메뉴 건너뛰기




Volumn 12, Issue 2, 2014, Pages 190-201

Transactivation of EGFR by G protein-coupled receptor in the pathophysiology of intimal hyperplasia

Author keywords

A disintegrin and metalloproteinases; Cell proliferation; Epidermal growth factor receptor; G protein coupled receptor; Intimal hyperplasia; Matrix matalloproteinases; Migration; Transactivation

Indexed keywords

ADAM PROTEIN; ANGIOTENSIN 1 RECEPTOR; ANGIOTENSIN II; CATECHOLAMINE; ENDOTHELIN 1; EPIDERMAL GROWTH FACTOR RECEPTOR; G PROTEIN COUPLED RECEPTOR; HEPARIN BINDING EPIDERMAL GROWTH FACTOR; HISTONE DEACETYLASE INHIBITOR; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE 14; MATRIX METALLOPROTEINASE INHIBITOR; MITOGEN ACTIVATED PROTEIN KINASE; MONOCLONAL ANTIBODY; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; PROTEIN TYROSINE KINASE INHIBITOR; THROMBIN; UROKINASE;

EID: 84900327239     PISSN: 15701611     EISSN: 18756212     Source Type: Journal    
DOI: 10.2174/1570161112666140226123745     Document Type: Article
Times cited : (16)

References (73)
  • 1
    • 0030044360 scopus 로고    scopus 로고
    • Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors
    • [1] Daub H, Weiss FU, Wallasch C, et al. Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors. Nature 1996; 379: 557-60.
    • (1996) Nature , vol.379 , pp. 557-560
    • Daub, H.1    Weiss, F.U.2    Wallasch, C.3
  • 2
    • 1342322686 scopus 로고    scopus 로고
    • Multiple G-protein-coupled receptor signals converge on the epidermal growth factor receptor to promote migration and invasion
    • [2] Schafer B, Gschwind A, Ullrich A. Multiple G-protein-coupled receptor signals converge on the epidermal growth factor receptor to promote migration and invasion. Oncogene 2004; 23: 991-9.
    • (2004) Oncogene , vol.23 , pp. 991-999
    • Schafer, B.1    Gschwind, A.2    Ullrich, A.3
  • 3
    • 84867329297 scopus 로고    scopus 로고
    • EGFR and PKC are involved in the activation of ERK1/2 and p90 RSK and the subsequent proliferation of SNU-407 colon cancer cells by muscarinic acetylcholine receptors
    • [3] Park YS, Cho NJ. EGFR and PKC are involved in the activation of ERK1/2 and p90 RSK and the subsequent proliferation of SNU-407 colon cancer cells by muscarinic acetylcholine receptors. Mol Cell Biochem 2012; 370: 191-8.
    • (2012) Mol Cell Biochem , vol.370 , pp. 191-198
    • Park, Y.S.1    Cho, N.J.2
  • 4
    • 0036127836 scopus 로고    scopus 로고
    • Epidermal growth factor receptor (EGFR) transactivation by estrogen via the G-protein-coupled receptor, GPR30: A novel signaling pathway with potential significance for breast cancer
    • [4] Filardo EJ. Epidermal growth factor receptor (EGFR) transactivation by estrogen via the G-protein-coupled receptor, GPR30: a novel signaling pathway with potential significance for breast cancer. J Steroid Biochem Mol Biol 2002; 80: 231-8.
    • (2002) J Steroid Biochem Mol Biol , vol.80 , pp. 231-238
    • Filardo, E.J.1
  • 5
    • 4143151913 scopus 로고    scopus 로고
    • Heparin-binding EGF-like growth factor is a promising target for ovarian cancer therapy
    • [5] Miyamoto S, Hirata M, Yamazaki A, et al. Heparin-binding EGF-like growth factor is a promising target for ovarian cancer therapy. Cancer Res 2004; 64: 5720-7.
    • (2004) Cancer Res , vol.64 , pp. 5720-5727
    • Miyamoto, S.1    Hirata, M.2    Yamazaki, A.3
  • 6
    • 0033601182 scopus 로고    scopus 로고
    • Intracellular signaling of angiotensin II-induced p70 S6 kinase phosphorylation at Ser(411) in vascular smooth muscle cells. Possible requirement of epidermal growth factor receptor, Ras, extracellular signal-regulated kinase, and Akt
    • [6] Eguchi S, Iwasaki H, Ueno H, et al. Intracellular signaling of angiotensin II-induced p70 S6 kinase phosphorylation at Ser(411) in vascular smooth muscle cells. Possible requirement of epidermal growth factor receptor, Ras, extracellular signal-regulated kinase, and Akt. J Biol Chem 1999; 274: 36843-51.
    • (1999) J Biol Chem , vol.274 , pp. 36843-36851
    • Eguchi, S.1    Iwasaki, H.2    Ueno, H.3
  • 7
    • 8844228835 scopus 로고    scopus 로고
    • Transactivation of epidermal growth factor receptor mediates catecholamine-induced growth of vascular smooth muscle
    • [7] Zhang H, Chalothorn D, Jackson LF, et al. Transactivation of epidermal growth factor receptor mediates catecholamine-induced growth of vascular smooth muscle. Circ Res 2004; 95: 989-97.
    • (2004) Circ Res , vol.95 , pp. 989-997
    • Zhang, H.1    Chalothorn, D.2    Jackson, L.F.3
  • 8
    • 34447503630 scopus 로고    scopus 로고
    • Platelet-activating factor induces ovine fetal pulmonary venous smooth muscle cell proliferation: Role of epidermal growth factor receptor transactivation
    • [8] Zhou W, Ibe BO, Raj JU. Platelet-activating factor induces ovine fetal pulmonary venous smooth muscle cell proliferation: role of epidermal growth factor receptor transactivation. Am J Physiol Heart Circ Physiol 2007; 292: H2773-81.
    • (2007) Am J Physiol Heart Circ Physiol , vol.292
    • Zhou, W.1    Ibe, B.O.2    Raj, J.U.3
  • 9
    • 45149135007 scopus 로고    scopus 로고
    • Heparin binding epidermal growth factor-like growth factor signaling in flow-induced arterial remodeling
    • [9] Zhang H, Sunnarborg SW, McNaughton KK, et al. Heparin binding epidermal growth factor-like growth factor signaling in flow-induced arterial remodeling. Circ Res 2008; 102: 1275-85.
    • (2008) Circ Res , vol.102 , pp. 1275-1285
    • Zhang, H.1    Sunnarborg, S.W.2    McNaughton, K.K.3
  • 10
    • 62749143963 scopus 로고    scopus 로고
    • Thrombin induces nestin expression via the transactivation of EGFR signalings in rat vascular smooth muscle cells
    • [10] Huang YL, Shi GY, Lee H, et al. Thrombin induces nestin expression via the transactivation of EGFR signalings in rat vascular smooth muscle cells. Cell Signal 2009; 21: 954-68.
    • (2009) Cell Signal , vol.21 , pp. 954-968
    • Huang, Y.L.1    Shi, G.Y.2    Lee, H.3
  • 11
    • 33846320461 scopus 로고    scopus 로고
    • Receptor transactivation cascades. Focus on "Effects of alpha1D-adrenergic receptors on shedding of biologically active EGF in freshly isolated lacrimal gland epithelial cells"
    • [11] Snider AC, Meier KE. Receptor transactivation cascades. Focus on "Effects of alpha1D-adrenergic receptors on shedding of biologically active EGF in freshly isolated lacrimal gland epithelial cells". Am J Physiol Cell Physiol 2007; 292: C1-3.
    • (2007) Am J Physiol Cell Physiol , vol.292 , pp. 1-3
    • Snider, A.C.1    Meier, K.E.2
  • 12
    • 78649889063 scopus 로고    scopus 로고
    • EGF receptor activation by GPCRs: An universal pathway reveals different versions
    • [12] Liebmann C. EGF receptor activation by GPCRs: an universal pathway reveals different versions. Mol Cell Endocrinol 2011; 331: 222-31.
    • (2011) Mol Cell Endocrinol , vol.331 , pp. 222-231
    • Liebmann, C.1
  • 13
    • 35848943698 scopus 로고    scopus 로고
    • Mitogenic signaling pathways induced by G protein coupled receptors
    • [13] Rozengurt E. Mitogenic signaling pathways induced by G protein coupled receptors. J Cell Physiol 2007; 213: 589-602.
    • (2007) J Cell Physiol , vol.213 , pp. 589-602
    • Rozengurt, E.1
  • 14
    • 77954870422 scopus 로고    scopus 로고
    • Transactivation of PDGFRbeta by dopamine D4 receptor does not require PDGFRbeta dimerization
    • [14] Chi SS, Vetiska SM, Gill RS, et al. Transactivation of PDGFRbeta by dopamine D4 receptor does not require PDGFRbeta dimerization. Mol Brain 2010; 3: 22.
    • (2010) Mol Brain , vol.3 , pp. 22
    • Chi, S.S.1    Vetiska, S.M.2    Gill, R.S.3
  • 15
    • 0030683639 scopus 로고    scopus 로고
    • Signal characteristics of G protein-transactivated EGF receptor
    • [15] Daub H, Wallasch C, Lankenau A, et al. Signal characteristics of G protein-transactivated EGF receptor. EMBO J 1997; 16: 7032-44.
    • (1997) EMBO J , vol.16 , pp. 7032-7044
    • Daub, H.1    Wallasch, C.2    Lankenau, A.3
  • 16
    • 0034773992 scopus 로고    scopus 로고
    • The EGFR family and its ligands in human cancer. Signalling mechanisms and therapeutic opportunities
    • [16] Yarden Y. The EGFR family and its ligands in human cancer. signalling mechanisms and therapeutic opportunities. Eur J Cancer 2001; 37 (Suppl 4): S3-8.
    • (2001) Eur J Cancer , vol.37 , Issue.4 , pp. 3-8
    • Yarden, Y.1
  • 17
    • 52649160344 scopus 로고    scopus 로고
    • EGFR family: Structure physiology signalling and therapeutic targets
    • [17] Burgess AW. EGFR family: structure physiology signalling and therapeutic targets. Growth Factors 2008; 26: 263-74.
    • (2008) Growth Factors , vol.26 , pp. 263-274
    • Burgess, A.W.1
  • 18
    • 33745234272 scopus 로고    scopus 로고
    • Analysis of G protein betagamma dimer formation in live cells using multicolor bimolecular fluorescence complementation demonstrates preferences of beta1 for particular gamma subunits
    • [18] Mervine SM, Yost EA, Sabo JL, et al. Analysis of G protein betagamma dimer formation in live cells using multicolor bimolecular fluorescence complementation demonstrates preferences of beta1 for particular gamma subunits. Mol Pharmacol 2006; 70: 194-205.
    • (2006) Mol Pharmacol , vol.70 , pp. 194-205
    • Mervine, S.M.1    Yost, E.A.2    Sabo, J.L.3
  • 19
    • 28544452607 scopus 로고    scopus 로고
    • Accessory proteins for G proteins: Partners in signaling
    • [19] Sato M, Blumer JB, Simon V, et al. Accessory proteins for G proteins: partners in signaling. Annu Rev Pharmacol Toxicol 2006; 46: 151-87.
    • (2006) Annu Rev Pharmacol Toxicol , vol.46 , pp. 151-187
    • Sato, M.1    Blumer, J.B.2    Simon, V.3
  • 20
    • 39749097760 scopus 로고    scopus 로고
    • GPR30: A novel therapeutic target in estrogen-related disease
    • [20] Prossnitz ER, Sklar LA, Oprea TI, et al. GPR30: a novel therapeutic target in estrogen-related disease. Trends Pharmacol Sci 2008; 29: 116-23.
    • (2008) Trends Pharmacol Sci , vol.29 , pp. 116-123
    • Prossnitz, E.R.1    Sklar, L.A.2    Oprea, T.I.3
  • 21
    • 0033599039 scopus 로고    scopus 로고
    • EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF
    • [21] Prenzel N, Zwick E, Daub H, et al. EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF. Nature 1999; 402: 884-8.
    • (1999) Nature , vol.402 , pp. 884-888
    • Prenzel, N.1    Zwick, E.2    Daub, H.3
  • 22
    • 0032502765 scopus 로고    scopus 로고
    • Calcium-dependent epidermal growth factor receptor transactivation mediates the angiotensin II-induced mitogen-activated protein kinase activation in vascular smooth muscle cells
    • [22] Eguchi S, Numaguchi K, Iwasaki H, et al. Calcium-dependent epidermal growth factor receptor transactivation mediates the angiotensin II-induced mitogen-activated protein kinase activation in vascular smooth muscle cells. J Biol Chem 1998; 273: 8890-6.
    • (1998) J Biol Chem , vol.273 , pp. 8890-8896
    • Eguchi, S.1    Numaguchi, K.2    Iwasaki, H.3
  • 23
    • 0034724860 scopus 로고    scopus 로고
    • Carbachol-stimulated transactivation of epidermal growth factor receptor and mitogen-activated protein kinase in T(84) cells is mediated by intracellular ca(2+), PYK-2, and p60(src)
    • [23] Keely SJ, Calandrella SO, Barrett KE. Carbachol-stimulated transactivation of epidermal growth factor receptor and mitogen-activated protein kinase in T(84) cells is mediated by intracellular ca(2+), PYK-2, and p60(src). J Biol Chem 2000; 275: 12619-25.
    • (2000) J Biol Chem , vol.275 , pp. 12619-12625
    • Keely, S.J.1    Calandrella, S.O.2    Barrett, K.E.3
  • 24
    • 0035827528 scopus 로고    scopus 로고
    • Src and Pyk2 mediate G-protein-coupled receptor activation of epidermal growth factor receptor (EGFR) but are not required for coupling to the mitogen-activated protein (MAP) kinase signaling cascade
    • [24] Andreev J, Galisteo ML, Kranenburg O, et al. Src and Pyk2 mediate G-protein-coupled receptor activation of epidermal growth factor receptor (EGFR) but are not required for coupling to the mitogen-activated protein (MAP) kinase signaling cascade. J Biol Chem 2001; 276: 20130-5.
    • (2001) J Biol Chem , vol.276 , pp. 20130-20135
    • Reev, J.1    Galisteo, M.L.2    Kranenburg, O.3
  • 25
    • 0030614911 scopus 로고    scopus 로고
    • Gbetagamma subunits mediate Src-dependent phosphorylation of the epidermal growth factor receptor. A scaffold for G protein-coupled receptor-mediated Ras activation
    • [25] Luttrell LM, Della Rocca GJ, van Biesen T, et al. Gbetagamma subunits mediate Src-dependent phosphorylation of the epidermal growth factor receptor. A scaffold for G protein-coupled receptor-mediated Ras activation. J Biol Chem 1997; 272: 4637-44.
    • (1997) J Biol Chem , vol.272 , pp. 4637-4644
    • Luttrell, L.M.1    Della Rocca, G.J.2    Van Biesen, T.3
  • 26
    • 34147192985 scopus 로고    scopus 로고
    • Protein kinase Calpha mediates feedback inhibition of EGF receptor transactivation induced by Gq-coupled receptor agonists
    • [26] Santiskulvong C, Rozengurt E. Protein kinase Calpha mediates feedback inhibition of EGF receptor transactivation induced by Gq-coupled receptor agonists. Cell Signal 2007; 19: 1348-57.
    • (2007) Cell Signal , vol.19 , pp. 1348-1357
    • Santiskulvong, C.1    Rozengurt, E.2
  • 27
    • 0032577953 scopus 로고    scopus 로고
    • Angiotensin II type 1 receptor-induced extracellular signal-regulated protein kinase activation is mediated by Ca2+/calmodulin-dependent transactivation of epidermal growth factor receptor
    • [27] Murasawa S, Mori Y, Nozawa Y, et al. Angiotensin II type 1 receptor-induced extracellular signal-regulated protein kinase activation is mediated by Ca2+/calmodulin-dependent transactivation of epidermal growth factor receptor. Circ Res 1998; 82: 1338-48.
    • (1998) Circ Res , vol.82 , pp. 1338-1348
    • Murasawa, S.1    Mori, Y.2    Nozawa, Y.3
  • 28
    • 33646377415 scopus 로고    scopus 로고
    • Muscarinic M2 receptors mediate transactivation of EGF receptor through Fyn kinase and without matrix metalloproteases
    • [28] Stirnweiss J, Valkova C, Ziesche E, et al. Muscarinic M2 receptors mediate transactivation of EGF receptor through Fyn kinase and without matrix metalloproteases. Cell Signal 2006; 18: 1338-49.
    • (2006) Cell Signal , vol.18 , pp. 1338-1349
    • Stirnweiss, J.1    Valkova, C.2    Ziesche, E.3
  • 29
    • 0036473397 scopus 로고    scopus 로고
    • The role of beta-arrestins in the termination and transduction of G-protein-coupled receptor signals
    • [29] Luttrell LM, Lefkowitz RJ. The role of beta-arrestins in the termination and transduction of G-protein-coupled receptor signals. J Cell Sci 2002; 115: 455-65.
    • (2002) J Cell Sci , vol.115 , pp. 455-465
    • Luttrell, L.M.1    Lefkowitz, R.J.2
  • 30
    • 84867582126 scopus 로고    scopus 로고
    • Urokinase requires NAD(P)H oxidase to transactivate the epidermal growth factor receptor
    • [30] Duru EA, Fu Y, Davies MG. Urokinase requires NAD(P)H oxidase to transactivate the epidermal growth factor receptor. Surgery 2012; 152: 879-85.
    • (2012) Surgery , vol.152 , pp. 879-885
    • Duru, E.A.1    Fu, Y.2    Davies, M.G.3
  • 31
    • 0043172403 scopus 로고    scopus 로고
    • Transactivation joins multiple tracks to the ERK/MAPK cascade
    • [31] Wetzker R, Bohmer FD. Transactivation joins multiple tracks to the ERK/MAPK cascade. Nat Rev Mol Cell Biol 2003; 4: 651-7.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 651-657
    • Wetzker, R.1    Bohmer, F.D.2
  • 32
    • 0038719741 scopus 로고    scopus 로고
    • Characterization of growth factor induced serine phosphorylation of tumor necrosis factor-alpha converting enzyme and of an alternatively translated polypeptide
    • [32] Fan H, Turck CW, Derynck R. Characterization of growth factor induced serine phosphorylation of tumor necrosis factor-alpha converting enzyme and of an alternatively translated polypeptide. J Biol Chem 2003; 278: 18617-27.
    • (2003) J Biol Chem , vol.278 , pp. 18617-18627
    • Fan, H.1    Turck, C.W.2    Derynck, R.3
  • 33
    • 33747422506 scopus 로고    scopus 로고
    • ADAM17 mediates epidermal growth factor receptor transactivation and vascular smooth muscle cell hypertrophy induced by angiotensin II
    • [33] Ohtsu H, Dempsey PJ, Frank GD, et al. ADAM17 mediates epidermal growth factor receptor transactivation and vascular smooth muscle cell hypertrophy induced by angiotensin II. Arterioscler Thromb Vasc Biol 2006; 26: e133-7.
    • (2006) Arterioscler Thromb Vasc Biol , vol.26
    • Ohtsu, H.1    Dempsey, P.J.2    Frank, G.D.3
  • 34
    • 0344443646 scopus 로고    scopus 로고
    • Matrix metalloproteinases 2 and 9 mediate epidermal growth factor receptor transactivation by gonadotropin-releasing hormone
    • [34] Roelle S, Grosse R, Aigner A, et al. Matrix metalloproteinases 2 and 9 mediate epidermal growth factor receptor transactivation by gonadotropin-releasing hormone. J Biol Chem 2003; 278: 47307-18.
    • (2003) J Biol Chem , vol.278 , pp. 47307-47318
    • Roelle, S.1    Grosse, R.2    Aigner, A.3
  • 35
    • 33745714456 scopus 로고    scopus 로고
    • ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors
    • [35] Ohtsu H, Dempsey PJ, Eguchi S. ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors. Am J Physiol Cell Physiol 2006; 291: C1-10.
    • (2006) Am J Physiol Cell Physiol , vol.291 , pp. 01-10
    • Ohtsu, H.1    Dempsey, P.J.2    Eguchi, S.3
  • 36
    • 0037157854 scopus 로고    scopus 로고
    • The metalloprotease Kuzbanian (ADAM10) mediates the transactivation of EGF receptor by G protein-coupled receptors
    • [36] Yan Y, Shirakabe K, Werb Z. The metalloprotease Kuzbanian (ADAM10) mediates the transactivation of EGF receptor by G protein-coupled receptors. J Cell Biol 2002; 158: 221-6.
    • (2002) J Cell Biol , vol.158 , pp. 221-226
    • Yan, Y.1    Shirakabe, K.2    Werb, Z.3
  • 37
    • 23844557144 scopus 로고    scopus 로고
    • Angiotensin II and EGF receptor cross-talk in chronic kidney diseases: A new therapeutic approach
    • [37] Lautrette A, Li S, Alili R, et al. Angiotensin II and EGF receptor cross-talk in chronic kidney diseases: a new therapeutic approach. Nat Med 2005; 11: 867-74.
    • (2005) Nat Med , vol.11 , pp. 867-874
    • Lautrette, A.1    Li, S.2    Alili, R.3
  • 38
    • 0036152858 scopus 로고    scopus 로고
    • Cardiac hypertrophy is inhibited by antagonism of ADAM12 processing of HB-EGF: Metalloproteinase inhibitors as a new therapy
    • [38] Asakura M, Kitakaze M, Takashima S, et al. Cardiac hypertrophy is inhibited by antagonism of ADAM12 processing of HB-EGF: metalloproteinase inhibitors as a new therapy. Nat Med 2002; 8: 35-40.
    • (2002) Nat Med , vol.8 , pp. 35-40
    • Asakura, M.1    Kitakaze, M.2    Takashima, S.3
  • 39
    • 10044256495 scopus 로고    scopus 로고
    • Involvement of metalloproteinases 2/9 in epidermal growth factor receptor transactivation in pressure-induced myogenic tone in mouse mesenteric resistance arteries
    • [39] Lucchesi PA, Sabri A, Belmadani S, et al. Involvement of metalloproteinases 2/9 in epidermal growth factor receptor transactivation in pressure-induced myogenic tone in mouse mesenteric resistance arteries. Circulation 2004; 110: 3587-93.
    • (2004) Circulation , vol.110 , pp. 3587-3593
    • Lucchesi, P.A.1    Sabri, A.2    Belmadani, S.3
  • 40
    • 0034698062 scopus 로고    scopus 로고
    • Heparin blockade of thrombin-induced smooth muscle cell migration involves inhibition of epidermal growth factor (EGF) receptor transactivation by heparin-binding EGF-like growth factor
    • [40] Kalmes A, Vesti BR, Daum G, et al. Heparin blockade of thrombin-induced smooth muscle cell migration involves inhibition of epidermal growth factor (EGF) receptor transactivation by heparin-binding EGF-like growth factor. Circ Res 2000; 87: 92-8.
    • (2000) Circ Res , vol.87 , pp. 92-98
    • Kalmes, A.1    Vesti, B.R.2    Daum, G.3
  • 41
    • 65249111522 scopus 로고    scopus 로고
    • Cell migration in response to the amino-terminal fragment of urokinase requires epidermal growth factor receptor activation through an ADAM-mediated mechanism
    • [41] Bakken AM, Protack CD, Roztocil E, et al. Cell migration in response to the amino-terminal fragment of urokinase requires epidermal growth factor receptor activation through an ADAM-mediated mechanism. J Vasc Surg 2009; 49: 1296-303.
    • (2009) J Vasc Surg , vol.49 , pp. 1296-1303
    • Bakken, A.M.1    Protack, C.D.2    Roztocil, E.3
  • 42
    • 33645214092 scopus 로고    scopus 로고
    • Angiotensin II promotes smooth muscle cell proliferation and migration through release of heparin-binding epidermal growth factor and activation of EGF-receptor pathway
    • [42] Yang X, Zhu MJ, Sreejayan N, et al. Angiotensin II promotes smooth muscle cell proliferation and migration through release of heparin-binding epidermal growth factor and activation of EGF-receptor pathway. Mol Cells 2005; 20: 263-70.
    • (2005) Mol Cells , vol.20 , pp. 263-270
    • Yang, X.1    Zhu, M.J.2    Sreejayan, N.3
  • 43
    • 79953202174 scopus 로고    scopus 로고
    • A disintegrin and metalloprotease 17 mediates neointimal hyperplasia in vasculature
    • [43] Takaguri A, Kimura K, Hinoki A, et al. A disintegrin and metalloprotease 17 mediates neointimal hyperplasia in vasculature. Hypertension 2011; 57: 841-5.
    • (2011) Hypertension , vol.57 , pp. 841-845
    • Takaguri, A.1    Kimura, K.2    Hinoki, A.3
  • 44
    • 48049101191 scopus 로고    scopus 로고
    • Beta-arrestins regulate atherosclerosis and neointimal hyperplasia by controlling smooth muscle cell proliferation and migration
    • [44] Kim J, Zhang L, Peppel K, et al. Beta-arrestins regulate atherosclerosis and neointimal hyperplasia by controlling smooth muscle cell proliferation and migration. Circ Res 2008; 103: 70-9.
    • (2008) Circ Res , vol.103 , pp. 70-79
    • Kim, J.1    Zhang, L.2    Peppel, K.3
  • 45
    • 66449134043 scopus 로고    scopus 로고
    • Independent beta-arrestin2 and Gq/protein kinase Czeta pathways for ERK stimulated by angiotensin type 1A receptors in vascular smooth muscle cells converge on transactivation of the epidermal growth factor receptor
    • [45] Kim J, Ahn S, Rajagopal K, et al. Independent beta-arrestin2 and Gq/protein kinase Czeta pathways for ERK stimulated by angiotensin type 1A receptors in vascular smooth muscle cells converge on transactivation of the epidermal growth factor receptor. J Biol Chem 2009; 284: 11953-62.
    • (2009) J Biol Chem , vol.284 , pp. 11953-11962
    • Kim, J.1    Ahn, S.2    Rajagopal, K.3
  • 46
    • 49149104318 scopus 로고    scopus 로고
    • PKC-delta/c-Src-mediated EGF receptor transactivation regulates thrombin-induced COX-2 expression and PGE(2) production in rat vascular smooth muscle cells
    • [46] Hsieh HL, Sun CC, Wang TS, et al. PKC-delta/c-Src-mediated EGF receptor transactivation regulates thrombin-induced COX-2 expression and PGE(2) production in rat vascular smooth muscle cells. Biochim Biophys Acta 2008; 1783: 1563-75.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 1563-1575
    • Hsieh, H.L.1    Sun, C.C.2    Wang, T.S.3
  • 47
    • 55549135364 scopus 로고    scopus 로고
    • The transactivated epidermal growth factor receptor recruits Pyk2 to regulate Src kinase activity
    • [47] Schauwienold D, Sastre AP, Genzel N, et al. The transactivated epidermal growth factor receptor recruits Pyk2 to regulate Src kinase activity. J Biol Chem 2008; 283: 27748-56.
    • (2008) J Biol Chem , vol.283 , pp. 27748-27756
    • Schauwienold, D.1    Sastre, A.P.2    Genzel, N.3
  • 48
    • 33845588970 scopus 로고    scopus 로고
    • Heparin binding EGF is necessary for vasospastic response to endothelin
    • [48] Chansel D, Ciroldi M, Vandermeersch S, et al. Heparin binding EGF is necessary for vasospastic response to endothelin. FASEB J 2006; 20: 1936-8.
    • (2006) FASEB J , vol.20 , pp. 1936-1938
    • Chansel, D.1    Ciroldi, M.2    Vandermeersch, S.3
  • 49
    • 0142089835 scopus 로고    scopus 로고
    • Galardin (GM 6001), a broad-spectrum matrix metalloproteinase inhibitor, blocks bombesin-and LPA-induced EGF receptor transactivation and DNA synthesis in rat-1 cells
    • [49] Santiskulvong C, Rozengurt E. Galardin (GM 6001), a broad-spectrum matrix metalloproteinase inhibitor, blocks bombesin-and LPA-induced EGF receptor transactivation and DNA synthesis in rat-1 cells. Exp Cell Res 2003; 290: 437-46.
    • (2003) Exp Cell Res , vol.290 , pp. 437-446
    • Santiskulvong, C.1    Rozengurt, E.2
  • 50
    • 0035371620 scopus 로고    scopus 로고
    • Regulation of receptor tyrosine kinase signaling by protein tyrosine phosphatases
    • [50] Ostman A, Bohmer FD. Regulation of receptor tyrosine kinase signaling by protein tyrosine phosphatases. Trends Cell Biol 2001; 11: 258-66.
    • (2001) Trends Cell Biol , vol.11 , pp. 258-266
    • Ostman, A.1    Bohmer, F.D.2
  • 52
    • 0038449116 scopus 로고    scopus 로고
    • EGF receptor as a therapeutic target
    • [52] Levitzki A. EGF receptor as a therapeutic target. Lung Cancer 2003; 41 (Suppl 1): S9-14.
    • (2003) Lung Cancer , vol.41 , pp. 09-14
    • Levitzki, A.1
  • 53
    • 0034988184 scopus 로고    scopus 로고
    • The epidermal growth factor receptor as a target for cancer therapy
    • [53] Mendelsohn J. The epidermal growth factor receptor as a target for cancer therapy. Endocr Relat Cancer 2001; 8: 3-9.
    • (2001) Endocr Relat Cancer , vol.8 , pp. 3-9
    • Mendelsohn, J.1
  • 54
    • 0035117355 scopus 로고    scopus 로고
    • Development of ABX-EGF, a fully human anti-EGF receptor monoclonal antibody, for cancer therapy
    • [54] Yang XD, Jia XC, Corvalan JR, et al. Development of ABX-EGF, a fully human anti-EGF receptor monoclonal antibody, for cancer therapy. Crit Rev Oncol Hematol 2001; 38: 17-23.
    • (2001) Crit Rev Oncol Hematol , vol.38 , pp. 17-23
    • Yang, X.D.1    Jia, X.C.2    Corvalan, J.R.3
  • 55
    • 0036118248 scopus 로고    scopus 로고
    • Therapeutic potential of ABX-EGF: A fully human anti-epidermal growth factor receptor monoclonal antibody for cancer treatment
    • [55] Lynch DH, Yang XD. Therapeutic potential of ABX-EGF: a fully human anti-epidermal growth factor receptor monoclonal antibody for cancer treatment. Semin Oncol 2002; 29: 47-50.
    • (2002) Semin Oncol , vol.29 , pp. 47-50
    • Lynch, D.H.1    Yang, X.D.2
  • 56
    • 34347395733 scopus 로고    scopus 로고
    • Trastuzumab--mechanism of action and use in clinical practice
    • [56] Hudis CA. Trastuzumab--mechanism of action and use in clinical practice. N Engl J Med 2007; 357: 39-51.
    • (2007) N Engl J Med , vol.357 , pp. 39-51
    • Hudis, C.A.1
  • 57
    • 79956101962 scopus 로고    scopus 로고
    • The dual EGFR/HER2 inhibitor lapatinib synergistically enhances the antitumor activity of the histone deacetylase inhibitor panobinostat in colorectal cancer models
    • [57] LaBonte MJ, Wilson PM, Fazzone W, et al. The dual EGFR/HER2 inhibitor lapatinib synergistically enhances the antitumor activity of the histone deacetylase inhibitor panobinostat in colorectal cancer models. Cancer Res 2011; 71: 3635-48.
    • (2011) Cancer Res , vol.71 , pp. 3635-3648
    • Labonte, M.J.1    Wilson, P.M.2    Fazzone, W.3
  • 58
    • 0036198508 scopus 로고    scopus 로고
    • ZD1839 (Iressa): Preclinical studies and pharmacology
    • [58] Ciardiello F, Tortora G, De Placido S, et al. ZD1839 (Iressa): preclinical studies and pharmacology. Tumori 2002; 88: S155-7.
    • (2002) Tumori , vol.88
    • Ciardiello, F.1    Tortora, G.2    De Placido, S.3
  • 59
    • 84886943115 scopus 로고    scopus 로고
    • Lapatinib for the treatment of HER2-overexpressing breast cancer
    • [59] Jones J, Takeda A, Picot J, et al. Lapatinib for the treatment of HER2-overexpressing breast cancer. Health Technol Assess 2009; 13 Suppl 3: 1-6.
    • (2009) Health Technol Assess , vol.13 , Issue.3 , pp. 1-6
    • Jones, J.1    Takeda, A.2    Picot, J.3
  • 60
    • 84855293765 scopus 로고    scopus 로고
    • Irreversible EGFR inhibitor EKB-569 targets low-LET gamma-radiation-triggered rel orchestration and potentiates cell death in squamous cell carcinoma
    • [60] Aravindan N, Thomas CR, Jr., Aravindan S, et al. Irreversible EGFR inhibitor EKB-569 targets low-LET gamma-radiation-triggered rel orchestration and potentiates cell death in squamous cell carcinoma. PLoS One 2011; 6: e29705.
    • (2011) Plos One , vol.6
    • Aravindan, N.1    Thomas, C.R.2    Aravindan, S.3
  • 61
    • 33748048505 scopus 로고    scopus 로고
    • Increased bioavailability of intravenous versus oral CI-1033, a pan erbB tyrosine kinase inhibitor: Results of a phase I pharmacokinetic study
    • [61] Simon GR, Garrett CR, Olson SC, et al. Increased bioavailability of intravenous versus oral CI-1033, a pan erbB tyrosine kinase inhibitor: results of a phase I pharmacokinetic study. Clin Cancer Res 2006; 12: 4645-51.
    • (2006) Clin Cancer Res , vol.12 , pp. 4645-4651
    • Simon, G.R.1    Garrett, C.R.2    Olson, S.C.3
  • 62
    • 3843096112 scopus 로고    scopus 로고
    • Inhibition of the tumor necrosis factor-alpha-converting enzyme by its pro domain
    • [62] Gonzales PE, Solomon A, Miller AB, et al. Inhibition of the tumor necrosis factor-alpha-converting enzyme by its pro domain. J Biol Chem 2004; 279: 31638-45.
    • (2004) J Biol Chem , vol.279 , pp. 31638-31645
    • Gonzales, P.E.1    Solomon, A.2    Miller, A.B.3
  • 63
    • 37249079599 scopus 로고    scopus 로고
    • The ADAM10 prodomain is a specific inhibitor of ADAM10 proteolytic activity and inhibits cellular shedding events
    • [63] Moss ML, Bomar M, Liu Q, et al. The ADAM10 prodomain is a specific inhibitor of ADAM10 proteolytic activity and inhibits cellular shedding events. J Biol Chem 2007; 282: 35712-21.
    • (2007) J Biol Chem , vol.282 , pp. 35712-35721
    • Moss, M.L.1    Bomar, M.2    Liu, Q.3
  • 64
    • 77955505776 scopus 로고    scopus 로고
    • Selective inhibition of ADAM12 catalytic activity through engineering of tissue inhibitor of metalloproteinase 2 (TIMP-2)
    • [64] Kveiborg M, Jacobsen J, Lee MH, et al. Selective inhibition of ADAM12 catalytic activity through engineering of tissue inhibitor of metalloproteinase 2 (TIMP-2). Biochem J 2010; 430: 79-86.
    • (2010) Biochem J , vol.430 , pp. 79-86
    • Kveiborg, M.1    Jacobsen, J.2    Lee, M.H.3
  • 65
    • 42449131043 scopus 로고    scopus 로고
    • The isolated N-terminal domains of TIMP-1 and TIMP-3 are insufficient for ADAM10 inhibition
    • [65] Rapti M, Atkinson SJ, Lee MH, et al. The isolated N-terminal domains of TIMP-1 and TIMP-3 are insufficient for ADAM10 inhibition. Biochem J 2008; 411: 433-9.
    • (2008) Biochem J , vol.411 , pp. 433-439
    • Rapti, M.1    Atkinson, S.J.2    Lee, M.H.3
  • 66
    • 11244269560 scopus 로고    scopus 로고
    • Increased expression of ADAM family members in human breast cancer and breast cancer cell lines
    • [66] Lendeckel U, Kohl J, Arndt M, et al. Increased expression of ADAM family members in human breast cancer and breast cancer cell lines. J Cancer Res Clin Oncol 2005; 131: 41-8.
    • (2005) J Cancer Res Clin Oncol , vol.131 , pp. 41-48
    • Lendeckel, U.1    Kohl, J.2    Arndt, M.3
  • 67
    • 84860641102 scopus 로고    scopus 로고
    • The ADAMs family of proteases: New biomarkers and therapeutic targets for cancer?
    • [67] Duffy MJ, Mullooly M, O'Donovan N, et al. The ADAMs family of proteases: new biomarkers and therapeutic targets for cancer? Clin Proteomics 2011; 8: 9.
    • (2011) Clin Proteomics , vol.8 , pp. 9
    • Duffy, M.J.1    Mullooly, M.2    O'donovan, N.3
  • 68
    • 0030064282 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinase activity inhibits smooth muscle cell migration but not neointimal thickening after arterial injury
    • [68] Bendeck MP, Irvin C, Reidy MA. Inhibition of matrix metalloproteinase activity inhibits smooth muscle cell migration but not neointimal thickening after arterial injury. Circ Res 1996; 78: 38-43.
    • (1996) Circ Res , vol.78 , pp. 38-43
    • Bendeck, M.P.1    Irvin, C.2    Reidy, M.A.3
  • 69
    • 0033044209 scopus 로고    scopus 로고
    • The metalloproteinase inhibitor batimastat (BB-94) causes cell cycle phase perturbations in ovarian cancer cells
    • [69] Erba E, Ronzoni S, Bassano L, et al. The metalloproteinase inhibitor batimastat (BB-94) causes cell cycle phase perturbations in ovarian cancer cells. Ann Oncol 1999; 10: 589-91.
    • (1999) Ann Oncol , vol.10 , pp. 589-591
    • Erba, E.1    Ronzoni, S.2    Bassano, L.3
  • 70
    • 0018260334 scopus 로고
    • Antihypertensive effect of the oral angiotensin converting-enzyme inhibitor SQ 14225 in man
    • [70] Gavras H, Brunner HR, Turini GA, et al. Antihypertensive effect of the oral angiotensin converting-enzyme inhibitor SQ 14225 in man. N Engl J Med 1978; 298: 991-5.
    • (1978) N Engl J Med , vol.298 , pp. 991-995
    • Gavras, H.1    Brunner, H.R.2    Turini, G.A.3
  • 71
    • 0035936402 scopus 로고    scopus 로고
    • Blood-pressure reduction and cardiovascular risk in HOPE study
    • [71] Sleight P, Yusuf S, Pogue J, et al. Blood-pressure reduction and cardiovascular risk in HOPE study. Lancet 2001; 358: 2130-1.
    • (2001) Lancet , vol.358 , pp. 2130-2131
    • Sleight, P.1    Yusuf, S.2    Pogue, J.3
  • 72
    • 20344396863 scopus 로고    scopus 로고
    • Prevention of atrial fibrillation with angiotensin-converting enzyme inhibitors and angiotensin receptor blockers: A meta-analysis
    • [72] Healey JS, Baranchuk A, Crystal E, et al. Prevention of atrial fibrillation with angiotensin-converting enzyme inhibitors and angiotensin receptor blockers: a meta-analysis. J Am Coll Cardiol 2005; 45: 1832-9.
    • (2005) J am Coll Cardiol , vol.45 , pp. 1832-1839
    • Healey, J.S.1    Baranchuk, A.2    Crystal, E.3
  • 73
    • 49749083154 scopus 로고    scopus 로고
    • Effect of angiotensin receptor blockers on cardiovascular events in patients undergoing hemodialysis: An open-label randomized controlled trial
    • [73] Suzuki H, Kanno Y, Sugahara S, et al. Effect of angiotensin receptor blockers on cardiovascular events in patients undergoing hemodialysis: an open-label randomized controlled trial. Am J Kidney Dis 2008; 52: 501-6.
    • (2008) Am J Kidney Dis , vol.52 , pp. 501-506
    • Suzuki, H.1    Kanno, Y.2    Sugahara, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.