transcription: activating transcription factor 2 is essential for the amino acid responsiveness of the CHOP promoter. Mol. Cell. Biol. 20, 7192-7204
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 7192-7204
    • Bruhat, A.1    Jousse, C.2    Carraro, V.3    Reimold, A.M.4    Ferrara, M.5    Fafournoux, P.6
  • 45
    • 0034671837 scopus 로고    scopus 로고
    • CHOP gene expression in response to endoplasmic-reticular stress requires NFY interaction with different domains of a conserved DNA-binding element
    • Ubeda, M. and Habener, J. F. (2000) CHOP gene expression in response to endoplasmic-reticular stress requires NFY interaction with different domains of a conserved DNA-binding element. Nucleic Acids Res. 28, 4987-4997
    • (2000) Nucleic Acids Res. , vol.28 , pp. 4987-4997
    • Ubeda, M.1    Habener, J.F.2
  • 47
    • 0035957929 scopus 로고    scopus 로고
    • Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress
    • Yoneda, T., Imaizumi, K., Oono, K., Yui, D., Gomi, F., Katayama, T. and Tohyama, M. (2001) Activation of caspase-12, an endoplastic reticulum (ER) resident caspase, through tumor necrosis factor receptor-associated factor 2-dependent mechanism in response to the ER stress. J. Biol. Chem. 276, 13935-13940
    • (2001) J. Biol. Chem. , vol.276 , pp. 13935-13940
    • Yoneda, T.1    Imaizumi, K.2    Oono, K.3    Yui, D.4    Gomi, F.5    Katayama, T.6    Tohyama, M.7
  • 48
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β
    • Nakagawa, T., Zhu, H., Morishima, N., Li, E., Xu, J., Yankner, B. A. and Yuan, J. (2000) Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β. Nature (London) 403, 98-103
    • (2000) Nature (London) , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 49
    • 0033590451 scopus 로고    scopus 로고
    • Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
    • Harding, H. P., Zhang, Y. and Ron, D. (1999) Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase Nature (London) 397, 271-274
    • (1999) Nature (London) , vol.397 , pp. 271-274
    • Harding, H.P.1    Zhang, Y.2    Ron, D.3
  • 50
    • 0029003018 scopus 로고
    • Expression of phosphatidylethanolamine N-methyltransferase-2 cannot compensate for an impaired CDP-choline pathway in mutant Chinese hamster ovary cells
    • Houweling, M., Cui, Z. and Vance, D. E. (1995) Expression of phosphatidylethanolamine N-methyltransferase-2 cannot compensate for an impaired CDP-choline pathway in mutant Chinese hamster ovary cells. J. Biol. Chem. 270, 16277-16282
    • (1995) J. Biol. Chem. , vol.270 , pp. 16277-16282
    • Houweling, M.1    Cui, Z.2    Vance, D.E.3
  • 51
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh, E. G. and Dyer, W. J. (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
  • 52
    • 51649179265 scopus 로고
    • Quantitative analysis of phospholipids by thin-layer chromatography and phosphorus analysis of spots
    • Rouser, G. S., Siakotos, A. N. and Fleisscher, S. (1966) Quantitative analysis of phospholipids by thin-layer chromatography and phosphorus analysis of spots. Lipids 1, 85-86
    • (1966) Lipids , vol.1 , pp. 85-86
    • Rouser, G.S.1    Siakotos, A.N.2    Fleisscher, S.3
  • 53
    • 0028291124 scopus 로고
    • Expression of wild-type and mutant rat liver CTP:Phosphocholine cytidylyltransferase in a cytidylyltransferase-deficient Chinese hamster ovary cell line
    • Sweitzer, T. D. and Kent, C. (1994) Expression of wild-type and mutant rat liver CTP:phosphocholine cytidylyltransferase in a cytidylyltransferase-deficient Chinese hamster ovary cell line. Arch. Biochem. Biophys. 311, 107-116
    • (1994) Arch. Biochem. Biophys. , vol.311 , pp. 107-116
    • Sweitzer, T.D.1    Kent, C.2
  • 54
    • 0029901711 scopus 로고    scopus 로고
    • GADD153/CHOP, a DNA damage-inducible protein, reduced CAAT/enhancer binding protein activities and increased apoptosis in 32D c13 myeloid cells
    • Friedman, A. D. (1996) GADD153/CHOP, a DNA damage-inducible protein, reduced CAAT/enhancer binding protein activities and increased apoptosis in 32D c13 myeloid cells. Cancer Res. 56, 3250-3256
    • (1996) Cancer Res. , vol.56 , pp. 3250-3256
    • Friedman, A.D.1
  • 55
    • 0026632457 scopus 로고
    • Gadd45 and Gadd153 messenger RNA levels are increased during hypoxia and after exposure of cells to agents which elevate the levels of the glucose-regulated proteins
    • Price, B. D. and Calderwood, S. K. (1992) Gadd45 and Gadd153 messenger RNA levels are increased during hypoxia and after exposure of cells to agents which elevate the levels of the glucose-regulated proteins. Cancer Res. 52, 3814-3817
    • (1992) Cancer Res. , vol.52 , pp. 3814-3817
    • Price, B.D.1    Calderwood, S.K.2
  • 56
    • 0036713724 scopus 로고    scopus 로고
    • Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response
    • Okada, T., Yoshida, H., Akazawa, R., Negishi, M. and Mori, K. (2002) Distinct roles of activating transcription factor 6 (ATF6) and double-stranded RNA-activated protein kinase-like endoplasmic reticulum kinase (PERK) in transcription during the mammalian unfolded protein response. Biochem. J. 366, 585-594
    • (2002) Biochem. J. , vol.366 , pp. 585-594
    • Okada, T.1    Yoshida, H.2    Akazawa, R.3    Negishi, M.4    Mori, K.5
  • 57
    • 0032920099 scopus 로고    scopus 로고
    • Amino acid limitation regulates CHOP expression through a specific pathway independent of the unfolded protein response
    • Jousse, C., Bruhat, A., Harding, H. P., Ferrara, M., Ron, D. and Fafournoux, P. (1999) Amino acid limitation regulates CHOP expression through a specific pathway independent of the unfolded protein response. FEBS Lett. 448, 211-216
    • (1999) FEBS Lett. , vol.448 , pp. 211-216
    • Jousse, C.1    Bruhat, A.2    Harding, H.P.3    Ferrara, M.4    Ron, D.5    Fafournoux, P.6
  • 58
    • 0033214640 scopus 로고    scopus 로고
    • Glutamine deprivation induces the expression of GADD45 and GADD153 primarily by mRNA stabilization
    • Abcouwer, S. F., Schwarz, C. and Meguid, R. A. (1999) Glutamine deprivation induces the expression of GADD45 and GADD153 primarily by mRNA stabilization. J. Biol. Chem. 274, 28645-28651
    • (1999) J. Biol. Chem. , vol.274 , pp. 28645-28651
    • Abcouwer, S.F.1    Schwarz, C.2    Meguid, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.