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Volumn 35, Issue , 2015, Pages

Signalling mechanisms regulating phenotypic changes in breast cancer cells

Author keywords

Breast cancer; Cell fate decisions; Lipid accumulation; MCF 7; MTOR; PI3 kinase; Receptor tyrosine kinases signalling pathways

Indexed keywords

ADENOSINE TRIPHOSPHATE CITRATE SYNTHASE; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; NEU DIFFERENTIATION FACTOR; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN TYROSINE KINASE; INSULIN; MULTIPROTEIN COMPLEX; NRG1 PROTEIN, HUMAN; TARGET OF RAPAMYCIN KINASE; TOR COMPLEX 2; TUMOR PROTEIN;

EID: 85017330182     PISSN: 01448463     EISSN: 15734935     Source Type: Journal    
DOI: 10.1042/BSR20140172     Document Type: Article
Times cited : (9)

References (77)
  • 1
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
    • CrossRef PubMed
    • Marshall, C.J. (1995) Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 80, 179-185 CrossRef PubMed
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 2
    • 0034796049 scopus 로고    scopus 로고
    • Specificity of MAP kinase signaling in yeast differentiation involves transient versus sustained MAPK activation
    • CrossRef PubMed
    • Sabbagh, Jr, W., Flatauer, L.J., Bardwell, A.J. and Bardwell, L. (2001) Specificity of MAP kinase signaling in yeast differentiation involves transient versus sustained MAPK activation. Mol. Cell 8, 683-691 CrossRef PubMed
    • (2001) Mol. Cell , vol.8 , pp. 683-691
    • Sabbagh, W.1    Flatauer, L.J.2    Bardwell, A.J.3    Bardwell, L.4
  • 3
    • 0036533386 scopus 로고    scopus 로고
    • New perspectives on a developmental dilemma: The kinetic signaling model and the importance of signal duration for the CD4/CD8 lineage decision
    • CrossRef PubMed
    • Singer, A. (2002) New perspectives on a developmental dilemma: the kinetic signaling model and the importance of signal duration for the CD4/CD8 lineage decision. Curr. Opin. Immunol. 14, 207-215 CrossRef PubMed
    • (2002) Curr. Opin. Immunol. , vol.14 , pp. 207-215
    • Singer, A.1
  • 4
    • 78650866393 scopus 로고    scopus 로고
    • MYB suppresses differentiation and apoptosis of human breast cancer cells
    • CrossRef PubMed
    • Drabsch, Y, Robert, R.G. and Gonda, T.J. (2010) MYB suppresses differentiation and apoptosis of human breast cancer cells. Breast Cancer Res. 12, R55 CrossRef PubMed
    • (2010) Breast Cancer Res. , vol.12 , pp. R55
    • Drabsch, Y.1    Robert, R.G.2    Gonda, T.J.3
  • 5
    • 0032581532 scopus 로고    scopus 로고
    • Increased expression of c-erbB-2 in hormone-dependent breast cancer cells inhibits cell growth and induces differentiation
    • CrossRef PubMed
    • Giani, C, Casalini, P., Pupa, S.M., De Vecchi, R., Ardini, E., Colnaghi, M.I., Giordano, A. and Menard, S. (1998) Increased expression of c-erbB-2 in hormone-dependent breast cancer cells inhibits cell growth and induces differentiation. Oncogene 17, 425-432 CrossRef PubMed
    • (1998) Oncogene , vol.17 , pp. 425-432
    • Giani, C.1    Casalini, P.2    Pupa, S.M.3    De Vecchi, R.4    Ardini, E.5    Colnaghi, M.I.6    Giordano, A.7    Menard, S.8
  • 6
    • 33947547741 scopus 로고    scopus 로고
    • Quantitative transcriptional control of ErbB receptor signaling undergoes graded to biphasic response for cell differentiation
    • CrossRef PubMed
    • Nagashima, T, Shimodaira, H., Ide, K., Nakakuki, T, Tani, Y, Takahashi, K., Yumoto, N. and Hatakeyama, M. (2007) Quantitative transcriptional control of ErbB receptor signaling undergoes graded to biphasic response for cell differentiation. J. Biol. Chem. 282, 4045-4056 CrossRef PubMed
    • (2007) J. Biol. Chem. , vol.282 , pp. 4045-4056
    • Nagashima, T.1    Shimodaira, H.2    Ide, K.3    Nakakuki, T.4    Tani, Y.5    Takahashi, K.6    Yumoto, N.7    Hatakeyama, M.8
  • 7
    • 0026899636 scopus 로고
    • A ligand for the erbB-2 oncogene product (gp30) induces differentiation of human breast cancer cells
    • PubMed
    • Bacus, S.S., Huberman, E., Chin, D., Kiguchi, K., Simpson, S., Lippman, M. and Lupu, R. (1992) A ligand for the erbB-2 oncogene product (gp30) induces differentiation of human breast cancer cells. Cell Growth Differ. 3, 401-411 PubMed
    • (1992) Cell Growth Differ. , vol.3 , pp. 401-411
    • Bacus, S.S.1    Huberman, E.2    Chin, D.3    Kiguchi, K.4    Simpson, S.5    Lippman, M.6    Lupu, R.7
  • 8
    • 0036905360 scopus 로고    scopus 로고
    • Fatty acid modulation of MCF-7 human breast cancer cell proliferation, apoptosis and differentiation
    • CrossRef PubMed
    • Chamras, H., Ardashian, A., Heber, D. and Glaspy, J.A. (2002) Fatty acid modulation of MCF-7 human breast cancer cell proliferation, apoptosis and differentiation. J. Nutr. Biochem. 13, 711-716 CrossRef PubMed
    • (2002) J. Nutr. Biochem. , vol.13 , pp. 711-716
    • Chamras, H.1    Ardashian, A.2    Heber, D.3    Glaspy, J.A.4
  • 9
    • 4644330224 scopus 로고    scopus 로고
    • Differentiation-inducing quinolines as experimental breast cancer agents in the MCF-7 human breast cancer cell model
    • CrossRef PubMed
    • Martirosyan, A.R., Rahim-Bata, R., Freeman, A.B., Clarke, CD., Howard, R.L. and Strobl, J.S. (2004) Differentiation-inducing quinolines as experimental breast cancer agents in the MCF-7 human breast cancer cell model. Biochem. Pharmacol. 68, 1729-1738 CrossRef PubMed
    • (2004) Biochem. Pharmacol. , vol.68 , pp. 1729-1738
    • Martirosyan, A.R.1    Rahim-Bata, R.2    Freeman, A.B.3    Clarke, C.D.4    Howard, R.L.5    Strobl, J.S.6
  • 10
    • 33746716146 scopus 로고    scopus 로고
    • Differential anti-proliferative actions of peroxisome proliferator-activated receptor-gamma agonists in MCF-7 breast cancer cells
    • CrossRef PubMed
    • Kim, K.Y., Kim, S.S. and Cheon, H.G. (2006) Differential anti-proliferative actions of peroxisome proliferator-activated receptor-gamma agonists in MCF-7 breast cancer cells. Biochem. Pharmacol. 72, 530-540 CrossRef PubMed
    • (2006) Biochem. Pharmacol. , vol.72 , pp. 530-540
    • Kim, K.Y.1    Kim, S.S.2    Cheon, H.G.3
  • 11
    • 0025173016 scopus 로고
    • Effects of differentiation-inducing agents on maturation of human MCF-7 breast cancer cells
    • CrossRef PubMed
    • Guilbaud, N.F., Gas, N., Dupont, M.A. and Valette, A. (1990) Effects of differentiation-inducing agents on maturation of human MCF-7 breast cancer cells. J. Cell. Physiol. 145, 162-172 CrossRef PubMed
    • (1990) J. Cell. Physiol. , vol.145 , pp. 162-172
    • Guilbaud, N.F.1    Gas, N.2    Dupont, M.A.3    Valette, A.4
  • 12
    • 0029021518 scopus 로고
    • Heterodimerization and functional interaction between EGF receptor family members: A new signaling paradigm with implications for breast cancer research
    • CrossRef PubMed
    • Earp, H.S., Dawson, T.L., Li, X. and Yu, H. (1995) Heterodimerization and functional interaction between EGF receptor family members: a new signaling paradigm with implications for breast cancer research. Breast Cancer Res. Treat. 35, 115-132 CrossRef PubMed
    • (1995) Breast Cancer Res. Treat. , vol.35 , pp. 115-132
    • Earp, H.S.1    Dawson, T.L.2    Li, X.3    Yu, H.4
  • 13
    • 77953896432 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • CrossRef PubMed
    • Lemmon, M.A. and Schlessinger, J. (2010) Cell signaling by receptor tyrosine kinases. Cell 141, 1117-1134 CrossRef PubMed
    • (2010) Cell , vol.141 , pp. 1117-1134
    • Lemmon, M.A.1    Schlessinger, J.2
  • 14
    • 0035256698 scopus 로고    scopus 로고
    • Untangling the ErbB signalling network
    • CrossRef PubMed
    • Yarden, Y. and Sliwkowski, M.X. (2001) Untangling the ErbB signalling network. Nat. Rev. Mol. Cell. Biol. 2, 127-137 CrossRef PubMed
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , pp. 127-137
    • Yarden, Y.1    Sliwkowski, M.X.2
  • 15
  • 16
    • 53649106357 scopus 로고    scopus 로고
    • Dissecting the role of the 3-phosphoinositide-dependent protein kinase-1 (PDK1) signalling pathways
    • CrossRef PubMed
    • Bayascas, J.R. (2008) Dissecting the role of the 3-phosphoinositide-dependent protein kinase-1 (PDK1) signalling pathways. Cell Cycle 7, 2978-2982 CrossRef PubMed
    • (2008) Cell Cycle , vol.7 , pp. 2978-2982
    • Bayascas, J.R.1
  • 17
    • 1342342993 scopus 로고    scopus 로고
    • PDK1, the master regulator of AGC kinase signal transduction
    • CrossRef PubMed
    • Mora, A., Komander, D., van Aalten, D.M. and Alessi, D.R. (2004) PDK1, the master regulator of AGC kinase signal transduction. Semin. Cell Dev. Biol. 15, 161-170 CrossRef PubMed
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 161-170
    • Mora, A.1    Komander, D.2    Van Aalten, D.M.3    Alessi, D.R.4
  • 18
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of akt/PKB by the rictor-mTOR complex
    • CrossRef PubMed
    • Sarbassov, D.D., Guertin, D.A., Ali, S.M. and Sabatini, D.M. (2005) Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex. Science 307, 1098-1101 CrossRef PubMed
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 19
    • 78650510609 scopus 로고    scopus 로고
    • MTOR: From growth signal integration to cancer, diabetes and ageing
    • CrossRef PubMed
    • Zoncu, R., Efeyan, A. and Sabatini, D.M. (2011) mTOR: from growth signal integration to cancer, diabetes and ageing. Nat. Rev. Mol. Cell. Biol. 12, 21-35 CrossRef PubMed
    • (2011) Nat. Rev. Mol. Cell. Biol. , vol.12 , pp. 21-35
    • Zoncu, R.1    Efeyan, A.2    Sabatini, D.M.3
  • 20
  • 21
    • 84874257493 scopus 로고    scopus 로고
    • Sensing the immune microenvironment to coordinate T cell metabolism, differentiation & function
    • CrossRef PubMed
    • Heikamp, E.B. and Powell, J.D. (2012) Sensing the immune microenvironment to coordinate T cell metabolism, differentiation & function. Semin. Immunol. 24, 414-420 CrossRef PubMed
    • (2012) Semin. Immunol. , vol.24 , pp. 414-420
    • Heikamp, E.B.1    Powell, J.D.2
  • 23
    • 79960128997 scopus 로고    scopus 로고
    • MTOR and the differentiation of mesenchymal stem cells
    • CrossRef
    • Xiang, X., Zhao, J., Xu, G., Li, Y. and Zhang, W. (2011) mTOR and the differentiation of mesenchymal stem cells. Acta Biochim. Biophys. Sin. 43, 501-510 CrossRef
    • (2011) Acta Biochim. Biophys. Sin. , vol.43 , pp. 501-510
    • Xiang, X.1    Zhao, J.2    Xu, G.3    Li, Y.4    Zhang, W.5
  • 24
    • 14844318077 scopus 로고    scopus 로고
    • When kinases meet mathematics: The systems biology of MAPK signalling
    • CrossRef PubMed
    • Kolch, W., Calder, M. and Gilbert, D. (2005) When kinases meet mathematics: the systems biology of MAPK signalling. FEBS Lett. 579, 1891-1895 CrossRef PubMed
    • (2005) FEBS Lett. , vol.579 , pp. 1891-1895
    • Kolch, W.1    Calder, M.2    Gilbert, D.3
  • 25
    • 84881046240 scopus 로고    scopus 로고
    • Complexity of receptor tyrosine kinase signal processing
    • CrossRef PubMed
    • Volinsky, N. and Kholodenko, B.N. (2013) Complexity of receptor tyrosine kinase signal processing. Cold Spring Harb. Perspect. Biol. 5, a009043 CrossRef PubMed
    • (2013) Cold Spring Harb. Perspect. Biol. , vol.5
    • Volinsky, N.1    Kholodenko, B.N.2
  • 26
    • 84856253626 scopus 로고    scopus 로고
    • Cross-talk between mitogenic ras/MAPK and survival PI3K/Akt pathways: A fine balance
    • CrossRef PubMed
    • Aksamitiene, E., Kiyatkin, A. and Kholodenko, B.N. (2012) Cross-talk between mitogenic Ras/MAPK and survival PI3K/Akt pathways: a fine balance. Biochem. Soc. Trans. 40, 139-146 CrossRef PubMed
    • (2012) Biochem. Soc. Trans. , vol.40 , pp. 139-146
    • Aksamitiene, E.1    Kiyatkin, A.2    Kholodenko, B.N.3
  • 28
    • 36849018402 scopus 로고    scopus 로고
    • Why is PTEN an important tumor suppressor?
    • CrossRef PubMed
    • Li, L. and Ross, A.H. (2007) Why is PTEN an important tumor suppressor? J. Cell. Biochem. 102, 1368-1374 CrossRef PubMed
    • (2007) J. Cell. Biochem. , vol.102 , pp. 1368-1374
    • Li, L.1    Ross, A.H.2
  • 29
    • 84860217431 scopus 로고    scopus 로고
    • The functions and regulation of the PTEN tumour suppressor. Nature reviews
    • Song, M.S., Salmena, L. and Pandolfi, P.P. (2012) The functions and regulation of the PTEN tumour suppressor. Nature reviews. Mol. Cell Biol. 13, 283-296
    • (2012) Mol. Cell Biol. , vol.13 , pp. 283-296
    • Song, M.S.1    Salmena, L.2    Pandolfi, P.P.3
  • 30
    • 59749091850 scopus 로고    scopus 로고
    • A complex interplay between akt, TSC2 and the two mTOR complexes
    • CrossRef PubMed
    • Huang, J. and Manning, B.D. (2009) A complex interplay between Akt, TSC2 and the two mTOR complexes. Biochem. Soc. Trans. 37, 217-222 CrossRef PubMed
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 217-222
    • Huang, J.1    Manning, B.D.2
  • 31
    • 75149112670 scopus 로고    scopus 로고
    • AZD8055 is a potent, selective, and orally bioavailable ATP-competitive Mammalian target of rapamycin kinase inhibitor with in vitro and in vivo antitumor activity
    • CrossRef PubMed
    • Chresta, C.M., Davies, B.R., Hickson, I., Harding, T., Cosulich, S., Critchlow, S.E., Vincent, J.P., Ellston, R., Jones, D., Sini, P. et al. (2010) AZD8055 is a potent, selective, and orally bioavailable ATP-competitive mammalian target of rapamycin kinase inhibitor with in vitro and in vivo antitumor activity. Cancer Res. 70, 288-298 CrossRef PubMed
    • (2010) Cancer Res. , vol.70 , pp. 288-298
    • Chresta, C.M.1    Davies, B.R.2    Hickson, I.3    Harding, T.4    Cosulich, S.5    Critchlow, S.E.6    Vincent, J.P.7    Ellston, R.8    Jones, D.9    Sini, P.10
  • 32
    • 34249326610 scopus 로고    scopus 로고
    • C-src modulates ErbB2 and ErbB3 heterocomplex formation and function
    • CrossRef PubMed
    • Ishizawar, R.C., Miyake, T. and Parsons, S.J. (2007) c-Src modulates ErbB2 and ErbB3 heterocomplex formation and function. Oncogene 26, 3503-3510 CrossRef PubMed
    • (2007) Oncogene , vol.26 , pp. 3503-3510
    • Ishizawar, R.C.1    Miyake, T.2    Parsons, S.J.3
  • 34
    • 48749118203 scopus 로고    scopus 로고
    • Targeting src in breast cancer
    • CrossRef PubMed
    • Finn, R.S. (2008) Targeting Src in breast cancer. Ann. Oncol. 19, 1379-1386 CrossRef PubMed
    • (2008) Ann. Oncol. , vol.19 , pp. 1379-1386
    • Finn, R.S.1
  • 35
    • 0023649672 scopus 로고
    • Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation
    • CrossRef PubMed
    • Kmiecik, T.E. and Shalloway, D. (1987) Activation and suppression of pp60c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation. Cell 49, 65-73 CrossRef PubMed
    • (1987) Cell , vol.49 , pp. 65-73
    • Kmiecik, T.E.1    Shalloway, D.2
  • 36
    • 17444374230 scopus 로고    scopus 로고
    • Src kinase regulation by phosphorylation and dephosphorylation
    • CrossRef PubMed
    • Roskoski, Jr, R. (2005) Src kinase regulation by phosphorylation and dephosphorylation. Biochem. Biophys. Res. Commun. 331, 1-14 CrossRef PubMed
    • (2005) Biochem. Biophys. Res. Commun. , vol.331 , pp. 1-14
    • Roskoski, R.1
  • 37
    • 0035823484 scopus 로고    scopus 로고
    • Functional analysis of csk and CHK kinases in breast cancer cells
    • CrossRef PubMed
    • Bougeret, C., Jiang, S., Keydar, I. and Avraham, H. (2001) Functional analysis of Csk and CHK kinases in breast cancer cells. J. Biol. Chem. 276, 33711-33720 CrossRef PubMed
    • (2001) J. Biol. Chem. , vol.276 , pp. 33711-33720
    • Bougeret, C.1    Jiang, S.2    Keydar, I.3    Avraham, H.4
  • 38
  • 39
    • 66249108601 scopus 로고    scopus 로고
    • Understanding the warburg effect: The metabolic requirements of cell proliferation
    • CrossRef PubMed
    • Vander Heiden, M.G., Cantley, L.C. and Thompson, C.B. (2009) Understanding the Warburg effect: the metabolic requirements of cell proliferation. Science 324, 1029-1033 CrossRef PubMed
    • (2009) Science , vol.324 , pp. 1029-1033
    • Vander Heiden, M.G.1    Cantley, L.C.2    Thompson, C.B.3
  • 40
    • 84864858864 scopus 로고    scopus 로고
    • ATP-citrate lyase: A key player in cancer metabolism
    • CrossRef PubMed
    • Zaidi, N., Swinnen, J.V. and Smans, K. (2012) ATP-citrate lyase: a key player in cancer metabolism. Cancer Res. 72, 3709-3714 CrossRef PubMed
    • (2012) Cancer Res. , vol.72 , pp. 3709-3714
    • Zaidi, N.1    Swinnen, J.V.2    Smans, K.3
  • 41
    • 0034620591 scopus 로고    scopus 로고
    • Phosphorylation of recombinant human ATP: Citrate lyase by cAMP-dependent protein kinase abolishes homotropic allosteric regulation of the enzyme by citrate and increases the enzyme activity
    • CrossRef PubMed
    • Potapova, I.A., El-Maghrabi, M.R., Doronin, S.V. and Benjamin, W.B. (2000) Phosphorylation of recombinant human ATP: citrate lyase by cAMP-dependent protein kinase abolishes homotropic allosteric regulation of the enzyme by citrate and increases the enzyme activity. Allosteric activation of ATP: citrate lyase by phosphorylated sugars. Biochemistry 39, 1169-1179 CrossRef PubMed
    • (2000) Allosteric Activation of ATP: Citrate Lyase by Phosphorylated Sugars. Biochemistry , vol.39 , pp. 1169-1179
    • Potapova, I.A.1    El-Maghrabi, M.R.2    Doronin, S.V.3    Benjamin, W.B.4
  • 42
    • 0037072780 scopus 로고    scopus 로고
    • The identification of ATP-citrate lyase as a protein kinase B (Akt) substrate in primary adipocytes
    • CrossRef PubMed
    • Berwick, D.C., Hers, I., Heesom, K.J., Moule, S.K. and Tavare, J.M. (2002) The identification of ATP-citrate lyase as a protein kinase B (Akt) substrate in primary adipocytes. J. Biol. Chem. 277, 33895-33900 CrossRef PubMed
    • (2002) J. Biol. Chem. , vol.277 , pp. 33895-33900
    • Berwick, D.C.1    Hers, I.2    Heesom, K.J.3    Moule, S.K.4    Tavare, J.M.5
  • 44
    • 43249086785 scopus 로고    scopus 로고
    • Mammalian long-chain acyl-coa synthetases
    • CrossRef
    • Soupene, E. and Kuypers, F.A. (2008) Mammalian long-chain acyl-CoA synthetases. Exp. Biol. Med. 233, 507-521 CrossRef
    • (2008) Exp. Biol. Med. , vol.233 , pp. 507-521
    • Soupene, E.1    Kuypers, F.A.2
  • 45
    • 0029994543 scopus 로고    scopus 로고
    • Role of the peroxisome proliferator-activated receptor (PPAR) in mediating the effects of fibrates and fatty acids on gene expression
    • PubMed
    • Schoonjans, K., Staels, B. and Auwerx, J. (1996) Role of the peroxisome proliferator-activated receptor (PPAR) in mediating the effects of fibrates and fatty acids on gene expression. J. Lipid Res. 37, 907-925 PubMed
    • (1996) J. Lipid Res. , vol.37 , pp. 907-925
    • Schoonjans, K.1    Staels, B.2    Auwerx, J.3
  • 46
    • 69449086702 scopus 로고    scopus 로고
    • Comparative analysis of gene regulation by the transcription factor PPARalpha between mouse and human
    • CrossRef PubMed
    • Rakhshandehroo, M., Hooiveld, G., Muller, M. and Kersten, S. (2009) Comparative analysis of gene regulation by the transcription factor PPARalpha between mouse and human. PLoS One 4, e6796 CrossRef PubMed
    • (2009) PLoS One , vol.4
    • Rakhshandehroo, M.1    Hooiveld, G.2    Muller, M.3    Kersten, S.4
  • 48
    • 0030658022 scopus 로고    scopus 로고
    • Coordinate regulation of the expression of the fatty acid transport protein and acyl-coa synthetase genes by PPARalpha and PPARgamma activators
    • CrossRef PubMed
    • Martin, G., Schoonjans, K., Lefebvre, A.M., Staels, B. and Auwerx, J. (1997) Coordinate regulation of the expression of the fatty acid transport protein and acyl-CoA synthetase genes by PPARalpha and PPARgamma activators. J. Biol. Chem. 272, 28210-28217 CrossRef PubMed
    • (1997) J. Biol. Chem. , vol.272 , pp. 28210-28217
    • Martin, G.1    Schoonjans, K.2    Lefebvre, A.M.3    Staels, B.4    Auwerx, J.5
  • 49
    • 84875967687 scopus 로고    scopus 로고
    • Acyl-coa synthetase 1 is induced by gram-negative bacteria and lipopolysaccharide and is required for phospholipid turnover in stimulated macrophages
    • CrossRef PubMed
    • Rubinow, K.B., Wall, V.Z., Nelson, J., Mar, D., Bomsztyk, K., Askari, B., Lai, M.A., Smith, K.D., Han, M.S., Vivekanandan-Giri, A. et al. (2013) Acyl-CoA synthetase 1 is induced by Gram-negative bacteria and lipopolysaccharide and is required for phospholipid turnover in stimulated macrophages. J. Biol. Chem. 288, 9957-9970 CrossRef PubMed
    • (2013) J. Biol. Chem. , vol.288 , pp. 9957-9970
    • Rubinow, K.B.1    Wall, V.Z.2    Nelson, J.3    Mar, D.4    Bomsztyk, K.5    Askari, B.6    Lai, M.A.7    Smith, K.D.8    Han, M.S.9    Vivekanandan-Giri, A.10
  • 50
    • 52249089184 scopus 로고    scopus 로고
    • Gene networks driving bovine milk fat synthesis during the lactation cycle
    • CrossRef PubMed
    • Bionaz, M. and Loor, J.J. (2008) Gene networks driving bovine milk fat synthesis during the lactation cycle. BMC Genomics 9, 366 CrossRef PubMed
    • (2008) BMC Genomics , vol.9 , pp. 366
    • Bionaz, M.1    Loor, J.J.2
  • 51
    • 0035377009 scopus 로고    scopus 로고
    • Antigen decoding by T lymphocytes: From synapses to fate determination
    • CrossRef PubMed
    • Lanzavecchia, A. and Sallusto, F. (2001) Antigen decoding by T lymphocytes: from synapses to fate determination. Nat. Immunol. 2, 487-492 CrossRef PubMed
    • (2001) Nat. Immunol. , vol.2 , pp. 487-492
    • Lanzavecchia, A.1    Sallusto, F.2
  • 52
    • 84871747595 scopus 로고    scopus 로고
    • The identity and fate decision control of Spermatogonial stem cells: Where is the point of no return?
    • CrossRef PubMed
    • Nagano, M.C. and Yeh, J.R. (2013) The identity and fate decision control of spermatogonial stem cells: where is the point of no return? Curr. Top. Dev. Biol. 102, 61-95 CrossRef PubMed
    • (2013) Curr. Top. Dev. Biol. , vol.102 , pp. 61-95
    • Nagano, M.C.1    Yeh, J.R.2
  • 53
    • 82555179207 scopus 로고    scopus 로고
    • B-lymphocyte commitment: Identifying the point of no return
    • CrossRef PubMed
    • Welinder, E., Ahsberg, J. and Sigvardsson, M. (2011) B-lymphocyte commitment: identifying the point of no return. Semin. Immunol. 23, 335-340 CrossRef PubMed
    • (2011) Semin. Immunol. , vol.23 , pp. 335-340
    • Welinder, E.1    Ahsberg, J.2    Sigvardsson, M.3
  • 54
    • 34748912615 scopus 로고    scopus 로고
    • Fatty acid synthase and the lipogenic phenotype in cancer pathogenesis
    • CrossRef PubMed
    • Menendez, J.A. and Lupu, R. (2007) Fatty acid synthase and the lipogenic phenotype in cancer pathogenesis. Nat. Rev. Cancer 7, 763-777 CrossRef PubMed
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 763-777
    • Menendez, J.A.1    Lupu, R.2
  • 55
    • 84896487990 scopus 로고    scopus 로고
    • Lipid transport in the lactating mammary gland
    • CrossRef PubMed
    • McManaman, J.L. (2014) Lipid transport in the lactating mammary gland. J. Mammary Gland Biol. Neoplasia 19, 35-42 CrossRef PubMed
    • (2014) J. Mammary Gland Biol. Neoplasia , vol.19 , pp. 35-42
    • McManaman, J.L.1
  • 56
    • 3242685815 scopus 로고    scopus 로고
    • Inhibition of fatty acid synthase (FAS) suppresses HER2/neu (erbB-2) oncogene overexpression in cancer cells
    • CrossRef PubMed
    • Menendez, J.A., Vellon, L., Mehmi, I., Oza, B.P., Ropero, S., Colomer, R. and Lupu, R. (2004) Inhibition of fatty acid synthase (FAS) suppresses HER2/neu (erbB-2) oncogene overexpression in cancer cells. Proc. Natl. Acad. Sci. U.S.A. 101, 10715-10720 CrossRef PubMed
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 10715-10720
    • Menendez, J.A.1    Vellon, L.2    Mehmi, I.3    Oza, B.P.4    Ropero, S.5    Colomer, R.6    Lupu, R.7
  • 57
    • 0030706079 scopus 로고    scopus 로고
    • Enzymes of the fatty acid synthesis pathway are highly expressed in in situ breast carcinoma
    • PubMed
    • Milgraum, L.Z., Witters, L.A., Pasternack, G.R. and Kuhajda, F.P. (1997) Enzymes of the fatty acid synthesis pathway are highly expressed in in situ breast carcinoma. Clin. Cancer Res. 3, 2115-2120 PubMed
    • (1997) Clin. Cancer Res. , vol.3 , pp. 2115-2120
    • Milgraum, L.Z.1    Witters, L.A.2    Pasternack, G.R.3    Kuhajda, F.P.4
  • 58
    • 0018769394 scopus 로고
    • Lipogenetic and glycolytic enzyme activities in carcinoma and Nonmalignant diseases of the human breast
    • CrossRef PubMed
    • Szutowicz, A., Kwiatkowski, J. and Angielski, S. (1979) Lipogenetic and glycolytic enzyme activities in carcinoma and nonmalignant diseases of the human breast. Br. J. Cancer. 39, 681-687 CrossRef PubMed
    • (1979) Br. J. Cancer. , vol.39 , pp. 681-687
    • Szutowicz, A.1    Kwiatkowski, J.2    Angielski, S.3
  • 59
    • 77649336663 scopus 로고    scopus 로고
    • Metabolic genes in cancer: Their roles in tumor progression and clinical implications
    • PubMed
    • Furuta, E., Okuda, H., Kobayashi, A. and Watabe, K. (2010) Metabolic genes in cancer: their roles in tumor progression and clinical implications. Biochim. Biophys. Acta 1805, 141-152 PubMed
    • (2010) Biochim. Biophys. Acta , vol.1805 , pp. 141-152
    • Furuta, E.1    Okuda, H.2    Kobayashi, A.3    Watabe, K.4
  • 61
    • 0024453198 scopus 로고
    • Haptoglobin-related protein (Hpr) epitopes in breast cancer as a predictor of recurrence of the disease
    • CrossRef PubMed
    • Kuhajda, F.P., Piantadosi, S. and Pasternack, G.R. (1989) Haptoglobin-related protein (Hpr) epitopes in breast cancer as a predictor of recurrence of the disease. N. Engl. J. Med. 321, 636-641 CrossRef PubMed
    • (1989) N. Engl. J. Med. , vol.321 , pp. 636-641
    • Kuhajda, F.P.1    Piantadosi, S.2    Pasternack, G.R.3
  • 62
    • 65249127544 scopus 로고    scopus 로고
    • MUC1-induced alterations in a lipid metabolic gene network predict response of human breast cancers to tamoxifen treatment
    • CrossRef PubMed
    • Pitroda, S.P., Khodarev, N.N., Beckett, M.A., Kufe, D.W. and Weichselbaum, R.R. (2009) MUC1-induced alterations in a lipid metabolic gene network predict response of human breast cancers to tamoxifen treatment. Proc. Natl. Acad. Sci. U.S.A. 106, 5837-5841 CrossRef PubMed
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 5837-5841
    • Pitroda, S.P.1    Khodarev, N.N.2    Beckett, M.A.3    Kufe, D.W.4    Weichselbaum, R.R.5
  • 64
    • 30544433533 scopus 로고    scopus 로고
    • ATP citrate lyase is an important component of cell growth and transformation
    • CrossRef PubMed
    • Bauer, D.E., Hatzivassiliou, G., Zhao, F., Andreadis, C. and Thompson, C.B. (2005) ATP citrate lyase is an important component of cell growth and transformation. Oncogene 24, 6314-6322 CrossRef PubMed
    • (2005) Oncogene , vol.24 , pp. 6314-6322
    • Bauer, D.E.1    Hatzivassiliou, G.2    Zhao, F.3    Andreadis, C.4    Thompson, C.B.5
  • 66
  • 67
    • 84855743864 scopus 로고    scopus 로고
    • Inhibition of lung cancer growth: ATP citrate lyase knockdown and statin treatment leads to dual blockade of mitogen-activated protein kinase (MAPK) and phosphatidylinositol-3-kinase (PI3K)/AKT pathways
    • CrossRef PubMed
    • Hanai, J., Doro, N., Sasaki, A.T., Kobayashi, S., Cantley, L.C., Seth, P. and Sukhatme, V.P. (2012) Inhibition of lung cancer growth: ATP citrate lyase knockdown and statin treatment leads to dual blockade of mitogen-activated protein kinase (MAPK) and phosphatidylinositol-3-kinase (PI3K)/AKT pathways. J. Cell. Physiol. 227, 1709-1720 CrossRef PubMed
    • (2012) J. Cell. Physiol. , vol.227 , pp. 1709-1720
    • Hanai, J.1    Doro, N.2    Sasaki, A.T.3    Kobayashi, S.4    Cantley, L.C.5    Seth, P.6    Sukhatme, V.P.7
  • 68
    • 84894465269 scopus 로고    scopus 로고
    • ATP citrate lyase knockdown impacts cancer stem cells in vitro
    • CrossRef PubMed
    • Hanai, J.I., Doro, N., Seth, P. and Sukhatme, V.P. (2013) ATP citrate lyase knockdown impacts cancer stem cells in vitro. Cell Death Dis. 4, e696 CrossRef PubMed
    • (2013) Cell Death Dis. , vol.4 , pp. e696
    • Hanai, J.I.1    Doro, N.2    Seth, P.3    Sukhatme, V.P.4
  • 69
    • 84882605310 scopus 로고    scopus 로고
    • Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth
    • CrossRef PubMed
    • Lin, R., Tao, R., Gao, X., Li, T., Zhou, X., Guan, K.L., Xiong, Y. and Lei, Q.Y. (2013) Acetylation stabilizes ATP-citrate lyase to promote lipid biosynthesis and tumor growth. Mol. Cell 51, 506-518 CrossRef PubMed
    • (2013) Mol. Cell , vol.51 , pp. 506-518
    • Lin, R.1    Tao, R.2    Gao, X.3    Li, T.4    Zhou, X.5    Guan, K.L.6    Xiong, Y.7    Lei, Q.Y.8
  • 70
    • 0036848491 scopus 로고    scopus 로고
    • The role of MAPK pathways in the action of chemotherapeutic drugs
    • CrossRef PubMed
    • Boldt, S., Weidle, U.H. and Kolch, W. (2002) The role of MAPK pathways in the action of chemotherapeutic drugs. Carcinogenesis 23, 1831-1838 CrossRef PubMed
    • (2002) Carcinogenesis , vol.23 , pp. 1831-1838
    • Boldt, S.1    Weidle, U.H.2    Kolch, W.3
  • 71
    • 84857058592 scopus 로고    scopus 로고
    • Protein kinase D1 stimulates proliferation and enhances tumorigenesis of MCF-7 human breast cancer cells through a MEK/ERK-dependent signaling pathway
    • CrossRef PubMed
    • Karam, M., Legay, C., Auclair, C. and Ricort, J.M. (2012) Protein kinase D1 stimulates proliferation and enhances tumorigenesis of MCF-7 human breast cancer cells through a MEK/ERK-dependent signaling pathway. Exp. Cell Res. 318, 558-569 CrossRef PubMed
    • (2012) Exp. Cell Res. , vol.318 , pp. 558-569
    • Karam, M.1    Legay, C.2    Auclair, C.3    Ricort, J.M.4
  • 72
    • 84907063686 scopus 로고    scopus 로고
    • PI3K/AKT signaling pathway and cancer: An updated review
    • CrossRef PubMed
    • Martini, M., De Santis, M.C., Braccini, L., Gulluni, F. and Hirsch, E. (2014) PI3K/AKT signaling pathway and cancer: an updated review. Ann. Med. 46, 372-383 CrossRef PubMed
    • (2014) Ann. Med. , vol.46 , pp. 372-383
    • Martini, M.1    De Santis, M.C.2    Braccini, L.3    Gulluni, F.4    Hirsch, E.5
  • 73
    • 79251517382 scopus 로고    scopus 로고
    • Regulation of cancer cell metabolism
    • CrossRef PubMed
    • Cairns, R.A., Harris, I.S. and Mak, T.W. (2011) Regulation of cancer cell metabolism. Nat. Rev. Cancer 11, 85-95 CrossRef PubMed
    • (2011) Nat. Rev. Cancer , vol.11 , pp. 85-95
    • Cairns, R.A.1    Harris, I.S.2    Mak, T.W.3
  • 74
    • 33847314539 scopus 로고    scopus 로고
    • The phosphatidyl inositol 3-kinase signaling network: Implications for human breast cancer
    • CrossRef PubMed
    • Dillon, R.L., White, D.E. and Muller, W.J. (2007) The phosphatidyl inositol 3-kinase signaling network: implications for human breast cancer. Oncogene 26, 1338-1345 CrossRef PubMed
    • (2007) Oncogene , vol.26 , pp. 1338-1345
    • Dillon, R.L.1    White, D.E.2    Muller, W.J.3
  • 75
    • 33745095268 scopus 로고    scopus 로고
    • Targeting the akt/Mammalian target of rapamycin pathway for radiosensitization of breast cancer
    • CrossRef PubMed
    • Albert, J.M., Kim, K.W., Cao, C. and Lu, B. (2006) Targeting the Akt/mammalian target of rapamycin pathway for radiosensitization of breast cancer. Mol. Cancer Ther. 5, 1183-1189 CrossRef PubMed
    • (2006) Mol. Cancer Ther. , vol.5 , pp. 1183-1189
    • Albert, J.M.1    Kim, K.W.2    Cao, C.3    Lu, B.4
  • 76
    • 22744458796 scopus 로고    scopus 로고
    • The antiapoptotic effect of fibroblast growth factor-2 is mediated through nuclear factor-kappaB activation induced via interaction between akt and IkappaB kinase-beta in breast cancer cells
    • CrossRef PubMed
    • Vandermoere, F., El Yazidi-Belkoura, I., Adriaenssens, E., Lemoine, J. and Hondermarck, H. (2005) The antiapoptotic effect of fibroblast growth factor-2 is mediated through nuclear factor-kappaB activation induced via interaction between Akt and IkappaB kinase-beta in breast cancer cells. Oncogene 24, 5482-5491 CrossRef PubMed
    • (2005) Oncogene , vol.24 , pp. 5482-5491
    • Vandermoere, F.1    Yazidi-Belkoura, E.2    Adriaenssens, I.3    Lemoine, J.E.4    Hondermarck, H.5


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