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Volumn 50, Issue 1, 2009, Pages 132-139

ERK1/2 mediate wounding- and G-protein-coupled receptor ligands - Induced EGFR activation via regulating ADAM17 and HB-EGF shedding

Author keywords

[No Author keywords available]

Indexed keywords

1,4 DIAMINO 1,4 BIS(2 AMINOPHENYLTHIO) 2,3 DICYANOBUTADIENE; 2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; ADAM 10 INHIBITOR; ADAM 17 INHIBITOR; ADENOSINE TRIPHOSPHATE; ALKALINE PHOSPHATASE; CALCIUM; EPIDERMAL GROWTH FACTOR RECEPTOR; G PROTEIN COUPLED RECEPTOR; HEPARIN BINDING EPIDERMAL GROWTH FACTOR; LYSOPHOSPHATIDIC ACID; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PHOSPHOSERINE; PHOSPHOTYROSINE; PROTEIN INHIBITOR; PROTEIN KINASE B; PROTEIN KINASE C; PROTEIN TYROSINE KINASE; SERINE; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME; UNCLASSIFIED DRUG; ADAM PROTEIN; ADENOSINE 5' O (3 THIOTRIPHOSPHATE); ADENOSINE 5'-O-(3-THIOTRIPHOSPHATE); DRUG DERIVATIVE; EGFR PROTEIN, HUMAN; ENZYME INHIBITOR; HEPARIN-BINDING EGF-LIKE GROWTH FACTOR; LIGAND; LYSOPHOSPHOLIPID; SIGNAL PEPTIDE; TUMOR NECROSIS FACTOR-ALPHA CONVERTASE;

EID: 58249092162     PISSN: 01460404     EISSN: 15525783     Source Type: Journal    
DOI: 10.1167/iovs.08-2246     Document Type: Article
Times cited : (55)

References (65)
  • 1
    • 0030934532 scopus 로고    scopus 로고
    • Wound healing: Aiming for perfect skin regeneration
    • Martin P. Wound healing: aiming for perfect skin regeneration. Science. 1997;276:75-81.
    • (1997) Science , vol.276 , pp. 75-81
    • Martin, P.1
  • 2
    • 0038676258 scopus 로고    scopus 로고
    • Regulation of wound healing by growth factors and cytokines
    • Werner S, Grose R. Regulation of wound healing by growth factors and cytokines. Physiol Rev. 2003;83:835-870.
    • (2003) Physiol Rev , vol.83 , pp. 835-870
    • Werner, S.1    Grose, R.2
  • 3
    • 1542637090 scopus 로고    scopus 로고
    • Wound-induced HB-EGF ectodomain shedding and EGFR activation in corneal epithelial cells
    • Xu KP, Ding Y, Ling J, Dong Z, Yu FS. Wound-induced HB-EGF ectodomain shedding and EGFR activation in corneal epithelial cells. Invest Ophthalmol Vis Sci. 2004;45:813-820.
    • (2004) Invest Ophthalmol Vis Sci , vol.45 , pp. 813-820
    • Xu, K.P.1    Ding, Y.2    Ling, J.3    Dong, Z.4    Yu, F.S.5
  • 5
    • 2642587326 scopus 로고    scopus 로고
    • Wounding induces motility in sheets of corneal epithelial cells through loss of spatial constraints: Role of heparin-binding epidermal growth factor-like growth factor signaling
    • Block ER, Matela AR, SundarRaj N, Iszkula ER, Klarlund JK. Wounding induces motility in sheets of corneal epithelial cells through loss of spatial constraints: role of heparin-binding epidermal growth factor-like growth factor signaling. J Biol Chem. 2004;279: 24307-24312.
    • (2004) J Biol Chem , vol.279 , pp. 24307-24312
    • Block, E.R.1    Matela, A.R.2    SundarRaj, N.3    Iszkula, E.R.4    Klarlund, J.K.5
  • 6
    • 33646687770 scopus 로고    scopus 로고
    • Epithelial cell motility is triggered by activation of the EGF receptor through phosphatidic acid signaling
    • Mazie AR, Spix JK, Block ER, Achebe HB, Klarlund JK. Epithelial cell motility is triggered by activation of the EGF receptor through phosphatidic acid signaling. J Cell Sci. 2006;119:1645-1654.
    • (2006) J Cell Sci , vol.119 , pp. 1645-1654
    • Mazie, A.R.1    Spix, J.K.2    Block, E.R.3    Achebe, H.B.4    Klarlund, J.K.5
  • 7
    • 0028028035 scopus 로고
    • Biosynthesis and processing by phorbol ester of the cells surface-associated precursor form of heparin-binding EGF-like growth factor
    • Raab G, Higashiyama S, Hetelekidis S, et al. Biosynthesis and processing by phorbol ester of the cells surface-associated precursor form of heparin-binding EGF-like growth factor. Biochem Biophys Res Commun. 1994;204:592-597.
    • (1994) Biochem Biophys Res Commun , vol.204 , pp. 592-597
    • Raab, G.1    Higashiyama, S.2    Hetelekidis, S.3
  • 8
    • 0029118420 scopus 로고
    • Phorbol ester induces the rapid processing of cell surface heparin-binding EGF-like growth factor: Conversion from juxtacrine to paracrine growth factor activity
    • Goishi K, Higashiyama S, Klagsbrun M, et al. Phorbol ester induces the rapid processing of cell surface heparin-binding EGF-like growth factor: conversion from juxtacrine to paracrine growth factor activity. Mol Biol Cell. 1995;6:967-980.
    • (1995) Mol Biol Cell , vol.6 , pp. 967-980
    • Goishi, K.1    Higashiyama, S.2    Klagsbrun, M.3
  • 9
    • 0033213984 scopus 로고    scopus 로고
    • The shedding of membrane-anchored heparin-binding epidermal-like growth factor is regulated by the Raf/mitogen-activated protein kinase cascade and by cell adhesion and spreading
    • Gechtman Z, Alonso JL, Raab G, Ingber DE, Klagsbrun M. The shedding of membrane-anchored heparin-binding epidermal-like growth factor is regulated by the Raf/mitogen-activated protein kinase cascade and by cell adhesion and spreading. J Biol Chem. 1999;274:28828-28835.
    • (1999) J Biol Chem , vol.274 , pp. 28828-28835
    • Gechtman, Z.1    Alonso, J.L.2    Raab, G.3    Ingber, D.E.4    Klagsbrun, M.5
  • 10
    • 0032741143 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: Modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding
    • Schlondorff J, Blobel CP. Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding. J Cell Sci. 1999;112:3603-3617.
    • (1999) J Cell Sci , vol.112 , pp. 3603-3617
    • Schlondorff, J.1    Blobel, C.P.2
  • 11
    • 0036185667 scopus 로고    scopus 로고
    • Functional and biochemical characterization of ADAMs and their predicted role in protein ectodomain shedding
    • Blobel CP. Functional and biochemical characterization of ADAMs and their predicted role in protein ectodomain shedding. Inflamm Res. 2002;51:83-84.
    • (2002) Inflamm Res , vol.51 , pp. 83-84
    • Blobel, C.P.1
  • 12
    • 22744450061 scopus 로고    scopus 로고
    • ADAM-mediated ectodomain shedding of HB-EGF in receptor cross-talk
    • Higashiyama S, Nanba D. ADAM-mediated ectodomain shedding of HB-EGF in receptor cross-talk. Biochim Biophys Acta. 2005;1751: 110-117.
    • (2005) Biochim Biophys Acta , vol.1751 , pp. 110-117
    • Higashiyama, S.1    Nanba, D.2
  • 13
    • 11244261160 scopus 로고    scopus 로고
    • Blobel CP. ADAMs: key components in EGFR signalling and development. Nat Rev Mol Cell Biol. 2005;6:32- 43.
    • Blobel CP. ADAMs: key components in EGFR signalling and development. Nat Rev Mol Cell Biol. 2005;6:32- 43.
  • 14
    • 1442358746 scopus 로고    scopus 로고
    • Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands
    • Sahin U, Weskamp G, Kelly K, et al. Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands. J Cell Biol. 2004;164:769-779.
    • (2004) J Cell Biol , vol.164 , pp. 769-779
    • Sahin, U.1    Weskamp, G.2    Kelly, K.3
  • 15
    • 0038806501 scopus 로고    scopus 로고
    • TACE/ADAM17 processing of EGFR ligands indicates a role as a physiological convertase
    • Lee DC, Sunnarborg SW, Hinkle CL, et al. TACE/ADAM17 processing of EGFR ligands indicates a role as a physiological convertase. Ann N Y Acad Sci. 2003;995:22-38.
    • (2003) Ann N Y Acad Sci , vol.995 , pp. 22-38
    • Lee, D.C.1    Sunnarborg, S.W.2    Hinkle, C.L.3
  • 16
    • 33745714456 scopus 로고    scopus 로고
    • ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors
    • 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-C10.
    • (2006) Am J Physiol Cell Physiol , vol.291
    • Ohtsu, H.1    Dempsey, P.J.2    Eguchi, S.3
  • 17
    • 17444373968 scopus 로고    scopus 로고
    • A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPAinduced ectodomain shedding of membrane-anchored heparinbinding EGF-like growth factor
    • Izumi Y, Hirata M, Hasuwa H, et al. A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPAinduced ectodomain shedding of membrane-anchored heparinbinding EGF-like growth factor. EMBO J. 1998;17:7260-7272.
    • (1998) EMBO J , vol.17 , pp. 7260-7272
    • Izumi, Y.1    Hirata, M.2    Hasuwa, H.3
  • 18
    • 0037157854 scopus 로고    scopus 로고
    • The metalloprotease Kuzbanian (ADAM10) mediates the transactivation of EGF receptor by G protein-coupled receptors
    • 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;158:221-226.
    • (2002) J Cell Biol , vol.158 , pp. 221-226
    • Yan, Y.1    Shirakabe, K.2    Werb, Z.3
  • 19
    • 0036152858 scopus 로고    scopus 로고
    • Cardiac hypertrophy is inhibited by antagonism of ADAM12 processing of HB-EGF: Metalloproteinase inhibitors as a new therapy
    • 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
  • 20
    • 0037066757 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha converting enzyme (TACE) regulates epidermal growth factor receptor ligand availability
    • Sunnarborg SW, Hinkle CL, Stevenson M, et al. Tumor necrosis factor-alpha converting enzyme (TACE) regulates epidermal growth factor receptor ligand availability. J Biol Chem. 2002; 277(15):12838-12845.
    • (2002) J Biol Chem , vol.277 , Issue.15 , pp. 12838-12845
    • Sunnarborg, S.W.1    Hinkle, C.L.2    Stevenson, M.3
  • 22
    • 0034769703 scopus 로고    scopus 로고
    • HGF- and KGF-induced activation of PI-3K/p70 s6 kinase pathway in corneal epithelial cells: Its relevance in wound healing
    • Chandrasekher G, Kakazu AH, Bazan HE. HGF- and KGF-induced activation of PI-3K/p70 s6 kinase pathway in corneal epithelial cells: its relevance in wound healing. Exp Eye Res. 2001;73:191-202.
    • (2001) Exp Eye Res , vol.73 , pp. 191-202
    • Chandrasekher, G.1    Kakazu, A.H.2    Bazan, H.E.3
  • 23
    • 0032936995 scopus 로고    scopus 로고
    • Corneal epithelial wound healing increases the expression but not long lasting activation of the p85alpha subunit of phosphatidylinositol-3 kinase
    • Chandrasekher G, Bazan HE. Corneal epithelial wound healing increases the expression but not long lasting activation of the p85alpha subunit of phosphatidylinositol-3 kinase. Curr Eye Res. 1999;18:168-176.
    • (1999) Curr Eye Res , vol.18 , pp. 168-176
    • Chandrasekher, G.1    Bazan, H.E.2
  • 24
    • 0030926967 scopus 로고    scopus 로고
    • Epidermal growth factor stimulation of phosphatidylinositol 3-kinase during wound closure in rabbit corneal epithelial cells
    • Zhang Y, Akhtar RA. Epidermal growth factor stimulation of phosphatidylinositol 3-kinase during wound closure in rabbit corneal epithelial cells. Invest Ophthalmol Vis Sci. 1997;38:1139-1148.
    • (1997) Invest Ophthalmol Vis Sci , vol.38 , pp. 1139-1148
    • Zhang, Y.1    Akhtar, R.A.2
  • 25
    • 0030249058 scopus 로고    scopus 로고
    • Effect of epidermal growth factor on phosphatidylinositol 3-kinase activity in rabbit corneal epithelial cells
    • Zhang Y, Akhtar RA. Effect of epidermal growth factor on phosphatidylinositol 3-kinase activity in rabbit corneal epithelial cells. Exp Eye Res. 1996;63:265-275.
    • (1996) Exp Eye Res , vol.63 , pp. 265-275
    • Zhang, Y.1    Akhtar, R.A.2
  • 26
    • 0034723310 scopus 로고    scopus 로고
    • Epidermal growth factor receptor activation of calpain is required for fibroblast motility and occurs via an ERK/MAP kinase signaling pathway
    • Glading A, Chang P, Lauffenburger D, Wells A. Epidermal growth factor receptor activation of calpain is required for fibroblast motility and occurs via an ERK/MAP kinase signaling pathway. J Biol Chem. 2000;275:2390-2398.
    • (2000) J Biol Chem , vol.275 , pp. 2390-2398
    • Glading, A.1    Chang, P.2    Lauffenburger, D.3    Wells, A.4
  • 28
    • 33847700488 scopus 로고    scopus 로고
    • Lysophosphatidic acid promoting corneal epithelial wound healing by transactivation of epidermal growth factor receptor
    • Xu KP, Yin J, Yu FS. Lysophosphatidic acid promoting corneal epithelial wound healing by transactivation of epidermal growth factor receptor. Invest Ophthalmol Vis Sci. 2007;48:636-643.
    • (2007) Invest Ophthalmol Vis Sci , vol.48 , pp. 636-643
    • Xu, K.P.1    Yin, J.2    Yu, F.S.3
  • 29
    • 34047114821 scopus 로고    scopus 로고
    • Wound-induced ATP release and EGF receptor activation in epithelial cells
    • Yin J, Xu K, Zhang J, Kumar A, Yu FS. Wound-induced ATP release and EGF receptor activation in epithelial cells. J Cell Sci. 2007;120: 815-825.
    • (2007) J Cell Sci , vol.120 , pp. 815-825
    • Yin, J.1    Xu, K.2    Zhang, J.3    Kumar, A.4    Yu, F.S.5
  • 30
    • 0028587054 scopus 로고
    • Growth factor-like effects of lysophosphatidic acid, a novel lipid mediator
    • Jalink K, Hordijk PL, Moolenaar WH. Growth factor-like effects of lysophosphatidic acid, a novel lipid mediator. Biochim Biophys Acta. 1994;1198:185-196.
    • (1994) Biochim Biophys Acta , vol.1198 , pp. 185-196
    • Jalink, K.1    Hordijk, P.L.2    Moolenaar, W.H.3
  • 31
    • 0035025354 scopus 로고    scopus 로고
    • Physiological responses to lysophosphatidic acid and related glycero-phospholipids
    • Tigyi G. Physiological responses to lysophosphatidic acid and related glycero-phospholipids. Prostaglandins. 2001;64:47-62.
    • (2001) Prostaglandins , vol.64 , pp. 47-62
    • Tigyi, G.1
  • 32
    • 0035287474 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors and ATP signalling at synapses
    • Khakh BS. Molecular physiology of P2X receptors and ATP signalling at synapses. Nat Rev Neurosci. 2001;2:165-174.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 165-174
    • Khakh, B.S.1
  • 33
    • 0032478615 scopus 로고    scopus 로고
    • Characterization of a novel subtype of human G protein-coupled receptor for lysophosphatidic acid
    • An S, Bleu T, Hallmark OG, Goetzl EJ. Characterization of a novel subtype of human G protein-coupled receptor for lysophosphatidic acid. J Biol Chem. 1998;273:7906-7910.
    • (1998) J Biol Chem , vol.273 , pp. 7906-7910
    • An, S.1    Bleu, T.2    Hallmark, O.G.3    Goetzl, E.J.4
  • 34
    • 0033600761 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel human G-protein-coupled receptor, EDG7, for lysophosphatidic acid
    • Bandoh K, Aoki J, Hosono H, et al. Molecular cloning and characterization of a novel human G-protein-coupled receptor, EDG7, for lysophosphatidic acid. J Biol Chem. 1999;274:27776-27785.
    • (1999) J Biol Chem , vol.274 , pp. 27776-27785
    • Bandoh, K.1    Aoki, J.2    Hosono, H.3
  • 35
    • 0043011159 scopus 로고    scopus 로고
    • Extracellular ATP as a signaling molecule for epithelial cells
    • Schwiebert EM, Zsembery A. Extracellular ATP as a signaling molecule for epithelial cells. Biochim Biophys Acta. 2003;1615:7-32.
    • (2003) Biochim Biophys Acta , vol.1615 , pp. 7-32
    • Schwiebert, E.M.1    Zsembery, A.2
  • 36
    • 0032928614 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase: Conservation of a three-kinase module from yeast to human
    • Widmann C, Gibson S, Jarpe MB, Johnson GL. Mitogen-activated protein kinase: conservation of a three-kinase module from yeast to human. Physiol Rev. 1999;79:143-180.
    • (1999) Physiol Rev , vol.79 , pp. 143-180
    • Widmann, C.1    Gibson, S.2    Jarpe, M.B.3    Johnson, G.L.4
  • 37
    • 0037821639 scopus 로고    scopus 로고
    • p38 and ERK1/2 coordinate cellular migration and proliferation in epithelial wound healing: Evidence of cross-talk activation between MAP kinase cascades
    • Sharma GD, He J, Bazan HE. p38 and ERK1/2 coordinate cellular migration and proliferation in epithelial wound healing: evidence of cross-talk activation between MAP kinase cascades. J Biol Chem. 2003;278:21989-21997.
    • (2003) J Biol Chem , vol.278 , pp. 21989-21997
    • Sharma, G.D.1    He, J.2    Bazan, H.E.3
  • 38
    • 0141539438 scopus 로고    scopus 로고
    • Phosphorylation of MAP kinase in corneal epithelial cells during wound healing
    • Imayasu M, Shimada S. Phosphorylation of MAP kinase in corneal epithelial cells during wound healing. Curr Eye Res. 2003;27:133-141.
    • (2003) Curr Eye Res , vol.27 , pp. 133-141
    • Imayasu, M.1    Shimada, S.2
  • 39
    • 0346727570 scopus 로고    scopus 로고
    • Role of p38 MAP kinase in regulation of cell migration and proliferation in healing corneal epithelium
    • Saika S, Okada Y, Miyamoto T, et al. Role of p38 MAP kinase in regulation of cell migration and proliferation in healing corneal epithelium. Invest Ophthalmol Vis Sci. 2004;45:100-109.
    • (2004) Invest Ophthalmol Vis Sci , vol.45 , pp. 100-109
    • Saika, S.1    Okada, Y.2    Miyamoto, T.3
  • 40
    • 0034886926 scopus 로고    scopus 로고
    • A role for MAP kinase in regulating ectodomain shedding of APLP2 in corneal epithelial cells
    • Xu K, Zoukhri D, Zieske J, et al. A role for MAP kinase in regulating ectodomain shedding of APLP2 in corneal epithelial cells. Am J Physiol Cell Physiol. 2001;280:C603-C614.
    • (2001) Am J Physiol Cell Physiol , vol.280
    • Xu, K.1    Zoukhri, D.2    Zieske, J.3
  • 41
    • 0037032817 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases
    • Johnson GL, Lapadat R. Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases. Science. 2002; 298:1911-1912.
    • (2002) Science , vol.298 , pp. 1911-1912
    • Johnson, G.L.1    Lapadat, R.2
  • 42
    • 0033573049 scopus 로고    scopus 로고
    • Ectodomain shedding of TGF-α and other transmembrane proteins is induced by receptor tyrosine kinase activation and MAP kinase signaling cascades
    • Fan H, Derynck R. Ectodomain shedding of TGF-α and other transmembrane proteins is induced by receptor tyrosine kinase activation and MAP kinase signaling cascades. EMBO J. 1999;18: 6962-6972.
    • (1999) EMBO J , vol.18 , pp. 6962-6972
    • Fan, H.1    Derynck, R.2
  • 43
    • 33846965544 scopus 로고    scopus 로고
    • Staphylococcus aureus protein A activates TACE through EGFR-dependent signaling
    • Gomez MI, Seaghdha MO, Prince AS. Staphylococcus aureus protein A activates TACE through EGFR-dependent signaling. EMBO J. 2007;26:701-709.
    • (2007) EMBO J , vol.26 , pp. 701-709
    • Gomez, M.I.1    Seaghdha, M.O.2    Prince, A.S.3
  • 44
    • 0042237924 scopus 로고    scopus 로고
    • The disintegrin-like metalloproteinase ADAM10 is involved in constitutive cleavage of CX3CL1 (fractalkine) and regulates CX3CL1-mediated cell-cell adhesion
    • Hundhausen C, Misztela D, Berkhout TA, et al. The disintegrin-like metalloproteinase ADAM10 is involved in constitutive cleavage of CX3CL1 (fractalkine) and regulates CX3CL1-mediated cell-cell adhesion. Blood. 2003;102:1186-1195.
    • (2003) Blood , vol.102 , pp. 1186-1195
    • Hundhausen, C.1    Misztela, D.2    Berkhout, T.A.3
  • 45
    • 0028953829 scopus 로고
    • An SV40-immortalized human corneal epithelial cell line and its characterization
    • Araki-Sasaki K, Ohashi Y, Sasabe T, et al. An SV40-immortalized human corneal epithelial cell line and its characterization. Invest Ophthalmol Vis Sci. 1995;36:614-621.
    • (1995) Invest Ophthalmol Vis Sci , vol.36 , pp. 614-621
    • Araki-Sasaki, K.1    Ohashi, Y.2    Sasabe, T.3
  • 46
    • 33746675805 scopus 로고    scopus 로고
    • SRC-family tyrosine kinases in wound- and ligand-induced epidermal growth factor receptor activation in human corneal epithelial cells
    • Xu KP, Yin J, Yu FS. SRC-family tyrosine kinases in wound- and ligand-induced epidermal growth factor receptor activation in human corneal epithelial cells. Invest Ophthalmol Vis Sci. 2006;47: 2832-2839.
    • (2006) Invest Ophthalmol Vis Sci , vol.47 , pp. 2832-2839
    • Xu, K.P.1    Yin, J.2    Yu, F.S.3
  • 47
    • 0032445816 scopus 로고    scopus 로고
    • Selective changes in protein kinase C (PKC) isoform expression in rabbit corneal epithelium during wound healing. Inhibition of corneal epithelial repair by PKCalpha antisense
    • Chandrasekher G, Bazan N, Bazan H. Selective changes in protein kinase C (PKC) isoform expression in rabbit corneal epithelium during wound healing. Inhibition of corneal epithelial repair by PKCalpha antisense. Exp Eye Res. 1998;67:603-610.
    • (1998) Exp Eye Res , vol.67 , pp. 603-610
    • Chandrasekher, G.1    Bazan, N.2    Bazan, H.3
  • 48
    • 0036905524 scopus 로고    scopus 로고
    • EGF-induced ERK phosphorylation independent of PKC isozymes in human corneal epithelial cells
    • Xu KP, Dartt DA, Yu FS. EGF-induced ERK phosphorylation independent of PKC isozymes in human corneal epithelial cells. Invest Ophthalmol Vis Sci. 2002;43:3673-3679.
    • (2002) Invest Ophthalmol Vis Sci , vol.43 , pp. 3673-3679
    • Xu, K.P.1    Dartt, D.A.2    Yu, F.S.3
  • 49
    • 0032079871 scopus 로고    scopus 로고
    • Extracellular calcium influx stimulates metalloproteinase cleavage and secretion of heparin-binding EGF-like growth factor independently of protein kinase C
    • Dethlefsen SM, Raab G, Moses MA, Adam RM, Klagsbrun M, Freeman MR. Extracellular calcium influx stimulates metalloproteinase cleavage and secretion of heparin-binding EGF-like growth factor independently of protein kinase C. J Cell Biochem. 1998;69:143-153.
    • (1998) J Cell Biochem , vol.69 , pp. 143-153
    • Dethlefsen, S.M.1    Raab, G.2    Moses, M.A.3    Adam, R.M.4    Klagsbrun, M.5    Freeman, M.R.6
  • 50
    • 0035985185 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: A potential role in regulated shedding
    • Diaz-Rodriguez E, Montero JC, Esparis-Ogando A, Yuste L, Pandiella A. Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding. Mol Biol Cell. 2002;13:2031-2044.
    • (2002) Mol Biol Cell , vol.13 , pp. 2031-2044
    • Diaz-Rodriguez, E.1    Montero, J.C.2    Esparis-Ogando, A.3    Yuste, L.4    Pandiella, A.5
  • 51
    • 0038719741 scopus 로고    scopus 로고
    • Characterization of growth factorinduced serine phosphorylation of tumor necrosis factor-alpha converting enzyme and of an alternatively translated polypeptide
    • Fan H, Turck CW, Derynck R. Characterization of growth factorinduced serine phosphorylation of tumor necrosis factor-alpha converting enzyme and of an alternatively translated polypeptide. J Biol Chem. 2003;278:18617-18627.
    • (2003) J Biol Chem , vol.278 , pp. 18617-18627
    • Fan, H.1    Turck, C.W.2    Derynck, R.3
  • 52
    • 21044444181 scopus 로고    scopus 로고
    • ERK-mediated phosphorylation of Thr735 in TNFalpha-converting enzyme and its potential role in TACE protein trafficking
    • Soond SM, Everson B, Riches DW, Murphy G. ERK-mediated phosphorylation of Thr735 in TNFalpha-converting enzyme and its potential role in TACE protein trafficking. J Cell Sci. 2005;118: 2371-2380.
    • (2005) J Cell Sci , vol.118 , pp. 2371-2380
    • Soond, S.M.1    Everson, B.2    Riches, D.W.3    Murphy, G.4
  • 53
    • 0035952656 scopus 로고    scopus 로고
    • Cell communication networks: Epidermal growth factor receptor transactivation as the paradigm for interreceptor signal transmission
    • Gschwind A, Zwick E, Prenzel N, Leserer M, Ullrich A. Cell communication networks: epidermal growth factor receptor transactivation as the paradigm for interreceptor signal transmission. Oncogene. 2001;20:1594-1600.
    • (2001) Oncogene , vol.20 , pp. 1594-1600
    • Gschwind, A.1    Zwick, E.2    Prenzel, N.3    Leserer, M.4    Ullrich, A.5
  • 54
    • 0030044360 scopus 로고    scopus 로고
    • Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors
    • Daub H, Weiss FU, Wallasch C, Ullrich A. Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors. Nature. 1996;379:557-560.
    • (1996) Nature , vol.379 , pp. 557-560
    • Daub, H.1    Weiss, F.U.2    Wallasch, C.3    Ullrich, A.4
  • 55
    • 0033917218 scopus 로고    scopus 로고
    • Epidermal growth factor receptor signal transactivation
    • Leserer M, Gschwind A, Ullrich A. Epidermal growth factor receptor signal transactivation. IUBMB Life. 2000;49:405-409.
    • (2000) IUBMB Life , vol.49 , pp. 405-409
    • Leserer, M.1    Gschwind, A.2    Ullrich, A.3
  • 58
    • 0034722889 scopus 로고    scopus 로고
    • The EGF receptor family as targets for cancer therapy
    • Mendelsohn J, Baselga J. The EGF receptor family as targets for cancer therapy. Oncogene. 2000;19:6550-6565.
    • (2000) Oncogene , vol.19 , pp. 6550-6565
    • Mendelsohn, J.1    Baselga, J.2
  • 59
    • 0037090626 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase-dependent and -independent routes control shedding of transmembrane growth factors through multiple secretases
    • Montero JC, Yuste L, Diaz-Rodriguez E, Esparis-Ogando A, Pandiella A. Mitogen-activated protein kinase-dependent and -independent routes control shedding of transmembrane growth factors through multiple secretases. Biochem J. 2002;363:211-221.
    • (2002) Biochem J , vol.363 , pp. 211-221
    • Montero, J.C.1    Yuste, L.2    Diaz-Rodriguez, E.3    Esparis-Ogando, A.4    Pandiella, A.5
  • 60
    • 0034012017 scopus 로고    scopus 로고
    • Insulin regulates soluble amyloid precursor protein release via phosphatidyl inositol 3 kinase-dependent pathway
    • Solano DC, Sironi M, Bonfini C, Solerte SB, Govoni S, Racchi M. Insulin regulates soluble amyloid precursor protein release via phosphatidyl inositol 3 kinase-dependent pathway. FASEB J. 2000; 14:1015-1022.
    • (2000) FASEB J , vol.14 , pp. 1015-1022
    • Solano, D.C.1    Sironi, M.2    Bonfini, C.3    Solerte, S.B.4    Govoni, S.5    Racchi, M.6
  • 61
    • 38049144010 scopus 로고    scopus 로고
    • Insulin stimulates the cleavage and release of the extracellular domain of Klotho by ADAM10 and ADAM17
    • Chen CD, Podvin S, Gillespie E, Leeman SE, Abraham CR. Insulin stimulates the cleavage and release of the extracellular domain of Klotho by ADAM10 and ADAM17. Proc Natl Acad Sci U S A. 2007;104:19796-19801.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 19796-19801
    • Chen, C.D.1    Podvin, S.2    Gillespie, E.3    Leeman, S.E.4    Abraham, C.R.5
  • 62
    • 34248591612 scopus 로고    scopus 로고
    • Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer
    • Roberts PJ, Der CJ. Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer. Oncogene. 2007;26:3291-3310.
    • (2007) Oncogene , vol.26 , pp. 3291-3310
    • Roberts, P.J.1    CJ, D.2
  • 63
    • 0029130410 scopus 로고
    • Rapid induction of heparin-binding epidermal growth factor/ diphtheria toxin receptor expression by Raf and Ras oncogenes
    • McCarthy SA, Samuels ML, Pritchard CA, Abraham JA, McMahon M. Rapid induction of heparin-binding epidermal growth factor/ diphtheria toxin receptor expression by Raf and Ras oncogenes. Genes Dev. 1995;9:1953-1964.
    • (1995) Genes Dev , vol.9 , pp. 1953-1964
    • McCarthy, S.A.1    Samuels, M.L.2    Pritchard, C.A.3    Abraham, J.A.4    McMahon, M.5
  • 64
    • 0035871383 scopus 로고    scopus 로고
    • Analysis of the transcriptional program induced by Raf in epithelial cells
    • Schulze A, Lehmann K, Jefferies HB, McMahon M, Downward J. Analysis of the transcriptional program induced by Raf in epithelial cells. Genes Dev. 2001;15:981-994.
    • (2001) Genes Dev , vol.15 , pp. 981-994
    • Schulze, A.1    Lehmann, K.2    Jefferies, H.B.3    McMahon, M.4    Downward, J.5
  • 65
    • 33750614996 scopus 로고    scopus 로고
    • Control of ErbB signaling through metalloprotease mediated ectodomain shedding of EGFlike factors
    • Sanderson MP, Dempsey PJ, Dunbar AJ. Control of ErbB signaling through metalloprotease mediated ectodomain shedding of EGFlike factors. Growth Factors. 2006;24:121-136.
    • (2006) Growth Factors , vol.24 , pp. 121-136
    • Sanderson, M.P.1    Dempsey, P.J.2    Dunbar, A.J.3


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