메뉴 건너뛰기




Volumn 30, Issue 8, 2010, Pages 3107-3112

Emerging strategies for ErbB ligand-based targeted therapy for cancer

Author keywords

Cancer; HB EGF; Review; Targeted therapy

Indexed keywords

CETUXIMAB; DIPHTHERIA TOXOID CRM197; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIDERMAL GROWTH FACTOR RECEPTOR KINASE INHIBITOR; ERLOTINIB; PACLITAXEL; TRASTUZUMAB; ANTINEOPLASTIC AGENT; EPIDERMAL GROWTH FACTOR RECEPTOR 2; LIGAND;

EID: 77957373100     PISSN: 02507005     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (15)

References (36)
  • 1
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • Blume-Jensen P and Hunter T: Oncogenic kinase signalling. Nature 411: 355-365, 2001.
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 2
    • 0028955388 scopus 로고
    • Epidermal growth factor-related peptides and their receptors in human malignancies
    • Salomon DS, Brandt R, Ciardiello F and Normando N: Epidermal growth factor-related peptides and their receptors in human malignancies. Crit Rev Oncol Hematol 19: 183-232, 1995.
    • (1995) Crit Rev Oncol Hematol , vol.19 , pp. 183-232
    • Salomon, D.S.1    Brandt, R.2    Ciardiello, F.3    Normando, N.4
  • 3
    • 0034600849 scopus 로고    scopus 로고
    • The ErbB signaling network: Receptor heterodimerization in development and cancer
    • Olayioye MA, Neve RM, Lane HA and Hynes NE: The ErbB signaling network: receptor heterodimerization in development and cancer. EMBO J 19: 3159-3167, 2000.
    • (2000) EMBO J , vol.19 , pp. 3159-3167
    • Olayioye, M.A.1    Neve, R.M.2    Lane, H.A.3    Hynes, N.E.4
  • 4
    • 0037291769 scopus 로고    scopus 로고
    • EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization
    • Ferguson KM, Berger MB, Mendrola JM, Cho HS, Leahy DJ and Lemmon MA: EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization. Mol Cell 11: 507-517, 2003.
    • (2003) Mol Cell , vol.11 , pp. 507-517
    • Ferguson, K.M.1    Berger, M.B.2    Mendrola, J.M.3    Cho, H.S.4    Leahy, D.J.5    Lemmon, M.A.6
  • 5
    • 0037162799 scopus 로고    scopus 로고
    • Structure of the extracellular region of HER3 reveals an interdomain tether
    • Cho HS and Leahy DJ: Structure of the extracellular region of HER3 reveals an interdomain tether. Science 297: 1330-1333, 2002.
    • (2002) Science , vol.297 , pp. 1330-1333
    • Cho, H.S.1    Leahy, D.J.2
  • 7
    • 67649472398 scopus 로고    scopus 로고
    • Novel anticancer targets: Revisiting ERBB2 and discovering ERBB3
    • Baselga J and Swain SM: Novel anticancer targets: revisiting ERBB2 and discovering ERBB3. Nat Rev Cancer 9: 463-475, 2009.
    • (2009) Nat Rev Cancer , vol.9 , pp. 463-475
    • Baselga, J.1    Swain, S.M.2
  • 9
    • 3042800393 scopus 로고    scopus 로고
    • ErbB3/Her3 does not homodimerize upon neuregulin binding at the cell surface
    • Berger MB, Mendrola JM and Lemmon MA: ErbB3/Her3 does not homodimerize upon neuregulin binding at the cell surface. FEBS lett 569: 332-336, 2004.
    • (2004) FEBS Lett , vol.569 , pp. 332-336
    • Berger, M.B.1    Mendrola, J.M.2    Lemmon, M.A.3
  • 10
    • 18344390418 scopus 로고    scopus 로고
    • ERBB receptors and cancer: The complexity of targeted inhibitors
    • Hynes NE and Lane HA: ERBB receptors and cancer: the complexity of targeted inhibitors. Nat Rev Cancer 5: 341-354, 2005.
    • (2005) Nat Rev Cancer , vol.5 , pp. 341-354
    • Hynes, N.E.1    Lane, H.A.2
  • 11
    • 33644529055 scopus 로고    scopus 로고
    • ErbB2 increases vascular endothelial growth factor protein synthesis via activation of mammalian target of rapamycin/p70S6K leading to increased angiogenesis and spontaneous metastasis of human breast cancer cells
    • DOI 10.1158/0008-5472.CAN-04-4559
    • Klos KS, Wyszomierski SL, Sun M, Tan M, Zhou X, Li P, Yang W, Yin G, Hittelman WN and Yu D: ErbB2 increases vascular endothelial growth factor protein synthesis via activation of mammalian target of rapamycin/p70S6K leading to increased angiogenesis and spontaneous metastasis of human breast cancer cells. Cancer Res 66: 2028-2037, 2006. (Pubitemid 43294911)
    • (2006) Cancer Research , vol.66 , Issue.4 , pp. 2028-2037
    • Klos, K.S.1    Wyszomierski, S.L.2    Sun, M.3    Tan, M.4    Zhou, X.5    Li, P.6    Yang, W.7    Yin, G.8    Hittelman, W.N.9    Yu, D.10
  • 12
    • 33745828702 scopus 로고    scopus 로고
    • EGF-ERBB signalling: Towards the systems level
    • Citri A and Yarden Y: EGF-ERBB signalling: towards the systems level. Nat Rev Mol Cell Biol 7: 505-516, 2006.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 505-516
    • Citri, A.1    Yarden, Y.2
  • 13
    • 33747855481 scopus 로고    scopus 로고
    • Comparing antibody and small-molecule therapies for cancer
    • DOI 10.1038/nrc1913, PII NRC1913
    • Imai K and Takaoka A: Comparing antibody and small-molecule therapies for cancer. Nat Rev Cancer 6: 714-727, 2006. (Pubitemid 44286003)
    • (2006) Nature Reviews Cancer , vol.6 , Issue.9 , pp. 714-727
    • Imai, K.1    Takaoka, A.2
  • 14
    • 46749144174 scopus 로고    scopus 로고
    • Mechanisms of resistance to ErbB-targeted cancer therapeutics
    • Wang Q and Greene MI: Mechanisms of resistance to ErbB-targeted cancer therapeutics. J Clin Invest 118: 2389-2392, 2008.
    • (2008) J Clin Invest , vol.118 , pp. 2389-2392
    • Wang, Q.1    Greene, M.I.2
  • 16
    • 63749101351 scopus 로고    scopus 로고
    • Targeting the EGFR and the PKB pathway in cancer
    • Klein S and Levitzki A: Targeting the EGFR and the PKB pathway in cancer. Curr Opin Cell Biol 21: 185-193, 2009.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 185-193
    • Klein, S.1    Levitzki, A.2
  • 17
    • 33645540607 scopus 로고    scopus 로고
    • Heparin-binding epidermal growth factor-like growth factor as a novel targeting molecule for cancer therapy
    • Miyamoto S, Yagi H, Yotsumoto F, Kawarabayashi T and Mekada E: Heparin-binding epidermal growth factor-like growth factor as a novel targeting molecule for cancer therapy. Cancer Sci 97: 341-347, 2006.
    • (2006) Cancer Sci , vol.97 , pp. 341-347
    • Miyamoto, S.1    Yagi, H.2    Yotsumoto, F.3    Kawarabayashi, T.4    Mekada, E.5
  • 19
    • 22744450061 scopus 로고    scopus 로고
    • ADAM-mediated ectodomain shedding of HB-EGF in receptor cross-talk
    • DOI 10.1016/j.bbapap.2004.11.009, PII S1570963904003188, Proteolysis
    • Higashiyama S and Nanba D: ADAM-mediated ectodomain shedding of HB-EGF in receptor cross-talk. Biochim Biophys Acta 1751: 110-117, 2005. (Pubitemid 41033299)
    • (2005) Biochimica et Biophysica Acta - Proteins and Proteomics , vol.1751 , Issue.1 , pp. 110-117
    • Higashiyama, S.1    Nanba, D.2
  • 20
    • 0025904265 scopus 로고
    • A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF
    • Higashiyama S, Abraham JA, Miller J, Fiddes JC and Klagsbrun M: A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF. Science 251: 936-939, 1991.
    • (1991) Science , vol.251 , pp. 936-939
    • Higashiyama, S.1    Abraham, J.A.2    Miller, J.3    Fiddes, J.C.4    Klagsbrun, M.5
  • 21
    • 17444373968 scopus 로고    scopus 로고
    • A metalloprotease-disintegrin MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor
    • Izumi Y, Hirata M, Hasuwa H, Iwamoto R, Umeta T, Miyado K, Tamai Y, Kurisaki T, Sehara-Fujisawa A, Ohno S and Mekada E: A metalloprotease- disintegrin MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor. EMBO J 17: 7260-7272, 1998.
    • (1998) EMBO J , vol.17 , pp. 7260-7272
    • Izumi, Y.1    Hirata, M.2    Hasuwa, H.3    Iwamoto, R.4    Umeta, T.5    Miyado, K.6    Tamai, Y.7    Kurisaki, T.8    Sehara-Fujisawa, A.9    Ohno, S.10    Mekada, E.11
  • 22
    • 0037224740 scopus 로고    scopus 로고
    • The ADAMs family of metalloproteases: Multidomain proteins with multiple functions
    • Seals DF and Coutneidges SA: The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev 17: 7-30, 1998.
    • (1998) Genes Dev , vol.17 , pp. 7-30
    • Seals, D.F.1    Coutneidges, S.A.2
  • 23
    • 0033599039 scopus 로고    scopus 로고
    • EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF
    • Prenzel N, Zwick E, Daub H, Laserer M, Abraham R, Wallasch C and Ullrich A: EGF receptor transactivation by G-protein-coupled receptor requires metalloproteases cleavage of proHB-EGF. Nature 402: 884-888, 1999. (Pubitemid 129515992)
    • (1999) Nature , vol.402 , Issue.6764 , pp. 884-888
    • Prenzel, N.1    Zwick, E.2    Daub, H.3    Leserer, M.4    Abraham, R.5    Wallasch, C.6    Ullrich, A.7
  • 24
    • 0037593847 scopus 로고    scopus 로고
    • The stress- and inflammatory cytokine-induced ectodomain shedding of heparin-binding epidermal growth factor-like growth factor is mediated by p38 MAPK, distinct from the 12-O-tetradecanoylphorbol-13-acetate- and lysophosphatidic acid-induced signaling cascades
    • Takenobu H, Yamazaki A, Hirata M, Umeta T and Mekada E: The stress- and inflammatory cytokine-induced ectodomain shedding of heparin-binding epidermal growth factor-like growth factor is mediated by p38 MAPK, distinct from the 12-O-tetradecanoylphorbol-13-acetate- and lysophosphatidic acid-induced signaling cascades. J Biol Chem 278: 17255-17262, 2003.
    • (2003) J Biol Chem , vol.278 , pp. 17255-17262
    • Takenobu, H.1    Yamazaki, A.2    Hirata, M.3    Umeta, T.4    Mekada, E.5
  • 25
    • 0242425875 scopus 로고    scopus 로고
    • Proteolytic release of the carboxy-terminal fragment of proHB-EGF causes nuclear export of PLZF
    • Nanba D, Mammoto A, Hashimoto K and Higashiyama S: Proteolytic release of the carboxy-terminal fragment of proHB-EGF causes nuclear export of PLZF. J Cell Biol 163: 489-502, 2003.
    • (2003) J Cell Biol , vol.163 , pp. 489-502
    • Nanba, D.1    Mammoto, A.2    Hashimoto, K.3    Higashiyama, S.4
  • 26
    • 34447529461 scopus 로고    scopus 로고
    • The carboxyl-terminal fragment of pro-HB-EGF reverses Bcl6-mediated gene repression
    • DOI 10.1074/jbc.M611036200
    • Kinugasa Y, Hieda M, Hori M and Higashiyama S: The carboxyl-terminal fragment of pro-HB-EGF reverses Bcl6-mediated gene repression. J Biol Chem 282: 14797-14806, 2007. (Pubitemid 47093367)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.20 , pp. 14797-14806
    • Kinugasa, Y.1    Hieda, M.2    Hori, M.3    Higashiyama, S.4
  • 27
    • 0035839518 scopus 로고    scopus 로고
    • BAG-1 is a novel cytoplasmic binding partner of the membrane form of heparin-binding EGF-like growth factor: A unique role for proHB-EGF in cell survival regulation
    • Lin J, Hutchinson L, Gaston SM, Raab G and Freeman MR: BAG-1 is a novel cytoplasmic binding partner of the membrane form of heparin-binding EGF-like growth factor: a unique role for proHB-EGF in cell survival regulation. J Biol Chem 276: 30127-30132, 2001.
    • (2001) J Biol Chem , vol.276 , pp. 30127-30132
    • Lin, J.1    Hutchinson, L.2    Gaston, S.M.3    Raab, G.4    Freeman, M.R.5
  • 29
    • 19944391895 scopus 로고    scopus 로고
    • Clinical significance of heparin-binding epidermal growth factor-like growth factor in peritoneal fluid of ovarian cancer
    • Yagi H, Miyamoto S, Tanaka Y, Sonoda K, Kobayashi H, Kishikawa T, Iwamoto R, Mekada E and Nakano H: Clinical significance of heparin-binding epidermal growth factor-like growth factor in peritoneal fluid of ovarian cancer. Br J Cancer 92: 1737-1745, 2005.
    • (2005) Br J Cancer , vol.92 , pp. 1737-1745
    • Yagi, H.1    Miyamoto, S.2    Tanaka, Y.3    Sonoda, K.4    Kobayashi, H.5    Kishikawa, T.6    Iwamoto, R.7    Mekada, E.8    Nakano, H.9
  • 30
    • 0028860250 scopus 로고
    • Diphtheria toxin binds to the epidermal growth factor (EGF)-like domain of human heparin-binding EGF-like growth factor/diphtheria toxin receptor and inhibits specifically its mitogenic activity
    • Mitamura T, Higashiyama S, Taniguchi N, Klagsbrun M and Mekada E: Diphtheria toxin binds to the epidermal growth factor (EGF)-like domain of human heparin-binding EGF-like growth factor/diphtheria toxin receptor and inhibits specifically its mitogenic activity. J Biol Chem 270: 1015-1019, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 1015-1019
    • Mitamura, T.1    Higashiyama, S.2    Taniguchi, N.3    Klagsbrun, M.4    Mekada, E.5
  • 31
    • 27644466636 scopus 로고    scopus 로고
    • Clinical significance of heparin-binding epidermal growth factor-like growth factor and a disintegrin and metalloprotease 17 expression in human ovarian cahceir
    • Tanaka Y, Miyamoto S, Suzuki SO, Oki E, Yagi H, Sonoda K, Yamazaki A, Mizushima H, Maehara Y, Mekada E and Nakano H: Clinical significance of heparin-binding epidermal growth factor-like growth factor and a disintegrin and metalloprotease 17 expression in human ovarian cahceir. Clin Cancer Res 11: 4783-4792, 2005.
    • (2005) Clin Cancer Res , vol.11 , pp. 4783-4792
    • Tanaka, Y.1    Miyamoto, S.2    Suzuki, S.O.3    Oki, E.4    Yagi, H.5    Sonoda, K.6    Yamazaki, A.7    Mizushima, H.8    Maehara, Y.9    Mekada, E.10    Nakano, H.11
  • 32
    • 55749092776 scopus 로고    scopus 로고
    • Heparin-binding epidermal growth factor-like growth factor promotes transcoelomic metastasis in ovarian cancer through epithelial-mesenchymal transition
    • Yagi H, Yotsumoto F and Miyamoto S: Heparin-binding epidermal growth factor-like growth factor promotes transcoelomic metastasis in ovarian cancer through epithelial-mesenchymal transition. Mol Cancer Ther 7: 3441-3451, 2008.
    • (2008) Mol Cancer Ther , vol.7 , pp. 3441-3451
    • Yagi, H.1    Yotsumoto, F.2    Miyamoto, S.3
  • 34
    • 60549113956 scopus 로고    scopus 로고
    • Synergistic anti-tumor effect of paclitaxel with CRM197, an inhibitor of HB-EGF, in ovarian cancer
    • Yagi H, Yotsumoto F, Sonoda K, Kuroki M, Mekada E and Miyamoto S: Synergistic anti-tumor effect of paclitaxel with CRM197, an inhibitor of HB-EGF, in ovarian cancer. Int J Cancer 124: 1429-1439, 2009.
    • (2009) Int J Cancer , vol.124 , pp. 1429-1439
    • Yagi, H.1    Yotsumoto, F.2    Sonoda, K.3    Kuroki, M.4    Mekada, E.5    Miyamoto, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.