메뉴 건너뛰기




Volumn 289, Issue 32, 2014, Pages 22413-22426

Heavy metal-induced metallothionein expression is regulated by specific protein phosphatase 2A complexes

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; BIOLOGY;

EID: 84905841279     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.548677     Document Type: Article
Times cited : (64)

References (60)
  • 1
    • 3242774357 scopus 로고    scopus 로고
    • Hazards of heavy metal contamination
    • Järup, L. (2003) Hazards of heavy metal contamination. Br. Med. Bull. 68, 167-182
    • (2003) Br. Med. Bull. , vol.68 , pp. 167-182
    • Järup, L.1
  • 2
    • 79954642381 scopus 로고    scopus 로고
    • Advances in metal-induced oxidative stress and human disease
    • Jomova, K., and Valko, M. (2011) Advances in metal-induced oxidative stress and human disease. Toxicology 283, 65-87
    • (2011) Toxicology , vol.283 , pp. 65-87
    • Jomova, K.1    Valko, M.2
  • 3
    • 81555227899 scopus 로고    scopus 로고
    • Heavy metal poisoning and cardiovascular disease
    • Alissa, E. M., and Ferns, G. A. (2011) Heavy metal poisoning and cardiovascular disease. J. Toxicol. 2011, 870125
    • (2011) J. Toxicol. , vol.2011 , pp. 870125
    • Alissa, E.M.1    Ferns, G.A.2
  • 4
    • 79955911056 scopus 로고    scopus 로고
    • Cancer mortality in a Chinese population surrounding a multi-metal sulphide mine in Guangdong province: An ecologic study
    • Wang, M., Song, H., Chen, W. Q., Lu, C., Hu, Q., Ren, Z., Yang, Y., Xu, Y., Zhong, A., and Ling, W. (2011) Cancer mortality in a Chinese population surrounding a multi-metal sulphide mine in Guangdong province: an ecologic study. BMC Public Health 11, 319
    • (2011) BMC Public Health , vol.11 , pp. 319
    • Wang, M.1    Song, H.2    Chen, W.Q.3    Lu, C.4    Hu, Q.5    Ren, Z.6    Yang, Y.7    Xu, Y.8    Zhong, A.9    Ling, W.10
  • 5
    • 80051792291 scopus 로고    scopus 로고
    • Long-term heavy metal pollution and mortalitioy in a Chinese population: An ecologic study
    • Wang, M., Xu, Y., Pan, S., Zhang, J., Zhong, A., Song, H., and Ling, W. (2011) Long-term heavy metal pollution and mortalitioy in a Chinese population: an ecologic study. Biol. Trace Elem. Res. 142, 362-379
    • (2011) Biol. Trace Elem. Res. , vol.142 , pp. 362-379
    • Wang, M.1    Xu, Y.2    Pan, S.3    Zhang, J.4    Zhong, A.5    Song, H.6    Ling, W.7
  • 6
    • 68749108412 scopus 로고    scopus 로고
    • Behavioural development of schoolaged children who live around a multi-metal sulphide mine in Guangdong province, China: A cross-sectional study
    • Bao, Q. S., Lu, C. Y., Song, H., Wang, M., Ling, W., Chen, W. Q., Deng, X. Q., Hao, Y. T., and Rao, S. (2009) Behavioural development of schoolaged children who live around a multi-metal sulphide mine in Guangdong province, China: a cross-sectional study. BMC Public Health 9, 217
    • (2009) BMC Public Health , vol.9 , pp. 217
    • Bao, Q.S.1    Lu, C.Y.2    Song, H.3    Wang, M.4    Ling, W.5    Chen, W.Q.6    Deng, X.Q.7    Hao, Y.T.8    Rao, S.9
  • 7
    • 18544371009 scopus 로고    scopus 로고
    • Metals, toxicity, and oxidative stress
    • Valko, M., Morris, H., and Cronin, M. T. (2005) Metals, toxicity, and oxidative stress. Curr. Med. Chem. 12, 1161-1208
    • (2005) Curr. Med. Chem. , vol.12 , pp. 1161-1208
    • Valko, M.1    Morris, H.2    Cronin, M.T.3
  • 8
    • 0019483405 scopus 로고
    • Transcriptional regulation of the mouse metallothionein-I gene by heavy metals
    • Durnam, D. M., and Palmiter, R. D. (1981) Transcriptional regulation of the mouse metallothionein-I gene by heavy metals. J. Biol. Chem. 256, 5712-5716
    • (1981) J. Biol. Chem. , vol.256 , pp. 5712-5716
    • Durnam, D.M.1    Palmiter, R.D.2
  • 9
    • 0034859756 scopus 로고    scopus 로고
    • Metal response element (MRE)-binding transcription factor-1 (MTF-1): Structure, function, and regulation
    • Giedroc, D. P., Chen, X., and Apuy, J. L. (2001) Metal response element (MRE)-binding transcription factor-1 (MTF-1): structure, function, and regulation. Antioxid. Redox Signal. 3, 577-596
    • (2001) Antioxid. Redox Signal. , vol.3 , pp. 577-596
    • Giedroc, D.P.1    Chen, X.2    Apuy, J.L.3
  • 10
    • 34047233414 scopus 로고    scopus 로고
    • Heavy metal responses of the human metallothionein isoform genes
    • Miura, N., and Koizumi, S. (2007) Heavy metal responses of the human metallothionein isoform genes. Yakugaku Zasshi 127, 665-673
    • (2007) Yakugaku Zasshi , vol.127 , pp. 665-673
    • Miura, N.1    Koizumi, S.2
  • 11
    • 0036200075 scopus 로고    scopus 로고
    • Metallothionein 2A expression is associated with cell proliferation in breast cancer
    • Jin, R., Chow, V. T., Tan, P. H., Dheen, S. T., Duan, W., and Bay, B. H. (2002) Metallothionein 2A expression is associated with cell proliferation in breast cancer. Carcinogenesis 23, 81-86
    • (2002) Carcinogenesis , vol.23 , pp. 81-86
    • Jin, R.1    Chow, V.T.2    Tan, P.H.3    Dheen, S.T.4    Duan, W.5    Bay, B.H.6
  • 12
    • 0031133179 scopus 로고    scopus 로고
    • Antisense down-regulation of metallothionein induces growth arrest and apoptosis in human breast carcinoma cells
    • Abdel-Mageed, A., and Agrawal, K. C. (1997) Antisense down-regulation of metallothionein induces growth arrest and apoptosis in human breast carcinoma cells. Cancer Gene Ther. 4, 199-207
    • (1997) Cancer Gene Ther. , vol.4 , pp. 199-207
    • Abdel-Mageed, A.1    Agrawal, K.C.2
  • 13
    • 0032953164 scopus 로고    scopus 로고
    • Metallothionein: An intracellular protein to protect against cadmium toxicity
    • Klaassen, C. D., Liu, J., and Choudhuri, S. (1999) Metallothionein: an intracellular protein to protect against cadmium toxicity. Annu. Rev. Pharmacol. Toxicol. 39, 267-294
    • (1999) Annu. Rev. Pharmacol. Toxicol. , vol.39 , pp. 267-294
    • Klaassen, C.D.1    Liu, J.2    Choudhuri, S.3
  • 14
    • 0023076963 scopus 로고
    • Role of metallothionein in detoxification and tolerance to transition metals
    • Huang, P. C., Morris, S., Dinman, J., Pine, R., and Smith, B. (1987) Role of metallothionein in detoxification and tolerance to transition metals. Experientia Suppl. 52, 439-446
    • (1987) Experientia Suppl. , vol.52 , pp. 439-446
    • Huang, P.C.1    Morris, S.2    Dinman, J.3    Pine, R.4    Smith, B.5
  • 15
    • 0020525253 scopus 로고
    • Altered subcellular distribution of cadmium following cadmium pretreatment: Possible mechanism of tolerance to cadmium-induced lethality
    • Goering, P. L., and Klaassen, C. D. (1983) Altered subcellular distribution of cadmium following cadmium pretreatment: possible mechanism of tolerance to cadmium-induced lethality. Toxicol. Appl. Pharmacol. 70, 195-203
    • (1983) Toxicol. Appl. Pharmacol. , vol.70 , pp. 195-203
    • Goering, P.L.1    Klaassen, C.D.2
  • 16
    • 0035927936 scopus 로고    scopus 로고
    • Protective effect of metallothionein against the toxicity of cadmium and other metals (1)
    • Park, J. D., Liu, Y., and Klaassen, C. D. (2001) Protective effect of metallothionein against the toxicity of cadmium and other metals (1). Toxicology 163, 93-100
    • (2001) Toxicology , vol.163 , pp. 93-100
    • Park, J.D.1    Liu, Y.2    Klaassen, C.D.3
  • 19
    • 80054756410 scopus 로고    scopus 로고
    • Metallothionein as potential biomarker of cadmium exposure in Persian sturgeon (Acipenser persicus)
    • Shariati, F., Esaili Sari, A., Mashinchian, A., and Pourkazemi, M. (2011) Metallothionein as potential biomarker of cadmium exposure in Persian sturgeon (Acipenser persicus). Biol. Trace Elem. Res. 143, 281-291
    • (2011) Biol. Trace Elem. Res. , vol.143 , pp. 281-291
    • Shariati, F.1    Esaili Sari, A.2    Mashinchian, A.3    Pourkazemi, M.4
  • 20
    • 34047224835 scopus 로고    scopus 로고
    • Metallothionein gene and protein expression as a biomarker for metal pollution in natural gudgeon populations
    • Knapen, D., Reynders, H., Bervoets, L., Verheyen, E., and Blust, R. (2007) Metallothionein gene and protein expression as a biomarker for metal pollution in natural gudgeon populations. Aquat. Toxicol. 82, 163-172
    • (2007) Aquat. Toxicol. , vol.82 , pp. 163-172
    • Knapen, D.1    Reynders, H.2    Bervoets, L.3    Verheyen, E.4    Blust, R.5
  • 21
    • 0345276583 scopus 로고    scopus 로고
    • Signaling events for metallothionein induction
    • Haq, F., Mahoney, M., and Koropatnick, J. (2003) Signaling events for metallothionein induction. Mutat. Res. 533, 211-226
    • (2003) Mutat. Res. , vol.533 , pp. 211-226
    • Haq, F.1    Mahoney, M.2    Koropatnick, J.3
  • 23
    • 0033990794 scopus 로고    scopus 로고
    • Regulation of metallothionein gene expression by oxidative stress and metal ions
    • Andrews, G. K. (2000) Regulation of metallothionein gene expression by oxidative stress and metal ions. Biochem. Pharmacol. 59, 95-104
    • (2000) Biochem. Pharmacol. , vol.59 , pp. 95-104
    • Andrews, G.K.1
  • 24
    • 0037036433 scopus 로고    scopus 로고
    • Regulation of metallothionein transcription by the metal-responsive transcription factor MTF-1: Identification of signal transduction cascades that control metal-inducible transcription
    • Saydam, N., Adams, T. K., Steiner, F., Schaffner, W., and Freedman, J. H. (2002) Regulation of metallothionein transcription by the metal-responsive transcription factor MTF-1: identification of signal transduction cascades that control metal-inducible transcription. J. Biol. Chem. 277, 20438-20445
    • (2002) J. Biol. Chem. , vol.277 , pp. 20438-20445
    • Saydam, N.1    Adams, T.K.2    Steiner, F.3    Schaffner, W.4    Freedman, J.H.5
  • 25
    • 0035834763 scopus 로고    scopus 로고
    • Phosphorylation is involved in the activation of metal-regulatory transcription factor 1 in response to metal ions
    • LaRochelle, O., Gagné, V., Charron, J., Soh, J. W., and Séguin, C. (2001) Phosphorylation is involved in the activation of metal-regulatory transcription factor 1 in response to metal ions. J. Biol. Chem. 276, 41879-41888
    • (2001) J. Biol. Chem. , vol.276 , pp. 41879-41888
    • Larochelle, O.1    Gagné, V.2    Charron, J.3    Soh, J.W.4    Séguin, C.5
  • 26
    • 0029834655 scopus 로고    scopus 로고
    • The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm
    • McCright, B., Rivers, A. M., Audlin, S., and Virshup, D. M. (1996) The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm. J. Biol. Chem. 271, 22081-22089
    • (1996) J. Biol. Chem. , vol.271 , pp. 22081-22089
    • McCright, B.1    Rivers, A.M.2    Audlin, S.3    Virshup, D.M.4
  • 27
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
    • Janssens, V., and Goris, J. (2001) Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem. J. 353, 417-439
    • (2001) Biochem. J. , vol.353 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 29
    • 67650237693 scopus 로고    scopus 로고
    • Tap42-associated protein phosphatase type 2A negatively regulates induction of autophagy
    • Yorimitsu, T., He, C., Wang, K., and Klionsky, D. J. (2009) Tap42-associated protein phosphatase type 2A negatively regulates induction of autophagy. Autophagy 5, 616-624
    • (2009) Autophagy , vol.5 , pp. 616-624
    • Yorimitsu, T.1    He, C.2    Wang, K.3    Klionsky, D.J.4
  • 30
    • 27944448894 scopus 로고    scopus 로고
    • Involvement of PP2A in viral and cellular transformation
    • Arroyo, J. D., and Hahn, W. C. (2005) Involvement of PP2A in viral and cellular transformation. Oncogene 24, 7746-7755
    • (2005) Oncogene , vol.24 , pp. 7746-7755
    • Arroyo, J.D.1    Hahn, W.C.2
  • 31
    • 0034009389 scopus 로고    scopus 로고
    • Protein phosphatase 2A: A panoply of enzymes
    • Virshup, D. M. (2000) Protein phosphatase 2A: a panoply of enzymes. Curr Opin Cell Biol. 12, 180-185
    • (2000) Curr Opin Cell Biol. , vol.12 , pp. 180-185
    • Virshup, D.M.1
  • 32
  • 33
    • 1042304324 scopus 로고    scopus 로고
    • Correlation of thymidylate synthase, thymidine phosphorylase, and dihydropyrimidine dehydrogenase with sensitivity of gastrointestinal cancer cells to 5-fluorouracil and 5-fluoro-2-deoxyuridine
    • Ma, T., Zhu, Z. G., Ji, Y. B., Zhang, Y., Yu, Y. Y., Liu, B. Y., Yin, H. R., and Lin, Y. Z. (2004) Correlation of thymidylate synthase, thymidine phosphorylase, and dihydropyrimidine dehydrogenase with sensitivity of gastrointestinal cancer cells to 5-fluorouracil and 5-fluoro-2-deoxyuridine. World J. Gastroenterol. 10, 172-176
    • (2004) World J. Gastroenterol. , vol.10 , pp. 172-176
    • Ma, T.1    Zhu, Z.G.2    Ji, Y.B.3    Zhang, Y.4    Yu, Y.Y.5    Liu, B.Y.6    Yin, H.R.7    Lin, Y.Z.8
  • 34
    • 0025794340 scopus 로고
    • Metallothionein induction in human peripheral blood lymphocytes by heavy metals
    • Yamada, H., and Koizumi, S. (1991) Metallothionein induction in human peripheral blood lymphocytes by heavy metals. Chem. Biol. Interact. 78, 347-354
    • (1991) Chem. Biol. Interact. , vol.78 , pp. 347-354
    • Yamada, H.1    Koizumi, S.2
  • 36
    • 0028358324 scopus 로고
    • The transcription factor MTF-1 is essential for basal and heavy metal-induced metallothionein gene expression
    • Heuchel, R., Radtke, F., Georgiev, O., Stark, G., Aguet, M., and Schaffner, W. (1994) The transcription factor MTF-1 is essential for basal and heavy metal-induced metallothionein gene expression. EMBO J. 13, 2870-2875
    • (1994) EMBO J. , vol.13 , pp. 2870-2875
    • Heuchel, R.1    Radtke, F.2    Georgiev, O.3    Stark, G.4    Aguet, M.5    Schaffner, W.6
  • 37
    • 84893737590 scopus 로고    scopus 로고
    • The role of Nrf1 and Nrf2 in the regulation of copper-responsive transcription
    • Song, M. O., Mattie, M. D., Lee, C. H., and Freedman, J. H. (2014) The role of Nrf1 and Nrf2 in the regulation of copper-responsive transcription. Exp. Cell Res. 322, 39-50
    • (2014) Exp. Cell Res. , vol.322 , pp. 39-50
    • Song, M.O.1    Mattie, M.D.2    Lee, C.H.3    Freedman, J.H.4
  • 38
    • 0035816670 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic trafficking of metal-regulatory transcription factor 1 is regulated by diverse stress signals
    • Saydam, N., Georgiev, O., Nakano, M. Y., Greber, U. F., and Schaffner, W. (2001) Nucleo-cytoplasmic trafficking of metal-regulatory transcription factor 1 is regulated by diverse stress signals. J. Biol. Chem. 276, 25487-25495
    • (2001) J. Biol. Chem. , vol.276 , pp. 25487-25495
    • Saydam, N.1    Georgiev, O.2    Nakano, M.Y.3    Greber, U.F.4    Schaffner, W.5
  • 39
    • 0034737599 scopus 로고    scopus 로고
    • Zinc and cadmium can promote rapid nuclear translocation of metal response element-binding transcription factor-1
    • Smirnova, I. V., Bittel, D. C., Ravindra, R., Jiang, H., and Andrews, G. K. (2000) Zinc and cadmium can promote rapid nuclear translocation of metal response element-binding transcription factor-1. J. Biol. Chem. 275, 9377-9384
    • (2000) J. Biol. Chem. , vol.275 , pp. 9377-9384
    • Smirnova, I.V.1    Bittel, D.C.2    Ravindra, R.3    Jiang, H.4    Andrews, G.K.5
  • 41
    • 4344716723 scopus 로고    scopus 로고
    • Gene-and cell-type-specific effects of signal transduction cascades on metal-regulated gene transcription appear to be independent of changes in the phosphorylation of metalresponse-element-binding transcription factor-1
    • Jiang, H., Fu, K., and Andrews, G. K. (2004) Gene-and cell-type-specific effects of signal transduction cascades on metal-regulated gene transcription appear to be independent of changes in the phosphorylation of metalresponse-element-binding transcription factor-1. Biochem. J. 382, 33-41
    • (2004) Biochem. J. , vol.382 , pp. 33-41
    • Jiang, H.1    Fu, K.2    Andrews, G.K.3
  • 42
    • 0029858934 scopus 로고    scopus 로고
    • Metallothionein is a component of exocrine pancreas secretion: Implications for zinc homeostasis
    • De Lisle, R. C., Sarras, M. P., Jr., Hidalgo, J., and Andrews, G. K. (1996) Metallothionein is a component of exocrine pancreas secretion: implications for zinc homeostasis. Am. J. Physiol. 271, C1103-C1110
    • (1996) Am. J. Physiol. , vol.271
    • De Lisle, R.C.1    Sarras Jr., M.P.2    Hidalgo, J.3    Andrews, G.K.4
  • 45
    • 0347683430 scopus 로고    scopus 로고
    • Metallothionein protects islets from hypoxia and extends islet graft survival by scavenging most kinds of reactive oxygen species
    • Li, X., Chen, H., and Epstein, P. N. (2004) Metallothionein protects islets from hypoxia and extends islet graft survival by scavenging most kinds of reactive oxygen species. J. Biol. Chem. 279, 765-771
    • (2004) J. Biol. Chem. , vol.279 , pp. 765-771
    • Li, X.1    Chen, H.2    Epstein, P.N.3
  • 46
    • 0032796684 scopus 로고    scopus 로고
    • Oyster metallothionein as an oxyradical scavenger: Implications for hemocyte defense responses
    • Anderson, R. S., Patel, K. M., and Roesijadi, G. (1999) Oyster metallothionein as an oxyradical scavenger: implications for hemocyte defense responses. Dev. Comp. Immunol. 23, 443-449
    • (1999) Dev. Comp. Immunol. , vol.23 , pp. 443-449
    • Anderson, R.S.1    Patel, K.M.2    Roesijadi, G.3
  • 47
    • 0027759612 scopus 로고
    • Metallothionein in human lung carcinoma
    • Hart, B. A., Voss, G. W., and Vacek, P. M. (1993) Metallothionein in human lung carcinoma. Cancer Lett. 75, 121-128
    • (1993) Cancer Lett. , vol.75 , pp. 121-128
    • Hart, B.A.1    Voss, G.W.2    Vacek, P.M.3
  • 49
    • 70450231904 scopus 로고    scopus 로고
    • Heavy metals in the fishery products of low Lazio and the use of metallothionein as a biomarker of contamination
    • Papetti, P., and Rossi, G. (2009) Heavy metals in the fishery products of low Lazio and the use of metallothionein as a biomarker of contamination. Environ. Monit. Assess. 159, 589-598
    • (2009) Environ. Monit. Assess. , vol.159 , pp. 589-598
    • Papetti, P.1    Rossi, G.2
  • 50
    • 0028125990 scopus 로고
    • Regulation of metallothionein genes by heavy metals appears to be mediated by a zinc-sensitive inhibitor that interacts with a constitutively active transcription factor, MTF-1
    • Palmiter, R. D. (1994) Regulation of metallothionein genes by heavy metals appears to be mediated by a zinc-sensitive inhibitor that interacts with a constitutively active transcription factor, MTF-1. Proc. Natl. Acad. Sci. U.S.A. 91, 1219-1223
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 1219-1223
    • Palmiter, R.D.1
  • 51
    • 0038813724 scopus 로고    scopus 로고
    • Regulation of estrogen receptor-mediated transcription by a direct interaction with protein phosphatase 2A
    • Lu, Q., Surks, H. K., Ebling, H., Baur, W. E., Brown, D., Pallas, D. C., and Karas, R. H. (2003) Regulation of estrogen receptor-mediated transcription by a direct interaction with protein phosphatase 2A. J. Biol. Chem. 278, 4639-4645
    • (2003) J. Biol. Chem. , vol.278 , pp. 4639-4645
    • Lu, Q.1    Surks, H.K.2    Ebling, H.3    Baur, W.E.4    Brown, D.5    Pallas, D.C.6    Karas, R.H.7
  • 52
    • 10344237581 scopus 로고    scopus 로고
    • Striatin assembles a membrane signaling complex necessary for rapid, nongenomic activation of endothelialNOsynthase by estrogen receptor
    • Lu, Q., Pallas, D. C., Surks, H. K., Baur, W. E., Mendelsohn, M. E., and Karas, R. H. (2004) Striatin assembles a membrane signaling complex necessary for rapid, nongenomic activation of endothelialNOsynthase by estrogen receptor. Proc. Natl. Acad. Sci. U.S.A. 101, 17126-17131
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 17126-17131
    • Lu, Q.1    Pallas, D.C.2    Surks, H.K.3    Baur, W.E.4    Mendelsohn, M.E.5    Karas, R.H.6
  • 54
    • 0035172754 scopus 로고    scopus 로고
    • Molecular cloning and characterization of phocein, a protein found from the Golgi complex to dendritic spines
    • Baillat, G., Moqrich, A., Castets, F., Baude, A., Bailly, Y., Benmerah, A., and Monneron, A. (2001) Molecular cloning and characterization of phocein, a protein found from the Golgi complex to dendritic spines. Mol. Biol. Cell 12, 663-673
    • (2001) Mol. Biol. Cell , vol.12 , pp. 663-673
    • Baillat, G.1    Moqrich, A.2    Castets, F.3    Baude, A.4    Bailly, Y.5    Benmerah, A.6    Monneron, A.7
  • 55
    • 0035968296 scopus 로고    scopus 로고
    • Amammalian homolog of yeast MOB1 is both a member and a putative substrate of striatin family-protein phosphatase 2A complexes
    • Moreno, C. S., Lane, W. S., and Pallas, D. C. (2001)Amammalian homolog of yeast MOB1 is both a member and a putative substrate of striatin family-protein phosphatase 2A complexes. J. Biol. Chem. 276, 24253-24260
    • (2001) J. Biol. Chem. , vol.276 , pp. 24253-24260
    • Moreno, C.S.1    Lane, W.S.2    Pallas, D.C.3
  • 56
    • 34047263219 scopus 로고    scopus 로고
    • Metallothionein expression is suppressed in primary human hepatocellular carcinomas and is mediated through inactivation of CCAAT/enhancer binding protein α by phosphatidylinositol 3-kinase signaling cascade
    • Datta, J., Majumder, S., Kutay, H., Motiwala, T., Frankel, W., Costa, R., Cha, H. C., MacDougald, O. A., Jacob, S. T., and Ghoshal, K. (2007) Metallothionein expression is suppressed in primary human hepatocellular carcinomas and is mediated through inactivation of CCAAT/enhancer binding protein α by phosphatidylinositol 3-kinase signaling cascade. Cancer Res. 67, 2736-2746
    • (2007) Cancer Res. , vol.67 , pp. 2736-2746
    • Datta, J.1    Majumder, S.2    Kutay, H.3    Motiwala, T.4    Frankel, W.5    Costa, R.6    Cha, H.C.7    Macdougald, O.A.8    Jacob, S.T.9    Ghoshal, K.10
  • 57
    • 61349123235 scopus 로고    scopus 로고
    • A PP2A regulatory subunit regulates C. Elegans insulin/IGF 1 signaling by modulating AKT-1 phosphorylation
    • Padmanabhan, S., Mukhopadhyay, A., Narasimhan, S. D., Tesz, G., Czech, M. P., and Tissenbaum, H. A. (2009) A PP2A regulatory subunit regulates C. elegans insulin/IGF-1 signaling by modulating AKT-1 phosphorylation. Cell 136, 939-951
    • (2009) Cell , vol.136 , pp. 939-951
    • Padmanabhan, S.1    Mukhopadhyay, A.2    Narasimhan, S.D.3    Tesz, G.4    Czech, M.P.5    Tissenbaum, H.A.6
  • 58
    • 79951506095 scopus 로고    scopus 로고
    • Clk2 and B56 mediate insulin-regulated assembly of the PP2A phosphatase holoenzyme complex on Akt
    • Rodgers, J. T., Vogel, R. O., and Puigserver, P. (2011) Clk2 and B56 mediate insulin-regulated assembly of the PP2A phosphatase holoenzyme complex on Akt. Mol. Cell 41, 471-479
    • (2011) Mol. Cell , vol.41 , pp. 471-479
    • Rodgers, J.T.1    Vogel, R.O.2    Puigserver, P.3
  • 59
    • 34548568958 scopus 로고    scopus 로고
    • GSK-3 acts downstream of PP2A and the PI 3-kinase-Akt pathway and upstream of caspase-2 in ceramide-induced mitochondrial apoptosis
    • Lin, C. F., Chen, C. L., Chiang, C. W., Jan, M. S., Huang, W. C., and Lin, Y. S. (2007) GSK-3 acts downstream of PP2A and the PI 3-kinase-Akt pathway and upstream of caspase-2 in ceramide-induced mitochondrial apoptosis. J. Cell Sci. 120, 2935-2943
    • (2007) J. Cell Sci. , vol.120 , pp. 2935-2943
    • Lin, C.F.1    Chen, C.L.2    Chiang, C.W.3    Jan, M.S.4    Huang, W.C.5    Lin, Y.S.6
  • 60
    • 1942466512 scopus 로고    scopus 로고
    • Liver tumors escape negative control of proliferation via PI3K/ Akt-mediated block of C/EBP α growth inhibitory activity
    • Wang, G. L., Iakova, P., Wilde, M., Awad, S., and Timchenko, N. A. (2004) Liver tumors escape negative control of proliferation via PI3K/ Akt-mediated block of C/EBP α growth inhibitory activity. Genes Dev. 18, 912-925
    • (2004) Genes Dev. , vol.18 , pp. 912-925
    • Wang, G.L.1    Iakova, P.2    Wilde, M.3    Awad, S.4    Timchenko, N.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.