메뉴 건너뛰기




Volumn 995, Issue , 2003, Pages 22-38

TACE/ADAM17 processing of EGFR ligands indicates a role as a physiological convertase

Author keywords

ADAM; EGF family; EGF receptor; ERBB; TACE ADAM17; TGF

Indexed keywords

AMPHIREGULIN; CELL PROTEIN; EPIDERMAL GROWTH FACTOR RECEPTOR; GROWTH FACTOR; HEPARIN BINDING EPIDERMAL GROWTH FACTOR; LIGAND; MEMBRANE PROTEIN; PROTEINASE; TRANSFORMING GROWTH FACTOR ALPHA; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME;

EID: 0038806501     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2003.tb03207.x     Document Type: Conference Paper
Times cited : (156)

References (47)
  • 1
    • 0031936410 scopus 로고    scopus 로고
    • Specificity within the EGF family/ErbB receptor family signaling network
    • RIESE, D.J., II & D.F. STERN. 1998. Specificity within the EGF family/ErbB receptor family signaling network. Bioessays 20: 41-48.
    • (1998) Bioessays , vol.20 , pp. 41-48
    • Riese D.J. II1    Stern, D.F.2
  • 2
    • 0034600849 scopus 로고    scopus 로고
    • The ErbB signaling network: Receptor heterodimerization in development and cancer
    • OLAYIOYE, M.A. et al. 2000. The ErbB signaling network: receptor heterodimerization in development and cancer. EMBO J. 19: 3159-3167.
    • (2000) EMBO J , vol.19 , pp. 3159-3167
    • Olayioye, M.A.1
  • 3
    • 0028618937 scopus 로고
    • Structure-function relationships for the EGF/TGF-alpha family of mitogens
    • GROENEN, L.C., E.C. NICE & A.W. BURGESS. 1994. Structure-function relationships for the EGF/TGF-alpha family of mitogens. Growth Factors 11: 235-257.
    • (1994) Growth Factors , vol.11 , pp. 235-257
    • Groenen, L.C.1    Nice, E.C.2    Burgess, A.W.3
  • 4
    • 0033947243 scopus 로고    scopus 로고
    • Evolutionary analysis of the ErbB receptor and ligand families
    • STEIN, R.A. & J.V. STAROS. 2000. Evolutionary analysis of the ErbB receptor and ligand families. J. Mol. Evol. 50: 397-412.
    • (2000) J. Mol. Evol. , vol.50 , pp. 397-412
    • Stein, R.A.1    Staros, J.V.2
  • 5
    • 0038414842 scopus 로고    scopus 로고
    • EGF family ligands
    • Elsevier Science. Amsterdam/London/New York. In press
    • LEE, D.C. et al. 2003. EGF family ligands. In The Cytokine Handbook. Fourth Edition. Elsevier Science. Amsterdam/London/New York. In press.
    • (2003) The Cytokine Handbook. Fourth Edition
    • Lee, D.C.1
  • 6
    • 0033009389 scopus 로고    scopus 로고
    • Binding specificities and affinities of egf domains for ErbB receptors
    • JONES, J.T., R.W. AKITA & M.X. SLIWKOWSKI. 1999. Binding specificities and affinities of egf domains for ErbB receptors. FEBS Lett. 447: 227-231.
    • (1999) FEBS Lett. , vol.447 , pp. 227-231
    • Jones, J.T.1    Akita, R.W.2    Sliwkowski, M.X.3
  • 7
    • 0028823802 scopus 로고
    • Neu differentiation factor activation of ErbB-3 and ErbB-4 is cell specific and displays a differential requirement for ErbB-2
    • BEERLI, R.R. et al. 1995. Neu differentiation factor activation of ErbB-3 and ErbB-4 is cell specific and displays a differential requirement for ErbB-2. Mol. Cell. Biol. 15: 6496-6505.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6496-6505
    • Beerli, R.R.1
  • 8
    • 0029118223 scopus 로고
    • The cellular response to neuregulins is governed by complex interactions of the erbB receptor family
    • RIESE, D.J., II et al. 1995. The cellular response to neuregulins is governed by complex interactions of the erbB receptor family. Mol. Cell. Biol. 15: 5770-5776.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5770-5776
    • Riese D.J. II1
  • 9
    • 2142843806 scopus 로고    scopus 로고
    • Diversification of Neu differentiation factor and epidermal growth factor signaling by combinatorial receptor interactions
    • PINKAS-KRAMARSKI, R. et al. 1996. Diversification of Neu differentiation factor and epidermal growth factor signaling by combinatorial receptor interactions. EMBO J. 15: 2452-2467.
    • (1996) EMBO J. , vol.15 , pp. 2452-2467
    • Pinkas-Kramarski, R.1
  • 11
    • 0032515018 scopus 로고    scopus 로고
    • An essential role for ectodomain shedding in mammalian development
    • PESCHON, J.J. et al. 1998. An essential role for ectodomain shedding in mammalian development. Science 282: 1281-1284.
    • (1998) Science , vol.282 , pp. 1281-1284
    • Peschon, J.J.1
  • 12
    • 0021752924 scopus 로고
    • Human transforming growth factor-alpha: Precursor structure and expression in E. coli
    • DERYNCK, R. et al. 1984. Human transforming growth factor-alpha: precursor structure and expression in E. coli. Cell 38: 287-297.
    • (1984) Cell , vol.38 , pp. 287-297
    • Derynck, R.1
  • 13
    • 0021959133 scopus 로고
    • Cloning and sequence analysis of a cDNA for rat transforming growth factor-alpha
    • LEE, D.C. et al. 1985. Cloning and sequence analysis of a cDNA for rat transforming growth factor-alpha. Nature 313: 489-491.
    • (1985) Nature , vol.313 , pp. 489-491
    • Lee, D.C.1
  • 14
    • 0022981639 scopus 로고
    • Biologically active precursor for transforming growth factor type alpha, released by retrovirally transformed cells
    • IGNOTZ, R.A. et al. 1986. Biologically active precursor for transforming growth factor type alpha, released by retrovirally transformed cells. Proc. Natl. Acad. Sci. USA 83: 6307-6311.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6307-6311
    • Ignotz, R.A.1
  • 15
    • 0023682326 scopus 로고
    • Characterization of high molecular weight transforming growth factor alpha produced by rat hepatocellular carcinoma cells
    • LUETTEKE, N.C. et al. 1988. Characterization of high molecular weight transforming growth factor alpha produced by rat hepatocellular carcinoma cells. Biochemistry 27: 6487-6494.
    • (1988) Biochemistry , vol.27 , pp. 6487-6494
    • Luetteke, N.C.1
  • 16
    • 0023839736 scopus 로고
    • Structural properties of a soluble bioactive precursor for transforming growth factor-alpha
    • TEIXIDO, J. & J. MASSAGUE. 1988. Structural properties of a soluble bioactive precursor for transforming growth factor-alpha. J. Biol. Chem. 263: 3924-3929.
    • (1988) J. Biol. Chem. , vol.263 , pp. 3924-3929
    • Teixido, J.1    Massague, J.2
  • 17
    • 0025240094 scopus 로고
    • Generation of transforming growth factor-alpha from the cell surface by an O-glycosylation-independent multistep process
    • TEIXIDO, J. et al. 1990. Generation of transforming growth factor-alpha from the cell surface by an O-glycosylation-independent multistep process. J. Biol. Chem. 265: 6410-6415.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6410-6415
    • Teixido, J.1
  • 18
    • 15844406752 scopus 로고    scopus 로고
    • Diverse cell surface protein ectodomains are shed by a system sensitive to metalloprotease inhibitors
    • ARRIBAS, J. et al. 1996. Diverse cell surface protein ectodomains are shed by a system sensitive to metalloprotease inhibitors. J. Biol. Chem. 271: 11376-11382.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11376-11382
    • Arribas, J.1
  • 19
    • 0026079746 scopus 로고
    • Multiple signals activate cleavage of the membrane transforming growth factor-alpha precursor
    • PANDIELLA, A. & J. MASSAGUE. 1991. Multiple signals activate cleavage of the membrane transforming growth factor-alpha precursor. J. Biol. Chem. 266: 5769-5773.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5769-5773
    • Pandiella, A.1    Massague, J.2
  • 20
    • 0030038201 scopus 로고    scopus 로고
    • Autocrine regulation of membrane transforming growth factor-alpha cleavage
    • BASELGA, J. et al. 1996. Autocrine regulation of membrane transforming growth factor-alpha cleavage. J. Biol. Chem. 271: 3279-3284.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3279-3284
    • Baselga, J.1
  • 21
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells
    • BLACK, R.A. et al. 1997. A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. Nature 385: 729-733.
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.A.1
  • 22
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha
    • Moss, M.L. et al. 1997. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha. Nature 385: 733-736.
    • (1997) Nature , vol.385 , pp. 733-736
    • Moss, M.L.1
  • 23
    • 0037224740 scopus 로고    scopus 로고
    • The ADAMs family of metalloproteases: Multidomain proteins with multiple functions
    • SEALS, D.F. & S.A. COURTNEIDGE. 2003. The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev. 17: 7-30.
    • (2003) Genes Dev. , vol.17 , pp. 7-30
    • Seals, D.F.1    Courtneidge, S.A.2
  • 24
    • 0037066757 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha converting enzyme (TACE) regulates epidermal growth factor receptor ligand availability
    • SUNNARBORG, S.W. et al. 2002. Tumor necrosis factor-alpha converting enzyme (TACE) regulates epidermal growth factor receptor ligand availability. J. Biol. Chem. 277: 12838-12845.
    • (2002) J. Biol. Chem. , vol.277 , pp. 12838-12845
    • Sunnarborg, S.W.1
  • 25
    • 1842332725 scopus 로고    scopus 로고
    • The carboxyl-terminal valine residues of proTGF alpha are required for its efficient maturation and intracellular routing
    • BRILEY, G.P. et al. 1997. The carboxyl-terminal valine residues of proTGF alpha are required for its efficient maturation and intracellular routing. Mol. Biol. Cell 8: 1619-1631.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1619-1631
    • Briley, G.P.1
  • 26
    • 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. 1995. 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) Mol. Biol. Cell , vol.6 , pp. 967-980
    • Goishi, K.1
  • 27
    • 10244252796 scopus 로고    scopus 로고
    • Characterization of the mouse transforming growth factor alpha gene: Its expression during eyelid development and in waved 1 tissues
    • BERKOWITZ, E.A. et al. 1996. Characterization of the mouse transforming growth factor alpha gene: its expression during eyelid development and in waved 1 tissues. Cell Growth Differ. 7: 1271-1282.
    • (1996) Cell Growth Differ. , vol.7 , pp. 1271-1282
    • Berkowitz, E.A.1
  • 28
    • 0032795261 scopus 로고    scopus 로고
    • Targeted inactivation of the EGF and amphiregulin genes reveals distinct roles for EGF receptor ligands in mouse mammary gland development
    • LUETTEKE, N.C. et al. 1999. Targeted inactivation of the EGF and amphiregulin genes reveals distinct roles for EGF receptor ligands in mouse mammary gland development. Development 126: 2739-2750.
    • (1999) Development , vol.126 , pp. 2739-2750
    • Luetteke, N.C.1
  • 29
    • 0028344729 scopus 로고
    • The mouse waved-2 phenotype results from a point mutation in the EGF receptor tyrosine kinase
    • LUETTEKE, N.C. et al. 1994. The mouse waved-2 phenotype results from a point mutation in the EGF receptor tyrosine kinase. Genes Dev. 8: 399-413.
    • (1994) Genes Dev. , vol.8 , pp. 399-413
    • Luetteke, N.C.1
  • 30
    • 0028944112 scopus 로고
    • A mutation in the epidermal growth factor receptor in waved-2 mice has a profound effect on receptor biochemistry that results in impaired lactation
    • FOWLER, K.J. et al. 1995. A mutation in the epidermal growth factor receptor in waved-2 mice has a profound effect on receptor biochemistry that results in impaired lactation. Proc. Natl. Acad. Sci. USA 92: 1465-1469.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1465-1469
    • Fowler, K.J.1
  • 31
    • 0035930617 scopus 로고    scopus 로고
    • Metalloprotease-dependent protransforming growth factor-alpha ectodomain shedding in the absence of tumor necrosis factor-alpha-converting enzyme
    • MERLOS-SUAREZ, A. et al. 2001. Metalloprotease-dependent protransforming growth factor-alpha ectodomain shedding in the absence of tumor necrosis factor-alpha-converting enzyme. J. Biol. Chem. 276: 48510-48517.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48510-48517
    • Merlos-Suarez, A.1
  • 32
    • 0037465443 scopus 로고    scopus 로고
    • Multiple metalloproteases process protransforming growth factor-α (proTGFα)
    • HINKLE, C.L. et al. 2003. Multiple metalloproteases process protransforming growth factor-α (proTGFα). Biochemistry 42: 2127-2136.
    • (2003) Biochemistry , vol.42 , pp. 2127-2136
    • Hinkle, C.L.1
  • 33
    • 0035313164 scopus 로고    scopus 로고
    • Pulmonary hypoplasia in mice lacking tumor necrosis factor-alpha converting enzyme indicates an indispensable role for cell surface protein shedding during embryonic lung branching morphogenesis
    • ZHAO, J. et al. 2001. Pulmonary hypoplasia in mice lacking tumor necrosis factor-alpha converting enzyme indicates an indispensable role for cell surface protein shedding during embryonic lung branching morphogenesis. Dev. Biol. 232: 204-218.
    • (2001) Dev. Biol. , vol.232 , pp. 204-218
    • Zhao, J.1
  • 34
    • 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. et al. 1998. 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) EMBO J. , vol.17 , pp. 7260-7272
    • Izumi, Y.1
  • 35
    • 0036152681 scopus 로고    scopus 로고
    • Platelet-activating factor receptor and ADAM10 mediate responses to Staphylococcus aureus in epithelial cells
    • LEMJABBAR, H. & C. BASBAUM. 2002. Platelet-activating factor receptor and ADAM10 mediate responses to Staphylococcus aureus in epithelial cells. Nat. Med. 8: 41-46.
    • (2002) Nat. Med. , vol.8 , pp. 41-46
    • Lemjabbar, H.1    Basbaum, C.2
  • 36
    • 0037157854 scopus 로고    scopus 로고
    • The metalloprotease Kuzbanian (ADAM 10) mediates the transactivation of EGF receptor by G protein-coupled receptors
    • YAN, Y., K. SHIRAKABE & Z. WERB. 2002. The metalloprotease Kuzbanian (ADAM 10) mediates the transactivation of EGF receptor by G protein-coupled receptors. J. Cell Biol. 158: 221-226.
    • (2002) J. Cell Biol. , vol.158 , pp. 221-226
    • Yan, Y.1    Shirakabe, K.2    Werb, Z.3
  • 37
    • 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. et al. 2002. Cardiac hypertrophy is inhibited by antagonism of ADAM12 processing of HB-EGF: metalloproteinase inhibitors as a new therapy. Nat. Med. 8: 35-40.
    • (2002) Nat. Med. , vol.8 , pp. 35-40
    • Asakura, M.1
  • 38
    • 0036468005 scopus 로고    scopus 로고
    • CD44 anchors the assembly of matrilysin/MMP-7 with heparin-binding epidermal growth factor precursor and ErbB4 and regulates female reproductive organ remodeling
    • Yu, W.H. et al. 2002. CD44 anchors the assembly of matrilysin/MMP-7 with heparin-binding epidermal growth factor precursor and ErbB4 and regulates female reproductive organ remodeling. Genes Dev. 16: 307-323.
    • (2002) Genes Dev. , vol.16 , pp. 307-323
    • Yu, W.H.1
  • 39
    • 14444272986 scopus 로고    scopus 로고
    • Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor
    • BUXBAUM, J.D. et al. 1998. Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor. J. Biol. Chem. 273: 27765-27767.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27765-27767
    • Buxbaum, J.D.1
  • 40
    • 0035424693 scopus 로고    scopus 로고
    • Constitutive shedding of the amyloid precursor protein ectodomain is up-regulated by tumour necrosis factor-alpha converting enzyme
    • SLACK, B.E., L.K. MA & C.C. SEAH. 2001. Constitutive shedding of the amyloid precursor protein ectodomain is up-regulated by tumour necrosis factor-alpha converting enzyme. Biochem. J. 357: 787-794.
    • (2001) Biochem. J. , vol.357 , pp. 787-794
    • Slack, B.E.1    Ma, L.K.2    Seah, C.C.3
  • 41
    • 0034616385 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha-converting enzyme is required for cleavage of erbB4/HER4
    • ROI, C. et al. 2000. Tumor necrosis factor-alpha-converting enzyme is required for cleavage of erbB4/HER4. J. Biol. Chem. 275: 10379-10387.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10379-10387
    • Roi, C.1
  • 42
    • 18644384411 scopus 로고    scopus 로고
    • Transmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMs
    • FRANZKE, C.W. et al. 2002. Transmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMs. EMBO J. 21: 5026-5035.
    • (2002) EMBO J. , vol.21 , pp. 5026-5035
    • Franzke, C.W.1
  • 43
    • 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. et al. 2002. Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding. Mol. Biol. Cell 13: 2031-2044.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2031-2044
    • Diaz-Rodriguez, E.1
  • 44
    • 0037044786 scopus 로고    scopus 로고
    • Evidence for regulation of the tumor necrosis factor alpha-convertase (TACE) by protein-tyrosine phosphatase PTPH1
    • ZHENG, Y., J. SCHLONDORFF & C.P. BLOBEL. 2002. Evidence for regulation of the tumor necrosis factor alpha-convertase (TACE) by protein-tyrosine phosphatase PTPH1. J. Biol. Chem. 277: 42463-42470.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42463-42470
    • Zheng, Y.1    Schlondorff, J.2    Blobel, C.P.3
  • 45
    • 0034640286 scopus 로고    scopus 로고
    • Functional analysis of the domain structure of tumor necrosis factor-alpha converting enzyme
    • REDDY, P. et al. 2000. Functional analysis of the domain structure of tumor necrosis factor-alpha converting enzyme. J. Biol. Chem. 275: 14608-14614.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14608-14614
    • Reddy, P.1
  • 46
    • 0025372020 scopus 로고
    • Cell-cell adhesion mediated by binding of membrane-anchored transforming growth factor alpha to epidermal growth factor receptors promotes cell proliferation
    • ANKLESARIA, P. et al. 1990. Cell-cell adhesion mediated by binding of membrane-anchored transforming growth factor alpha to epidermal growth factor receptors promotes cell proliferation. Proc. Natl. Acad. Sci. USA 87: 3289-3293.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3289-3293
    • Anklesaria, P.1
  • 47
    • 0033520312 scopus 로고    scopus 로고
    • Contact-dependent growth inhibition and apoptosis of epidermal growth factor (EGF) receptor-expressing cells by the membrane-anchored form of heparin-binding EGF-like growth factor
    • IWAMOTO, R., K. HANDA & E. MEKADA. 1999. Contact-dependent growth inhibition and apoptosis of epidermal growth factor (EGF) receptor-expressing cells by the membrane-anchored form of heparin-binding EGF-like growth factor. J. Biol. Chem. 274: 25906-25912.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25906-25912
    • Iwamoto, R.1    Handa, K.2    Mekada, E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.