메뉴 건너뛰기




Volumn 7, Issue 1-2, 2007, Pages 80-88

CHOP (C/EBP homologous protein) and ASNS (asparagine synthetase) induction in cybrid cells harboring MELAS and NARP mitochondrial DNA mutations

Author keywords

ASNS; CHOP; DNA microarray; MELAS; Mitochondrial dysfunction; NARP

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ADENOSINE TRIPHOSPHATASE; ARGININE; ASPARTATE AMMONIA LIGASE; CCAAT ENHANCER BINDING PROTEIN; CYTOSINE; MESSENGER RNA; MITOCHONDRIAL DNA; THYMINE; TRANSFER RNA;

EID: 33847653346     PISSN: 15677249     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mito.2006.11.003     Document Type: Article
Times cited : (30)

References (45)
  • 1
    • 1242272070 scopus 로고    scopus 로고
    • Induction of CHOP expression by amino acid limitation requires both ATF4 expression and ATF2 phosphorylation
    • Averous J., Bruhat A., Jousse C., Carraro V., Thiel G., and Fafournoux P. Induction of CHOP expression by amino acid limitation requires both ATF4 expression and ATF2 phosphorylation. J. Biol. Chem. 279 (2004) 5288-5297
    • (2004) J. Biol. Chem. , vol.279 , pp. 5288-5297
    • Averous, J.1    Bruhat, A.2    Jousse, C.3    Carraro, V.4    Thiel, G.5    Fafournoux, P.6
  • 2
    • 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. 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 (2000) 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
  • 3
    • 0037073799 scopus 로고    scopus 로고
    • Differences in the molecular mechanisms involved in the transcriptional activation of the CHOP and asparagine synthetase genes in response to amino acid deprivation or activation of the unfolded protein response
    • Bruhat A., Averous J., Carraro V., Zhong C., Reimold A.M., Kilberg M.S., and Fafournoux P. Differences in the molecular mechanisms involved in the transcriptional activation of the CHOP and asparagine synthetase genes in response to amino acid deprivation or activation of the unfolded protein response. J. Biol. Chem. 277 (2002) 48107-48114
    • (2002) J. Biol. Chem. , vol.277 , pp. 48107-48114
    • Bruhat, A.1    Averous, J.2    Carraro, V.3    Zhong, C.4    Reimold, A.M.5    Kilberg, M.S.6    Fafournoux, P.7
  • 4
    • 4644329647 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species control the transcription factor CHOP-10/GADD153 and adipocyte differentiation: a mechanism for hypoxia-dependent effect
    • Carriere A., Carmona M.C., Fernandez Y., Rigoulet M., Wenger R.H., Penicaud L., and Casteilla L. Mitochondrial reactive oxygen species control the transcription factor CHOP-10/GADD153 and adipocyte differentiation: a mechanism for hypoxia-dependent effect. J. Biol. Chem. 279 (2004) 40462-40469
    • (2004) J. Biol. Chem. , vol.279 , pp. 40462-40469
    • Carriere, A.1    Carmona, M.C.2    Fernandez, Y.3    Rigoulet, M.4    Wenger, R.H.5    Penicaud, L.6    Casteilla, L.7
  • 5
    • 0023392945 scopus 로고
    • High-efficiency transformation of mammalian cells by plasmid DNA
    • Chen C., and Okayama H. High-efficiency transformation of mammalian cells by plasmid DNA. Mol. Cell. Biol. 7 (1987) 2745-2752
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2745-2752
    • Chen, C.1    Okayama, H.2
  • 6
    • 0026608057 scopus 로고
    • MELAS mutation in mtDNA binding site for transcription termination factor causes defects in protein synthesis and in respiration but no change in levels of upstream and downstream mature transcripts
    • Chomyn A., Martinuzzi A., Yoneda M., Daga A., Hurko O., Johns D., Lai S.T., Nonaka I., Angelini C., and Attardi G. MELAS mutation in mtDNA binding site for transcription termination factor causes defects in protein synthesis and in respiration but no change in levels of upstream and downstream mature transcripts. Proc. Natl. Acad. Sci. USA 89 (1992) 4221-4225
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4221-4225
    • Chomyn, A.1    Martinuzzi, A.2    Yoneda, M.3    Daga, A.4    Hurko, O.5    Johns, D.6    Lai, S.T.7    Nonaka, I.8    Angelini, C.9    Attardi, G.10
  • 8
    • 0034306249 scopus 로고    scopus 로고
    • Amino acid regulation of gene expression
    • Fafournoux P., Bruhat A., and Jousse C. Amino acid regulation of gene expression. Biochem. J. 351 (2000) 1-12
    • (2000) Biochem. J. , vol.351 , pp. 1-12
    • Fafournoux, P.1    Bruhat, A.2    Jousse, C.3
  • 9
    • 0034646642 scopus 로고    scopus 로고
    • Structure, functioning, and assembly of the ATP synthase in cells from patients with the T8993G mitochondrial DNA mutation. Comparison with the enzyme in Rho(0) cells completely lacking mtDNA
    • Garcia J.J., Ogilvie I., Robinson B.H., and Capaldi R.A. Structure, functioning, and assembly of the ATP synthase in cells from patients with the T8993G mitochondrial DNA mutation. Comparison with the enzyme in Rho(0) cells completely lacking mtDNA. J. Biol. Chem. 275 (2000) 11075-11081
    • (2000) J. Biol. Chem. , vol.275 , pp. 11075-11081
    • Garcia, J.J.1    Ogilvie, I.2    Robinson, B.H.3    Capaldi, R.A.4
  • 10
    • 0025666322 scopus 로고
    • A mutation in the tRNA(Leu)(UUR) gene associated with the MELAS subgroup of mitochondrial encephalomyopathies
    • Goto Y., Nonaka I., and Horai S. A mutation in the tRNA(Leu)(UUR) gene associated with the MELAS subgroup of mitochondrial encephalomyopathies. Nature 348 (1990) 651-653
    • (1990) Nature , vol.348 , pp. 651-653
    • Goto, Y.1    Nonaka, I.2    Horai, S.3
  • 11
    • 0029927983 scopus 로고    scopus 로고
    • Induction of the mammalian stress response gene GADD153 by oxidative stress: role of AP-1 element
    • Guyton K.Z., Xu Q., and Holbrook N.J. Induction of the mammalian stress response gene GADD153 by oxidative stress: role of AP-1 element. Biochem. J. 314 Pt 2 (1996) 547-554
    • (1996) Biochem. J. , vol.314 , Issue.PART 2 , pp. 547-554
    • Guyton, K.Z.1    Xu, Q.2    Holbrook, N.J.3
  • 12
    • 0033634654 scopus 로고    scopus 로고
    • Regulated translation initiation controls stress-induced gene expression in mammalian cells
    • Harding H.P., Novoa I., Zhang Y., Zeng H., Wek R., Schapira M., and Ron D. Regulated translation initiation controls stress-induced gene expression in mammalian cells. Mol. Cell 6 (2000) 1099-1108
    • (2000) Mol. Cell , vol.6 , pp. 1099-1108
    • Harding, H.P.1    Novoa, I.2    Zhang, Y.3    Zeng, H.4    Wek, R.5    Schapira, M.6    Ron, D.7
  • 13
    • 0025267548 scopus 로고
    • A new mitochondrial disease associated with mitochondrial DNA heteroplasmy
    • Holt I.J., Harding A.E., Petty R.K., and Morgan-Hughes J.A. A new mitochondrial disease associated with mitochondrial DNA heteroplasmy. Am. J. Hum. Genet. 46 (1990) 428-433
    • (1990) Am. J. Hum. Genet. , vol.46 , pp. 428-433
    • Holt, I.J.1    Harding, A.E.2    Petty, R.K.3    Morgan-Hughes, J.A.4
  • 16
    • 0029790507 scopus 로고    scopus 로고
    • Altered mitochondrial function in fibroblasts containing MELAS or MERRF mitochondrial DNA mutations
    • James A.M., Wei Y.H., Pang C.Y., and Murphy M.P. Altered mitochondrial function in fibroblasts containing MELAS or MERRF mitochondrial DNA mutations. Biochem. J. 318 Pt 2 (1996) 401-407
    • (1996) Biochem. J. , vol.318 , Issue.PART 2 , pp. 401-407
    • James, A.M.1    Wei, Y.H.2    Pang, C.Y.3    Murphy, M.P.4
  • 17
    • 17144389838 scopus 로고    scopus 로고
    • Phosphorylation of the alpha-subunit of the eukaryotic initiation factor-2 (eIF2alpha) reduces protein synthesis and enhances apoptosis in response to proteasome inhibition
    • Jiang H.Y., and Wek R.C. Phosphorylation of the alpha-subunit of the eukaryotic initiation factor-2 (eIF2alpha) reduces protein synthesis and enhances apoptosis in response to proteasome inhibition. J. Biol. Chem. 280 (2005) 14189-14202
    • (2005) J. Biol. Chem. , vol.280 , pp. 14189-14202
    • Jiang, H.Y.1    Wek, R.C.2
  • 19
    • 6344221310 scopus 로고    scopus 로고
    • Codon-specific translational defect caused by a wobble modification deficiency in mutant tRNA from a human mitochondrial disease
    • Kirino Y., Yasukawa T., Ohta S., Akira S., Ishihara K., Watanabe K., and Suzuki T. Codon-specific translational defect caused by a wobble modification deficiency in mutant tRNA from a human mitochondrial disease. Proc. Natl. Acad. Sci. USA 101 (2004) 15070-15075
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 15070-15075
    • Kirino, Y.1    Yasukawa, T.2    Ohta, S.3    Akira, S.4    Ishihara, K.5    Watanabe, K.6    Suzuki, T.7
  • 21
    • 0037424245 scopus 로고    scopus 로고
    • Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production
    • Li N., Ragheb K., Lawler G., Sturgis J., Rajwa B., Melendez J.A., and Robinson J.P. Mitochondrial complex I inhibitor rotenone induces apoptosis through enhancing mitochondrial reactive oxygen species production. J. Biol. Chem. 278 (2003) 8516-8525
    • (2003) J. Biol. Chem. , vol.278 , pp. 8516-8525
    • Li, N.1    Ragheb, K.2    Lawler, G.3    Sturgis, J.4    Rajwa, B.5    Melendez, J.A.6    Robinson, J.P.7
  • 22
    • 5444264022 scopus 로고    scopus 로고
    • Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response
    • Lu P.D., Harding H.P., and Ron D. Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response. J. Cell. Biol. 167 (2004) 27-33
    • (2004) J. Cell. Biol. , vol.167 , pp. 27-33
    • Lu, P.D.1    Harding, H.P.2    Ron, D.3
  • 24
    • 0035794142 scopus 로고    scopus 로고
    • Impaired ATP synthase assembly associated with a mutation in the human ATP synthase subunit 6 gene
    • Nijtmans L.G., Henderson N.S., Attardi G., and Holt I.J. Impaired ATP synthase assembly associated with a mutation in the human ATP synthase subunit 6 gene. J. Biol. Chem. 276 (2001) 6755-6762
    • (2001) J. Biol. Chem. , vol.276 , pp. 6755-6762
    • Nijtmans, L.G.1    Henderson, N.S.2    Attardi, G.3    Holt, I.J.4
  • 25
    • 0021143782 scopus 로고
    • Mitochondrial myopathy, encephalopathy, lactic acidosis, and strokelike episodes: a distinctive clinical syndrome
    • Pavlakis S.G., Phillips P.C., DiMauro S., De Vivo D.C., and Rowland L.P. Mitochondrial myopathy, encephalopathy, lactic acidosis, and strokelike episodes: a distinctive clinical syndrome. Ann. Neurol. 16 (1984) 481-488
    • (1984) Ann. Neurol. , vol.16 , pp. 481-488
    • Pavlakis, S.G.1    Phillips, P.C.2    DiMauro, S.3    De Vivo, D.C.4    Rowland, L.P.5
  • 26
    • 0036310982 scopus 로고    scopus 로고
    • The immunosuppressant rapamycin mimics a starvation-like signal distinct from amino acid and glucose deprivation
    • Peng T., Golub T.R., and Sabatini D.M. The immunosuppressant rapamycin mimics a starvation-like signal distinct from amino acid and glucose deprivation. Mol. Cell. Biol. 22 (2002) 5575-5584
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5575-5584
    • Peng, T.1    Golub, T.R.2    Sabatini, D.M.3
  • 27
    • 0036856008 scopus 로고    scopus 로고
    • Translational control in the endoplasmic reticulum stress response
    • Ron D. Translational control in the endoplasmic reticulum stress response. J. Clin. Invest. 110 (2002) 1383-1388
    • (2002) J. Clin. Invest. , vol.110 , pp. 1383-1388
    • Ron, D.1
  • 28
    • 0033990284 scopus 로고    scopus 로고
    • Increased activities of antioxidant enzymes and decreased ATP concentration in cultured myoblasts with the 3243A->G mutation in mitochondrial DNA
    • Rusanen H., Majamaa K., and Hassinen I.E. Increased activities of antioxidant enzymes and decreased ATP concentration in cultured myoblasts with the 3243A->G mutation in mitochondrial DNA. Biochim. Biophys. Acta 1500 (2000) 10-16
    • (2000) Biochim. Biophys. Acta , vol.1500 , pp. 10-16
    • Rusanen, H.1    Majamaa, K.2    Hassinen, I.E.3
  • 30
    • 27444447841 scopus 로고    scopus 로고
    • Effects of nitric oxide donors on cybrids harbouring the mitochondrial myopathy, encephalopathy, lactic acidosis and stroke-like episodes (MELAS) A3243G mitochondrial DNA mutation
    • Sandhu J.K., Sodja C., McRae K., Li Y., Rippstein P., Wei Y.H., Lach B., Lee F., Bucurescu S., Harper M.E., and Sikorska M. Effects of nitric oxide donors on cybrids harbouring the mitochondrial myopathy, encephalopathy, lactic acidosis and stroke-like episodes (MELAS) A3243G mitochondrial DNA mutation. Biochem. J. 391 (2005) 191-202
    • (2005) Biochem. J. , vol.391 , pp. 191-202
    • Sandhu, J.K.1    Sodja, C.2    McRae, K.3    Li, Y.4    Rippstein, P.5    Wei, Y.H.6    Lach, B.7    Lee, F.8    Bucurescu, S.9    Harper, M.E.10    Sikorska, M.11
  • 32
    • 0035930599 scopus 로고    scopus 로고
    • CCAAT/enhancer-binding protein-beta is a mediator of the nutrient-sensing response pathway that activates the human asparagine synthetase gene
    • Siu F., Chen C., Zhong C., and Kilberg M.S. CCAAT/enhancer-binding protein-beta is a mediator of the nutrient-sensing response pathway that activates the human asparagine synthetase gene. J. Biol. Chem. 276 (2001) 48100-48107
    • (2001) J. Biol. Chem. , vol.276 , pp. 48100-48107
    • Siu, F.1    Chen, C.2    Zhong, C.3    Kilberg, M.S.4
  • 33
    • 0037025396 scopus 로고    scopus 로고
    • ATF4 is a mediator of the nutrient-sensing response pathway that activates the human asparagine synthetase gene
    • Siu F., Bain P.J., LeBlanc-Chaffin R., Chen H., and Kilberg M.S. ATF4 is a mediator of the nutrient-sensing response pathway that activates the human asparagine synthetase gene. J. Biol. Chem. 277 (2002) 24120-24127
    • (2002) J. Biol. Chem. , vol.277 , pp. 24120-24127
    • Siu, F.1    Bain, P.J.2    LeBlanc-Chaffin, R.3    Chen, H.4    Kilberg, M.S.5
  • 34
    • 0033962298 scopus 로고    scopus 로고
    • A mammalian homologue of GCN2 protein kinase important for translational control by phosphorylation of eukaryotic initiation factor-2alpha
    • Sood R., Porter A.C., Olsen D.A., Cavener D.R., and Wek R.C. A mammalian homologue of GCN2 protein kinase important for translational control by phosphorylation of eukaryotic initiation factor-2alpha. Genetics 154 (2000) 787-801
    • (2000) Genetics , vol.154 , pp. 787-801
    • Sood, R.1    Porter, A.C.2    Olsen, D.A.3    Cavener, D.R.4    Wek, R.C.5
  • 39
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • Turrens J.F., and Boveris A. Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem. J. 191 (1980) 421-427
    • (1980) Biochem. J. , vol.191 , pp. 421-427
    • Turrens, J.F.1    Boveris, A.2
  • 40
    • 0034635519 scopus 로고    scopus 로고
    • Modification defect at anticodon wobble nucleotide of mitochondrial tRNAs(Leu)(UUR) with pathogenic mutations of mitochondrial myopathy, encephalopathy, lactic acidosis, and stroke-like episodes
    • Yasukawa T., Suzuki T., Ueda T., Ohta S., and Watanabe K. Modification defect at anticodon wobble nucleotide of mitochondrial tRNAs(Leu)(UUR) with pathogenic mutations of mitochondrial myopathy, encephalopathy, lactic acidosis, and stroke-like episodes. J. Biol. Chem. 275 (2000) 4251-4257
    • (2000) J. Biol. Chem. , vol.275 , pp. 4251-4257
    • Yasukawa, T.1    Suzuki, T.2    Ueda, T.3    Ohta, S.4    Watanabe, K.5
  • 42
    • 0028348251 scopus 로고
    • Complementation of mutant and wild-type human mitochondrial DNAs coexisting since the mutation event and lack of complementation of DNAs introduced separately into a cell within distinct organelles
    • Yoneda M., Miyatake T., and Attardi G. Complementation of mutant and wild-type human mitochondrial DNAs coexisting since the mutation event and lack of complementation of DNAs introduced separately into a cell within distinct organelles. Mol. Cell. Biol. 14 (1994) 2699-2712
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2699-2712
    • Yoneda, M.1    Miyatake, T.2    Attardi, G.3
  • 43
    • 0033815971 scopus 로고    scopus 로고
    • ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response
    • Yoshida H., Okada T., Haze K., Yanagi H., Yura T., Negishi M., and Mori K. ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response. Mol. Cell. Biol. 20 (2000) 6755-6767
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6755-6767
    • Yoshida, H.1    Okada, T.2    Haze, K.3    Yanagi, H.4    Yura, T.5    Negishi, M.6    Mori, K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.