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Volumn 8, Issue 1, 2018, Pages

The ferroptosis inducer erastin irreversibly inhibits system xc- and synergizes with cisplatin to increase cisplatin's cytotoxicity in cancer cells

Author keywords

[No Author keywords available]

Indexed keywords

CISPLATIN; ERASTIN; GLUTATHIONE; PIPERAZINE DERIVATIVE;

EID: 85040769180     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/s41598-018-19213-4     Document Type: Article
Times cited : (277)

References (45)
  • 1
    • 0018963749 scopus 로고
    • Transport interaction of L-cystine and L-glutamate in human diploid fibroblasts in culture
    • Bannai, S. & Kitamura, E. Transport interaction of L-cystine and L-glutamate in human diploid fibroblasts in culture. J. Biol. Chem. 255, 2372-2376 (1980).
    • (1980) J. Biol. Chem. , vol.255 , pp. 2372-2376
    • Bannai, S.1    Kitamura, E.2
  • 2
    • 0033597349 scopus 로고    scopus 로고
    • Cloning and expression of a plasma membrane cystine/glutamate exchange transporter composed of two distinct proteins
    • Sato, H., Tamba, M., Ishii, T. & Bannai, S. Cloning and expression of a plasma membrane cystine/glutamate exchange transporter composed of two distinct proteins. J. Biol. Chem. 274, 11455-11458 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 11455-11458
    • Sato, H.1    Tamba, M.2    Ishii, T.3    Bannai, S.4
  • 3
    • 0034527749 scopus 로고    scopus 로고
    • Molecular cloning and expression of human xCT, the light chain of amino acid transport system xc
    • Sato, H., Tamba, M., Kuriyama-Matsumura, K., Okuno, S. & Bannai, S. Molecular cloning and expression of human xCT, the light chain of amino acid transport system xc. Antioxid. Redox Signal. 2, 665-671 (2000).
    • (2000) Antioxid. Redox Signal. , vol.2 , pp. 665-671
    • Sato, H.1    Tamba, M.2    Kuriyama-Matsumura, K.3    Okuno, S.4    Bannai, S.5
  • 4
    • 0032541636 scopus 로고    scopus 로고
    • Amino-acid transport by heterodimers of 4F2hc/CD98 and members of a permease family
    • Mastroberardino, L. et al. Amino-acid transport by heterodimers of 4F2hc/CD98 and members of a permease family. Nature 395, 288-291 (1998).
    • (1998) Nature , vol.395 , pp. 288-291
    • Mastroberardino, L.1
  • 5
    • 0032508585 scopus 로고    scopus 로고
    • Expression cloning and characterization of a transporter for large neutral amino acids activated by the heavy chain of 4F2 antigen (CD98)
    • Kanai, Y. et al. Expression cloning and characterization of a transporter for large neutral amino acids activated by the heavy chain of 4F2 antigen (CD98). J. Biol. Chem. 273, 23629-23632 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 23629-23632
    • Kanai, Y.1
  • 6
    • 0032484216 scopus 로고    scopus 로고
    • Identification and characterization of a membrane protein (y + L amino acid transporter-1) that associates with 4F2hc to encode the amino acid transport activity y + L. A candidate gene for lysinuric protein intolerance
    • Torrents, D. et al. Identification and characterization of a membrane protein (y + L amino acid transporter-1) that associates with 4F2hc to encode the amino acid transport activity y + L. A candidate gene for lysinuric protein intolerance. J. Biol. Chem. 273, 32437-32445 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 32437-32445
    • Torrents, D.1
  • 7
    • 0022969399 scopus 로고
    • Exchange of cystine and glutamate across plasma membrane of human fibroblasts
    • Bannai, S. Exchange of cystine and glutamate across plasma membrane of human fibroblasts. J. Biol. Chem. 261, 2256-2263 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 2256-2263
    • Bannai, S.1
  • 8
    • 84926430043 scopus 로고    scopus 로고
    • Cystathionine is a novel substrate of cystine/glutamate transporter: Implications for immune function
    • Kobayashi, S. et al. Cystathionine is a novel substrate of cystine/glutamate transporter: implications for immune function. J. Biol. Chem. 290, 8778-8788 (2015).
    • (2015) J. Biol. Chem. , vol.290 , pp. 8778-8788
    • Kobayashi, S.1
  • 9
    • 0022638764 scopus 로고
    • Role of membrane transport in metabolism and function of glutathione in mammals
    • Bannai, S. & Tateishi, N. Role of membrane transport in metabolism and function of glutathione in mammals. J. Membr. Biol. 89, 1-8 (1986).
    • (1986) J. Membr. Biol. , vol.89 , pp. 1-8
    • Bannai, S.1    Tateishi, N.2
  • 10
    • 0021215013 scopus 로고
    • Transport of cystine and cysteine in mammalian cells
    • Bannai, S. Transport of cystine and cysteine in mammalian cells. Biochim. Biophys. Acta 779, 289-306 (1984).
    • (1984) Biochim. Biophys. Acta , vol.779 , pp. 289-306
    • Bannai, S.1
  • 11
    • 40449094829 scopus 로고    scopus 로고
    • The cystine/cysteine cycle: A redox cycle regulating susceptibility versus resistance to cell death
    • Banjac, A. et al. The cystine/cysteine cycle: a redox cycle regulating susceptibility versus resistance to cell death. Oncogene 27, 1618-1628 (2008).
    • (2008) Oncogene , vol.27 , pp. 1618-1628
    • Banjac, A.1
  • 12
    • 77954614863 scopus 로고    scopus 로고
    • System x(c)- and thioredoxin reductase 1 cooperatively rescue glutathione deficiency
    • Mandal, P. K. et al. System x(c)- and thioredoxin reductase 1 cooperatively rescue glutathione deficiency. J. Biol. Chem. 285, 22244-22253 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 22244-22253
    • Mandal, P.K.1
  • 13
    • 84859031263 scopus 로고    scopus 로고
    • The oxidative stress-inducible cystine/glutamate antiporter, system x(c)(-): Cystine supplier and beyond
    • Conrad, M. & Sato, H. The oxidative stress-inducible cystine/glutamate antiporter, system x(c)(-): cystine supplier and beyond. Amino Acids 42, 231-246 (2012).
    • (2012) Amino Acids , vol.42 , pp. 231-246
    • Conrad, M.1    Sato, H.2
  • 14
    • 84954538622 scopus 로고    scopus 로고
    • Main path and byways: Non-vesicular glutamate release by system xc(-) as an important modifier of glutamatergic neurotransmission
    • Massie, A., Boillee, S., Hewett, S., Knackstedt, L. & Lewerenz, J. Main path and byways: non-vesicular glutamate release by system xc(-) as an important modifier of glutamatergic neurotransmission. J. Neurochem. 135, 1062-1079 (2015).
    • (2015) J. Neurochem. , vol.135 , pp. 1062-1079
    • Massie, A.1    Boillee, S.2    Hewett, S.3    Knackstedt, L.4    Lewerenz, J.5
  • 15
    • 42949126711 scopus 로고    scopus 로고
    • The x(c)- cystine/glutamate antiporter: A potential target for therapy of cancer and other diseases
    • Lo, M., Wang, Y. Z. & Gout, P. W. The x(c)- cystine/glutamate antiporter: a potential target for therapy of cancer and other diseases. J. Cell. Physiol. 215, 593-602 (2008).
    • (2008) J. Cell. Physiol. , vol.215 , pp. 593-602
    • Lo, M.1    Wang, Y.Z.2    Gout, P.W.3
  • 16
    • 84872191631 scopus 로고    scopus 로고
    • The cystine/glutamate antiporter system x(c)(-) in health and disease: From molecular mechanisms to novel therapeutic opportunities
    • Lewerenz, J. et al. The cystine/glutamate antiporter system x(c)(-) in health and disease: from molecular mechanisms to novel therapeutic opportunities. Antioxid. Redox Signal. 18, 522-555 (2013).
    • (2013) Antioxid. Redox Signal. , vol.18 , pp. 522-555
    • Lewerenz, J.1
  • 17
    • 81055127888 scopus 로고    scopus 로고
    • System xc(-) cystine/glutamate antiporter: An update on molecular pharmacology and roles within the CNS
    • Bridges, R. J., Natale, N. R. & Patel, S. A. System xc(-) cystine/glutamate antiporter: an update on molecular pharmacology and roles within the CNS. Br. J. Pharmacol. 165, 20-34 (2012).
    • (2012) Br. J. Pharmacol. , vol.165 , pp. 20-34
    • Bridges, R.J.1    Natale, N.R.2    Patel, S.A.3
  • 19
    • 0037932865 scopus 로고    scopus 로고
    • Identification of genotype-selective antitumor agents using synthetic lethal chemical screening in engineered human tumor cells
    • Dolma, S., Lessnick, S. L., Hahn, W. C. & Stockwell, B. R. Identification of genotype-selective antitumor agents using synthetic lethal chemical screening in engineered human tumor cells. Cancer Cell 3, 285-296 (2003).
    • (2003) Cancer Cell , vol.3 , pp. 285-296
    • Dolma, S.1    Lessnick, S.L.2    Hahn, W.C.3    Stockwell, B.R.4
  • 20
    • 84861541814 scopus 로고    scopus 로고
    • Ferroptosis: An iron-dependent form of nonapoptotic cell death
    • Dixon, S. J. et al. Ferroptosis: an iron-dependent form of nonapoptotic cell death. Cell 149, 1060-1072, https://doi.org/10.1016/j. cell.2012.03.042 (2012).
    • (2012) Cell , vol.149 , pp. 1060-1072
    • Dixon, S.J.1
  • 21
    • 84901323900 scopus 로고    scopus 로고
    • Pharmacological inhibition of cystine-glutamate exchange induces endoplasmic reticulum stress and ferroptosis
    • Dixon, S. J. et al. Pharmacological inhibition of cystine-glutamate exchange induces endoplasmic reticulum stress and ferroptosis. Elife 3, e02523 (2014).
    • (2014) Elife , vol.3 , pp. e02523
    • Dixon, S.J.1
  • 22
    • 0242499988 scopus 로고    scopus 로고
    • Role of cystine transport in intracellular glutathione level and cisplatin resistance in human ovarian cancer cell lines
    • Okuno, S. et al. Role of cystine transport in intracellular glutathione level and cisplatin resistance in human ovarian cancer cell lines. Br. J. Cancer 88, 951-956 (2003).
    • (2003) Br. J. Cancer , vol.88 , pp. 951-956
    • Okuno, S.1
  • 23
    • 0347480436 scopus 로고    scopus 로고
    • Differentiation of substrate and non-substrate inhibitors of transport system xc(-): An obligate exchanger of L-glutamate and L-cystine
    • Patel, S. A., Warren, B. A., Rhoderick, J. F. & Bridges, R. J. Differentiation of substrate and non-substrate inhibitors of transport system xc(-): an obligate exchanger of L-glutamate and L-cystine. Neuropharmacology 46, 273-284 (2004).
    • (2004) Neuropharmacology , vol.46 , pp. 273-284
    • Patel, S.A.1    Warren, B.A.2    Rhoderick, J.F.3    Bridges, R.J.4
  • 24
    • 72049130253 scopus 로고    scopus 로고
    • Isoxazole analogues bind the system xc - Transporter: Structure-activity relationship and pharmacophore model
    • Patel, S. A. et al. Isoxazole analogues bind the system xc - transporter: structure-activity relationship and pharmacophore model. Bioorg. Med. Chem. 18, 202-213 (2010).
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 202-213
    • Patel, S.A.1
  • 25
    • 0034772516 scopus 로고    scopus 로고
    • Sulfasalazine a potent suppressor of lymphoma growth by inhibition of the x(c)- cystine transporter: A new action for an old drug
    • Gout, P. W., Buckley, A. R., Simms, C. R. & Bruchovsky, N. Sulfasalazine, a potent suppressor of lymphoma growth by inhibition of the x(c)- cystine transporter: a new action for an old drug. Leukemia 15, 1633-1640 (2001).
    • (2001) Leukemia , vol.15 , pp. 1633-1640
    • Gout, P.W.1    Buckley, A.R.2    Simms, C.R.3    Bruchovsky, N.4
  • 26
    • 1642524280 scopus 로고    scopus 로고
    • Thiol modification of cysteine 327 in the eighth transmembrane domain of the light subunit xCT of the heteromeric cystine/glutamate antiporter suggests close proximity to the substrate binding site/permeation pathway
    • Jimenez-Vidal, M. et al. Thiol modification of cysteine 327 in the eighth transmembrane domain of the light subunit xCT of the heteromeric cystine/glutamate antiporter suggests close proximity to the substrate binding site/permeation pathway. J. Biol. Chem. 279, 11214-11221 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 11214-11221
    • Jimenez-Vidal, M.1
  • 27
    • 34250372956 scopus 로고    scopus 로고
    • RAS-RAF-MEK-dependent oxidative cell death involving voltage-dependent anion channels
    • Yagoda, N. et al. RAS-RAF-MEK-dependent oxidative cell death involving voltage-dependent anion channels. Nature 447, 864-868 (2007).
    • (2007) Nature , vol.447 , pp. 864-868
    • Yagoda, N.1
  • 28
    • 0030885408 scopus 로고    scopus 로고
    • Increased cystine uptake capability associated with malignant progression of Nb2 lymphoma cells
    • Gout, P. W., Kang, Y. J., Buckley, D. J., Bruchovsky, N. & Buckley, A. R. Increased cystine uptake capability associated with malignant progression of Nb2 lymphoma cells. Leukemia 11, 1329-1337 (1997).
    • (1997) Leukemia , vol.11 , pp. 1329-1337
    • Gout, P.W.1    Kang, Y.J.2    Buckley, D.J.3    Bruchovsky, N.4    Buckley, A.R.5
  • 29
    • 23844486685 scopus 로고    scopus 로고
    • Cystine-glutamate transporter SLC7A11 in cancer chemosensitivity and chemoresistance
    • Huang, Y., Dai, Z., Barbacioru, C. & Sadee, W. Cystine-glutamate transporter SLC7A11 in cancer chemosensitivity and chemoresistance. Cancer Res. 65, 7446-7454 (2005).
    • (2005) Cancer Res. , vol.65 , pp. 7446-7454
    • Huang, Y.1    Dai, Z.2    Barbacioru, C.3    Sadee, W.4
  • 30
    • 23444449591 scopus 로고    scopus 로고
    • Inhibition of cystine uptake disrupts the growth of primary brain tumors
    • Chung, W. J. et al. Inhibition of cystine uptake disrupts the growth of primary brain tumors. J. Neurosci. 25, 7101-7110 (2005).
    • (2005) J. Neurosci. , vol.25 , pp. 7101-7110
    • Chung, W.J.1
  • 32
    • 44949122670 scopus 로고    scopus 로고
    • Small interfering RNA-mediated xCT silencing in gliomas inhibits neurodegeneration and alleviates brain edema
    • Savaskan, N. E. et al. Small interfering RNA-mediated xCT silencing in gliomas inhibits neurodegeneration and alleviates brain edema. Nat. Med. 14, 629-632 (2008).
    • (2008) Nat. Med. , vol.14 , pp. 629-632
    • Savaskan, N.E.1
  • 33
    • 79952528125 scopus 로고    scopus 로고
    • CD44 variant regulates redox status in cancer cells by stabilizing the xCT subunit of system xc(-) and thereby promotes tumor growth
    • Ishimoto, T. et al. CD44 variant regulates redox status in cancer cells by stabilizing the xCT subunit of system xc(-) and thereby promotes tumor growth. Cancer Cell 19, 387-400 (2011).
    • (2011) Cancer Cell , vol.19 , pp. 387-400
    • Ishimoto, T.1
  • 34
    • 84926387317 scopus 로고    scopus 로고
    • Ferroptosis as a p53-mediated activity during tumour suppression
    • Jiang, L. et al. Ferroptosis as a p53-mediated activity during tumour suppression. Nature 520, 57-62 (2015).
    • (2015) Nature , vol.520 , pp. 57-62
    • Jiang, L.1
  • 35
    • 80052916095 scopus 로고    scopus 로고
    • Inhibition of xc(-) transporter-mediated cystine uptake by sulfasalazine analogs
    • Shukla, K. et al. Inhibition of xc(-) transporter-mediated cystine uptake by sulfasalazine analogs. Bioorg. Med. Chem. Lett. 21, 6184-6187 (2011).
    • (2011) Bioorg. Med. Chem. Lett. , vol.21 , pp. 6184-6187
    • Shukla, K.1
  • 36
    • 33144461875 scopus 로고    scopus 로고
    • A phase 1-2, prospective, double blind, randomized study of the safety and efficacy of Sulfasalazine for the treatment of progressing malignant gliomas: Study protocol of [ISRCTN45828668]
    • Robe, P. A. et al. A phase 1-2, prospective, double blind, randomized study of the safety and efficacy of Sulfasalazine for the treatment of progressing malignant gliomas: study protocol of [ISRCTN45828668]. BMC Cancer 6, 29 (2006).
    • (2006) BMC Cancer , vol.6 , pp. 29
    • Robe, P.A.1
  • 37
    • 70450228522 scopus 로고    scopus 로고
    • Early termination of ISRCTN45828668, a phase 1/2 prospective, randomized study of sulfasalazine for the treatment of progressing malignant gliomas in adults
    • Robe, P. A. et al. Early termination of ISRCTN45828668, a phase 1/2 prospective, randomized study of sulfasalazine for the treatment of progressing malignant gliomas in adults. BMC Cancer 9, 372 (2009).
    • (2009) BMC Cancer , vol.9 , pp. 372
    • Robe, P.A.1
  • 38
    • 84979872952 scopus 로고    scopus 로고
    • Induction of ferroptotic cell death for overcoming cisplatin resistance of head and neck cancer
    • Roh, J. L., Kim, E. H., Jang, H. J., Park, J. Y. & Shin, D. Induction of ferroptotic cell death for overcoming cisplatin resistance of head and neck cancer. Cancer Lett. 381, 96-103 (2016).
    • (2016) Cancer Lett. , vol.381 , pp. 96-103
    • Roh, J.L.1    Kim, E.H.2    Jang, H.J.3    Park, J.Y.4    Shin, D.5
  • 39
    • 50049133588 scopus 로고    scopus 로고
    • Glutathione peroxidase 4 senses and translates oxidative stress into 12/15-lipoxygenase dependent- and AIFmediated cell death
    • Seiler, A. et al. Glutathione peroxidase 4 senses and translates oxidative stress into 12/15-lipoxygenase dependent- and AIFmediated cell death. Cell Metab. 8, 237-248 (2008).
    • (2008) Cell Metab. , vol.8 , pp. 237-248
    • Seiler, A.1
  • 40
    • 84901610814 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinases upregulate system xc(-) via eukaryotic initiation factor 2alpha and activating transcription factor 4 - A pathway active in glioblastomas and epilepsy
    • Lewerenz, J. et al. Phosphoinositide 3-kinases upregulate system xc(-) via eukaryotic initiation factor 2alpha and activating transcription factor 4 - A pathway active in glioblastomas and epilepsy. Antioxid. Redox Signal. 20, 2907-2922 (2014).
    • (2014) Antioxid. Redox Signal. , vol.20 , pp. 2907-2922
    • Lewerenz, J.1
  • 41
    • 0032505716 scopus 로고    scopus 로고
    • A composite CMV-IE enhancer/beta-actin promoter is ubiquitously expressed in mouse cutaneous epithelium
    • Sawicki, J. A., Morris, R. J., Monks, B., Sakai, K. & Miyazaki, J. A composite CMV-IE enhancer/beta-actin promoter is ubiquitously expressed in mouse cutaneous epithelium. Exp. Cell Res. 244, 367-369 (1998).
    • (1998) Exp. Cell Res. , vol.244 , pp. 367-369
    • Sawicki, J.A.1    Morris, R.J.2    Monks, B.3    Sakai, K.4    Miyazaki, J.5
  • 42
    • 27844530663 scopus 로고    scopus 로고
    • Redox imbalance in cystine/glutamate transporter-deficient mice
    • Sato, H. et al. Redox imbalance in cystine/glutamate transporter-deficient mice. J. Biol. Chem. 280, 37423-37429 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 37423-37429
    • Sato, H.1
  • 43
    • 0033009895 scopus 로고    scopus 로고
    • Co-expression of gamma-glutamylcysteine synthetase sub-units in response to cisplatin and doxorubicin in human cancer cells
    • Iida, T. et al. Co-expression of gamma-glutamylcysteine synthetase sub-units in response to cisplatin and doxorubicin in human cancer cells. Int. J. Cancer 82, 405-411 (1999).
    • (1999) Int. J. Cancer , vol.82 , pp. 405-411
    • Iida, T.1
  • 44
    • 0014481378 scopus 로고
    • Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: Applications to mammalian blood and other tissues
    • Tietze, F. Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal. Biochem. 27, 502-522 (1969).
    • (1969) Anal. Biochem. , vol.27 , pp. 502-522
    • Tietze, F.1
  • 45
    • 0024991898 scopus 로고
    • PEF-BOS, a powerful mammalian expression vector
    • Mizushima, S. & Nagata, S. pEF-BOS, a powerful mammalian expression vector. Nucleic Acids Res. 18, 5322 (1990).
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5322
    • Mizushima, S.1    Nagata, S.2


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