메뉴 건너뛰기




Volumn 402, Issue 6764, 1999, Pages 884-888

EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF

Author keywords

[No Author keywords available]

Indexed keywords

BATIMASTAT; BOMBESIN; CARBACHOL; ENDOTHELIN; EPIDERMAL GROWTH FACTOR; EPIDERMAL GROWTH FACTOR RECEPTOR; G PROTEIN COUPLED RECEPTOR; LIGAND; LYSOPHOSPHATIDIC ACID; METALLOPROTEINASE; PLATELET DERIVED GROWTH FACTOR; PLATELET DERIVED GROWTH FACTOR RECEPTOR; THROMBIN;

EID: 0033599039     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/47260     Document Type: Article
Times cited : (1523)

References (29)
  • 1
    • 0030683639 scopus 로고    scopus 로고
    • Signal characteristics of G protein transactivated EGF receptor
    • Daub, H., Wallasch, C., Lankenau, A., Herrlich, A. & Ullrich, A. Signal characteristics of G protein transactivated EGF receptor. EMBO J. 16, 7032-7044 (1997).
    • (1997) EMBO J. , vol.16 , pp. 7032-7044
    • Daub, H.1    Wallasch, C.2    Lankenau, A.3    Herrlich, A.4    Ullrich, A.5
  • 2
    • 0030044360 scopus 로고    scopus 로고
    • Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors
    • Daub, H., Weiss, F. U., Wallasch, C. & Ullrich, A. Role of transactivation of the EGF receptor in signalling by G-protein-coupled receptors. Nature 379, 557-560 (1996).
    • (1996) Nature , vol.379 , pp. 557-560
    • Daub, H.1    Weiss, F.U.2    Wallasch, C.3    Ullrich, A.4
  • 3
    • 0032938716 scopus 로고    scopus 로고
    • Regulation of tyrosine cascades by G-protein-coupled receptors
    • Luttrell, L. M., Daaka, Y. & Lefkowitz, R. J. Regulation of tyrosine cascades by G-protein-coupled receptors. Curr. Opin. Cell Biol. 11, 177-183 (1999).
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 177-183
    • Luttrell, L.M.1    Daaka, Y.2    Lefkowitz, R.J.3
  • 4
    • 0032915392 scopus 로고    scopus 로고
    • Epidermal growth factor receptors: Critical mediators of multiple receptor pathways
    • Hackel, P. O., Zwick, E., Prenzel, N. & Ullrich, A. Epidermal growth factor receptors: critical mediators of multiple receptor pathways. Curr. Opin. Cell Biol. 11, 184-189 (1999).
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 184-189
    • Hackel, P.O.1    Zwick, E.2    Prenzel, N.3    Ullrich, A.4
  • 5
    • 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
    • Eguchi, S. 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. 273, 8890-8896 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 8890-8896
    • Eguchi, S.1
  • 6
    • 0030614911 scopus 로고    scopus 로고
    • Gβγ subunits mediate Src-dependent phosphorylation of the epidermal growth factor receptor
    • Luttrell, L. M., Della Rocca, G. J., van Biesen, T., Luttrell, E. K. & Lefkowitz, R. J. Gβγ subunits mediate Src-dependent phosphorylation of the epidermal growth factor receptor. J. Biol. Chem. 272, 4637-4644 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 4637-4644
    • Luttrell, L.M.1    Della Rocca, G.J.2    Van Biesen, T.3    Luttrell, E.K.4    Lefkowitz, R.J.5
  • 8
    • 0030837027 scopus 로고    scopus 로고
    • The m1 muscarinic acetylcholine receptor transactivates the EGF receptor to modulate ion channel activity
    • Tsai, W., Morielli, A. D. & Peralta, E. G. The m1 muscarinic acetylcholine receptor transactivates the EGF receptor to modulate ion channel activity. EMBO J. 16, 4597-4605 (1997).
    • (1997) EMBO J. , vol.16 , pp. 4597-4605
    • Tsai, W.1    Morielli, A.D.2    Peralta, E.G.3
  • 9
    • 0032079960 scopus 로고    scopus 로고
    • Angiotensin II stimulates ERK via two pathways in epithelial cells: Protein kinase C suppresses a G-protein coupled receptor-EGF receptor transactivation pathway
    • Li, X., Lee, J. W., Graves, L. M. & Earp, H. S. Angiotensin II stimulates ERK via two pathways in epithelial cells: protein kinase C suppresses a G-protein coupled receptor-EGF receptor transactivation pathway, EMBO J. 9, 2574-2583 (1998).
    • (1998) EMBO J. , vol.9 , pp. 2574-2583
    • Li, X.1    Lee, J.W.2    Graves, L.M.3    Earp, H.S.4
  • 10
    • 0025866978 scopus 로고
    • Analysis of platelet-derived growth factor receptor domain function using a novel chimeric receptor approach
    • Seedorf, K., Felder, S., Millauer, B., Schlessinger, J. & Ullrich, A. Analysis of platelet-derived growth factor receptor domain function using a novel chimeric receptor approach. J. Biol. Chem. 266, 12424-12431 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 12424-12431
    • Seedorf, K.1    Felder, S.2    Millauer, B.3    Schlessinger, J.4    Ullrich, A.5
  • 11
    • 0028091564 scopus 로고
    • Selective platelet-derived growth factor receptor kinase blockers reverse sistransformation
    • Kovalenko, M. et al. Selective platelet-derived growth factor receptor kinase blockers reverse sistransformation. Cancer Res. 54, 6106-6114 (1994).
    • (1994) Cancer Res. , vol.54 , pp. 6106-6114
    • Kovalenko, M.1
  • 12
    • 0027399168 scopus 로고
    • Activation of a phosphotyrosine phosphatase by tyrosine phosphorytation
    • Vogel, W., Lammers, R., Huang, J. & Ullrich, A. Activation of a phosphotyrosine phosphatase by tyrosine phosphorytation. Science 259, 1611-1614 (1993).
    • (1993) Science , vol.259 , pp. 1611-1614
    • Vogel, W.1    Lammers, R.2    Huang, J.3    Ullrich, A.4
  • 13
    • 0030910482 scopus 로고    scopus 로고
    • Humanization of a mouse monoclonal antibody that blocks the epidermal growth factor receplor: Recovery of antagonistic activity
    • Mateo, C. et al. Humanization of a mouse monoclonal antibody that blocks the epidermal growth factor receplor: recovery of antagonistic activity, Immunotechnology 3, 71-81 (1997).
    • (1997) Immunotechnology , vol.3 , pp. 71-81
    • Mateo, C.1
  • 15
    • 0027269975 scopus 로고
    • Activated release of membrane-anchored TGF-α in the absence of cytosol
    • Bosenberg, M. W., Pandiella, A. & Massaque, J. Activated release of membrane-anchored TGF-α in the absence of cytosol. J. Cell Biol. 122, 95-101 (1993).
    • (1993) J. Cell Biol. , vol.122 , pp. 95-101
    • Bosenberg, M.W.1    Pandiella, A.2    Massaque, J.3
  • 16
    • 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. 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 6, 967-980 (1995).
    • (1995) Mol. Biol. Cell , vol.6 , pp. 967-980
    • Goishi, K.1
  • 17
    • 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, S. M. et al. Extracellular calcium influx stimulates metalloproteinase cleavage and secretion of heparin-binding EGF-like growth factor independently of protein kinase C. J. Cell. Biochem. 69, 143-153 (1998).
    • (1998) J. Cell. Biochem. , vol.69 , pp. 143-153
    • Dethlefsen, S.M.1
  • 18
    • 0030770603 scopus 로고    scopus 로고
    • Critical role of calcium-dependent epidermal growth factor receptor transactivation in PC12 cells membrane depolarization and bradykinin signaling
    • Zwick, E. et al. Critical role of calcium-dependent epidermal growth factor receptor transactivation in PC12 cells membrane depolarization and bradykinin signaling. J. Biol. Chem. 272, 24767-24770 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 24767-24770
    • Zwick, E.1
  • 19
    • 0031561480 scopus 로고    scopus 로고
    • Heparin-binding EGF-like growth factor
    • Raab, G. & Klagsbrun, M. Heparin-binding EGF-like growth factor. Biochim. Biophys. Acta 1333, F179-F199 (1997).
    • (1997) Biochim. Biophys. Acta , vol.1333
    • Raab, G.1    Klagsbrun, M.2
  • 20
    • 0026747170 scopus 로고
    • Expression cloning of a diphtheria toxin receptor; identity with a heparin-binding EGF-like growth factor precursor
    • Naglich, J. G., Metherall, J. E., Russell, D. W., & Eidels, L. Expression cloning of a diphtheria toxin receptor; identity with a heparin-binding EGF-like growth factor precursor. Cell 69, 1051-1061 (1992).
    • (1992) Cell , vol.69 , pp. 1051-1061
    • Naglich, J.G.1    Metherall, J.E.2    Russell, D.W.3    Eidels, L.4
  • 21
    • 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. & 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. Boil. Chem. 270, 1015-1019 (1995).
    • (1995) J. Boil. Chem. , vol.270 , pp. 1015-1019
    • Mitamura, T.1    Higashiyama, S.2    Taniguchi, N.3    Klagsbrun, M.4    Mekada, E.5
  • 22
    • 0029964035 scopus 로고    scopus 로고
    • Shc adaptor proteins are key transducers of mitogenic signaling mediated by the G protein-coupled thrombin receptor
    • Chen, Y. et al. Shc adaptor proteins are key transducers of mitogenic signaling mediated by the G protein-coupled thrombin receptor. EMBO J. 15, 1037-1044 (1996).
    • (1996) EMBO J. , vol.15 , pp. 1037-1044
    • Chen, Y.1
  • 23
    • 17444373968 scopus 로고    scopus 로고
    • A metalloprotease-disintegrin, MDC9/meltrin-γ/ADAM9 and PKCδ are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor
    • Izumi, Y. et al. A metalloprotease-disintegrin, MDC9/meltrin-γ/ADAM9 and PKCδ 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
  • 25
    • 0027730415 scopus 로고
    • Expression of mRNA for epidermal growth factor, transforming growth factor-alpha and their receptor in human prostate tissue and cell lines
    • Ching, K. Z. et al. Expression of mRNA for epidermal growth factor, transforming growth factor-alpha and their receptor in human prostate tissue and cell lines. Mol. Cell Biochem. 126, 151-158 (1993).
    • (1993) Mol. Cell Biochem. , vol.126 , pp. 151-158
    • Ching, K.Z.1
  • 26
    • 0027189659 scopus 로고
    • Differential effects of peptide hormones bombesin, vasoactive intestinal polypeptide and somatostatin analog RC-160 on the invasive capacity of human prostatic carcinoma cells
    • Hoosein, N. M., Logothetis, C. J. & Chung, L. W. K. Differential effects of peptide hormones bombesin, vasoactive intestinal polypeptide and somatostatin analog RC-160 on the invasive capacity of human prostatic carcinoma cells. J. Urol. 149, 1209-1213 (1993).
    • (1993) J. Urol. , vol.149 , pp. 1209-1213
    • Hoosein, N.M.1    Logothetis, C.J.2    Chung, L.W.K.3
  • 27
    • 0032991651 scopus 로고    scopus 로고
    • Metalloprotease-mediated ligand release regulates autocrine signaling through the epidermal growth factor receptor
    • Dong, J. et al. Metalloprotease-mediated ligand release regulates autocrine signaling through the epidermal growth factor receptor. Proc. Natl Acad. Sci. USA 96, 6235-6240 (1999).
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6235-6240
    • Dong, J.1
  • 28
    • 0030715322 scopus 로고    scopus 로고
    • ECM and cell surface proteolysis: Regulating cellular ecology
    • Werb, Z. ECM and cell surface proteolysis: regulating cellular ecology. Cell 91, 439-442 (1997).
    • (1997) Cell , vol.91 , pp. 439-442
    • Werb, Z.1
  • 29
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDA
    • Schägger, H. & von Iagow, G. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDA. Anal. Biochem. 166, 368-379 (1987).
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Iagow, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.