메뉴 건너뛰기




Volumn 6, Issue 12, 2015, Pages 10146-10160

Targeting the degradation of AXL receptor tyrosine kinase to overcome resistance in gefitinib-resistant non-small cell lung cancer

Author keywords

AXL; EGFR TKI resistance; NSCLC; PS RIP; Yuanhuadine

Indexed keywords

ANTINEOPLASTIC AGENT; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; CHLOROQUINE; GEFITINIB; PRESENILIN; PROTEIN AXL; PROTEIN TYROSINE KINASE; UNCLASSIFIED DRUG; YUANHUADINE; AXL RECEPTOR TYROSINE KINASE; ONCOPROTEIN; PROTEIN KINASE INHIBITOR; QUINAZOLINE DERIVATIVE;

EID: 84929573682     PISSN: None     EISSN: 19492553     Source Type: Journal    
DOI: 10.18632/oncotarget.3380     Document Type: Article
Times cited : (62)

References (34)
  • 3
    • 18244371651 scopus 로고    scopus 로고
    • Acquired resistance of lung adenocarcinomas to gefitinib or erlotinib is associated with a second mutation in the EGFR kinase domain
    • Pao W, Miller VA, Politi KA, Riely GJ, Somwar R, Zakowski MF, Kris MG, Varmus H. Acquired resistance of lung adenocarcinomas to gefitinib or erlotinib is associated with a second mutation in the EGFR kinase domain. PLoS Med. 2005; 2:e73.
    • (2005) PLoS Med , vol.2 , pp. e73
    • Pao, W.1    Miller, V.A.2    Politi, K.A.3    Riely, G.J.4    Somwar, R.5    Zakowski, M.F.6    Kris, M.G.7    Varmus, H.8
  • 4
    • 84868320526 scopus 로고    scopus 로고
    • Strategies for overcoming acquired resistance to epidermal growth factor receptor: targeted therapies in lung cancer
    • Oxnard GR. Strategies for overcoming acquired resistance to epidermal growth factor receptor: targeted therapies in lung cancer. Arch Pathol Lab Med. 2012; 136:1205-1209.
    • (2012) Arch Pathol Lab Med , vol.136 , pp. 1205-1209
    • Oxnard, G.R.1
  • 5
    • 84856886733 scopus 로고    scopus 로고
    • Treatment of nonsmall cell lung cancer: overcoming the resistance to epidermal growth factor receptor inhibitors
    • Carter CA, Giaccone G. Treatment of nonsmall cell lung cancer: overcoming the resistance to epidermal growth factor receptor inhibitors. Curr Opin Oncol. 2012; 24:123-129.
    • (2012) Curr Opin Oncol , vol.24 , pp. 123-129
    • Carter, C.A.1    Giaccone, G.2
  • 6
    • 84871998076 scopus 로고    scopus 로고
    • An epithelial-mesenchymal transition gene signature predicts resistance to EGFR and PI3K inhibitors and identifies Axl as a therapeutic target for overcoming EGFR inhibitor resistance
    • Byers LA, Diao L, Wang J, Saintigny P, Girard L, Peyton M, Shen L, Fan Y, Giri U, Tumula PK, Nilsson MB, Gudikote J, Tran H, et al. An epithelial-mesenchymal transition gene signature predicts resistance to EGFR and PI3K inhibitors and identifies Axl as a therapeutic target for overcoming EGFR inhibitor resistance. Clin Cancer Res. 2013; 19:279-290.
    • (2013) Clin Cancer Res , vol.19 , pp. 279-290
    • Byers, L.A.1    Diao, L.2    Wang, J.3    Saintigny, P.4    Girard, L.5    Peyton, M.6    Shen, L.7    Fan, Y.8    Giri, U.9    Tumula, P.K.10    Nilsson, M.B.11    Gudikote, J.12    Tran, H.13
  • 8
    • 33745814436 scopus 로고    scopus 로고
    • Signalling and functional diversity within the Axl subfamily of receptor tyrosine kinases
    • Hafizi S, Dahlback B. Signalling and functional diversity within the Axl subfamily of receptor tyrosine kinases. Cytokine Growth Factor Rev. 2006; 17:295-304.
    • (2006) Cytokine Growth Factor Rev , vol.17 , pp. 295-304
    • Hafizi, S.1    Dahlback, B.2
  • 9
    • 84857065479 scopus 로고    scopus 로고
    • Axl-dependent signalling: a clinical update
    • Korshunov VA. Axl-dependent signalling: a clinical update. Clin Sci (Lond). 2012; 122:361-368.
    • (2012) Clin Sci (Lond) , vol.122 , pp. 361-368
    • Korshunov, V.A.1
  • 10
    • 77957092501 scopus 로고    scopus 로고
    • Taking aim at Mer and Axl receptor tyrosine kinases as novel therapeutic targets in solid tumors
    • Linger RM, Keating AK, Earp HS, Graham DK. Taking aim at Mer and Axl receptor tyrosine kinases as novel therapeutic targets in solid tumors. Expert Opin Ther Targets. 2010; 14:1073-1090.
    • (2010) Expert Opin Ther Targets , vol.14 , pp. 1073-1090
    • Linger, R.M.1    Keating, A.K.2    Earp, H.S.3    Graham, D.K.4
  • 12
    • 4143083728 scopus 로고    scopus 로고
    • Intracellular signaling pathways involved in Gas6-Axlmediated survival of endothelial cells
    • Hasanbasic I, Cuerquis J, Varnum B, Blostein MD. Intracellular signaling pathways involved in Gas6-Axlmediated survival of endothelial cells. Am J Physiol Heart Circ Physiol. 2004; 287:H1207-1213.
    • (2004) Am J Physiol Heart Circ Physiol , vol.287 , pp. H1207-1213
    • Hasanbasic, I.1    Cuerquis, J.2    Varnum, B.3    Blostein, M.D.4
  • 13
    • 85047698138 scopus 로고    scopus 로고
    • Akt is required for Axl-Gas6 signaling to protect cells from E1A-mediated apoptosis
    • Lee WP, Wen Y, Varnum B, Hung MC. Akt is required for Axl-Gas6 signaling to protect cells from E1A-mediated apoptosis. Oncogene. 2002; 21:329-336.
    • (2002) Oncogene , vol.21 , pp. 329-336
    • Lee, W.P.1    Wen, Y.2    Varnum, B.3    Hung, M.C.4
  • 14
    • 48549094691 scopus 로고    scopus 로고
    • Receptor tyrosine kinase AXL is induced by chemotherapy drugs and overexpression of AXL confers drug resistance in acute myeloid leukemia
    • Hong CC, Lay JD, Huang JS, Cheng AL, Tang JL, Lin MT, Lai GM, Chuang SE. Receptor tyrosine kinase AXL is induced by chemotherapy drugs and overexpression of AXL confers drug resistance in acute myeloid leukemia. Cancer Lett. 2008; 268:314-324.
    • (2008) Cancer Lett , vol.268 , pp. 314-324
    • Hong, C.C.1    Lay, J.D.2    Huang, J.S.3    Cheng, A.L.4    Tang, J.L.5    Lin, M.T.6    Lai, G.M.7    Chuang, S.E.8
  • 15
    • 67349106681 scopus 로고    scopus 로고
    • Proteolytic cleavages give receptor tyrosine kinases the gift of ubiquity
    • Ancot F, Foveau B, Lefebvre J, Leroy C, Tulasne D. Proteolytic cleavages give receptor tyrosine kinases the gift of ubiquity. Oncogene. 2009; 28:2185-2195.
    • (2009) Oncogene , vol.28 , pp. 2185-2195
    • Ancot, F.1    Foveau, B.2    Lefebvre, J.3    Leroy, C.4    Tulasne, D.5
  • 16
    • 4344624361 scopus 로고    scopus 로고
    • Got RIP? Presenilin-dependent intramembrane proteolysis in growth factor receptor signaling
    • Landman N, Kim TW. Got RIP? Presenilin-dependent intramembrane proteolysis in growth factor receptor signaling. Cytokine Growth Factor Rev. 2004; 15:337-351.
    • (2004) Cytokine Growth Factor Rev , vol.15 , pp. 337-351
    • Landman, N.1    Kim, T.W.2
  • 18
    • 0037059458 scopus 로고    scopus 로고
    • Vascular origin of a soluble truncated form of the hepatocyte growth factor receptor (c-met)
    • Wajih N, Walter J, Sane DC. Vascular origin of a soluble truncated form of the hepatocyte growth factor receptor (c-met). Circ Res. 2002; 90:46-52.
    • (2002) Circ Res , vol.90 , pp. 46-52
    • Wajih, N.1    Walter, J.2    Sane, D.C.3
  • 19
    • 80055067832 scopus 로고    scopus 로고
    • Growth inhibition of human lung cancer cells via down-regulation of epidermal growth factor receptor signaling by yuanhuadine, a daphnane diterpene from Daphne genkwa
    • Hong JY, Chung HJ, Lee HJ, Park HJ, Lee SK. Growth inhibition of human lung cancer cells via down-regulation of epidermal growth factor receptor signaling by yuanhuadine, a daphnane diterpene from Daphne genkwa. J Nat Prod. 2011; 74:2102-2108.
    • (2011) J Nat Prod , vol.74 , pp. 2102-2108
    • Hong, J.Y.1    Chung, H.J.2    Lee, H.J.3    Park, H.J.4    Lee, S.K.5
  • 20
    • 76149099282 scopus 로고    scopus 로고
    • Daphnane diterpene esters with anti-proliferative activities against human lung cancer cells from Daphne genkwa
    • Hong JY, Nam JW, Seo EK, Lee SK. Daphnane diterpene esters with anti-proliferative activities against human lung cancer cells from Daphne genkwa. Chem Pharm Bull (Tokyo). 2010; 58:234-237.
    • (2010) Chem Pharm Bull (Tokyo) , vol.58 , pp. 234-237
    • Hong, J.Y.1    Nam, J.W.2    Seo, E.K.3    Lee, S.K.4
  • 21
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans
    • Brown MS, Ye J, Rawson RB, Goldstein JL. Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell. 2000; 100:391-398.
    • (2000) Cell , vol.100 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 22
    • 33644876133 scopus 로고    scopus 로고
    • Expression of axl in lung adenocarcinoma and correlation with tumor progression
    • Shieh YS, Lai CY, Kao YR, Shiah SG, Chu YW, Lee HS, Wu CW. Expression of axl in lung adenocarcinoma and correlation with tumor progression. Neoplasia. 2005; 7:1058-1064.
    • (2005) Neoplasia , vol.7 , pp. 1058-1064
    • Shieh, Y.S.1    Lai, C.Y.2    Kao, Y.R.3    Shiah, S.G.4    Chu, Y.W.5    Lee, H.S.6    Wu, C.W.7
  • 26
    • 84884167635 scopus 로고    scopus 로고
    • The receptor AXL diversifies EGFR signaling and limits the response to EGFR-targeted inhibitors in triple-negative breast cancer cells
    • Meyer AS, Miller MA, Gertler FB, Lauffenburger DA. The receptor AXL diversifies EGFR signaling and limits the response to EGFR-targeted inhibitors in triple-negative breast cancer cells. Sci Signal. 2013; 6:ra66.
    • (2013) Sci Signal , vol.6 , pp. ra66
    • Meyer, A.S.1    Miller, M.A.2    Gertler, F.B.3    Lauffenburger, D.A.4
  • 27
    • 2942557122 scopus 로고    scopus 로고
    • Gamma-secretase: proteasome of the membrane?
    • Kopan R, Ilagan MX. Gamma-secretase: proteasome of the membrane?. Nat Rev Mol Cell Biol. 2004; 5:499-504.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 499-504
    • Kopan, R.1    Ilagan, M.X.2
  • 28
    • 0028938732 scopus 로고
    • The transforming receptor tyrosine kinase, Axl, is post-translationally regulated by proteolytic cleavage
    • O'Bryan JP, Fridell YW, Koski R, Varnum B, Liu ET. The transforming receptor tyrosine kinase, Axl, is post-translationally regulated by proteolytic cleavage. J Biol Chem. 1995; 270:551-557.
    • (1995) J Biol Chem , vol.270 , pp. 551-557
    • O'Bryan, J.P.1    Fridell, Y.W.2    Koski, R.3    Varnum, B.4    Liu, E.T.5
  • 29
    • 0346363758 scopus 로고    scopus 로고
    • Phorbol 12-myristate 13-acetate-induced release of the colony-stimulating factor 1 receptor cytoplasmic domain into the cytosol involves two separate cleavage events
    • Wilhelmsen K, van der Geer P. Phorbol 12-myristate 13-acetate-induced release of the colony-stimulating factor 1 receptor cytoplasmic domain into the cytosol involves two separate cleavage events. Mol Cell Biol. 2004; 24:454-464.
    • (2004) Mol Cell Biol , vol.24 , pp. 454-464
    • Wilhelmsen, K.1    van der Geer, P.2
  • 30
    • 0035824391 scopus 로고    scopus 로고
    • gamma-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase
    • Ni CY, Murphy MP, Golde TE, Carpenter G. gamma-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase. Science. 2001; 294:2179-2181.
    • (2001) Science , vol.294 , pp. 2179-2181
    • Ni, C.Y.1    Murphy, M.P.2    Golde, T.E.3    Carpenter, G.4
  • 31
    • 8444243682 scopus 로고    scopus 로고
    • The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone
    • Williams CC, Allison JG, Vidal GA, Burow ME, Beckman BS, Marrero L, Jones FE. The ERBB4/HER4 receptor tyrosine kinase regulates gene expression by functioning as a STAT5A nuclear chaperone. J Cell Biol. 2004; 167:469-478.
    • (2004) J Cell Biol , vol.167 , pp. 469-478
    • Williams, C.C.1    Allison, J.G.2    Vidal, G.A.3    Burow, M.E.4    Beckman, B.S.5    Marrero, L.6    Jones, F.E.7
  • 33
    • 84871605340 scopus 로고    scopus 로고
    • Antiproliferative effect of (19Z)-halichondramide, a novel marine macrolide isolated from the sponge Chondrosia corticata, is associated with G2/M cell cycle arrest and suppression of mTOR signaling in human lung cancer cells
    • Bae SY, Kim GD, Jeon JE, Shin J, Lee SK. Antiproliferative effect of (19Z)-halichondramide, a novel marine macrolide isolated from the sponge Chondrosia corticata, is associated with G2/M cell cycle arrest and suppression of mTOR signaling in human lung cancer cells. Toxicol In Vitro. 2013; 27:694-699.
    • (2013) Toxicol In Vitro , vol.27 , pp. 694-699
    • Bae, S.Y.1    Kim, G.D.2    Jeon, J.E.3    Shin, J.4    Lee, S.K.5
  • 34
    • 33748794547 scopus 로고    scopus 로고
    • Theoretical basis, experimental design, and computerized simulation of synergism and antagonism in drug combination studies
    • Chou TC. Theoretical basis, experimental design, and computerized simulation of synergism and antagonism in drug combination studies. Pharmacol Rev. 2006; 58:621-681.
    • (2006) Pharmacol Rev , vol.58 , pp. 621-681
    • Chou, T.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.