메뉴 건너뛰기




Volumn 164, Issue 5, 2004, Pages 769-779

Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands

Author keywords

ADAMs; Ectodomain shedding; EGF receptor; EGF receptor ligands; Growth factor signaling

Indexed keywords

AMPHIREGULIN; BETACELLULIN; CELL PROTEIN; DISINTEGRIN; EPIDERMAL GROWTH FACTOR RECEPTOR; EPIREGULIN; HEPARIN BINDING EPIDERMAL GROWTH FACTOR; LIGAND; PROTEIN ADAM10; PROTEIN ADAM12; PROTEIN ADAM15; PROTEIN ADAM17; PROTEIN ADAM19; PROTEIN ADAM9; TRANSFORMING GROWTH FACTOR ALPHA; UNCLASSIFIED DRUG;

EID: 1442358746     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200307137     Document Type: Article
Times cited : (843)

References (58)
  • 2
    • 0031698581 scopus 로고    scopus 로고
    • ADAMs: Focus on the protease domain
    • Black, R.A., and J.M. White. 1998. ADAMs: focus on the protease domain. Curr. Opin. Cell Biol. 10:654-659.
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 654-659
    • Black, R.A.1    White, J.M.2
  • 3
    • 0037416187 scopus 로고    scopus 로고
    • TACE is required for the activation of the EGFR by TGF-α in tumors
    • Borrell-Pages, M., F. Rojo, J. Albanell, J. Baselga, and J. Arribas. 2003. TACE is required for the activation of the EGFR by TGF-α in tumors. EMBO J. 22:1114-1124.
    • (2003) EMBO J. , vol.22 , pp. 1114-1124
    • Borrell-Pages, M.1    Rojo, F.2    Albanell, J.3    Baselga, J.4    Arribas, J.5
  • 6
    • 84916265276 scopus 로고
    • Isolation of a mouse submaxillary gland protein accelerating incisor eruption and eyelid opening in the new-born animal
    • Cohen, S. 1962. Isolation of a mouse submaxillary gland protein accelerating incisor eruption and eyelid opening in the new-born animal. J. Biol. Chem. 237:1555-1562.
    • (1962) J. Biol. Chem. , vol.237 , pp. 1555-1562
    • Cohen, S.1
  • 7
    • 0013825447 scopus 로고
    • The stimulation of epidermal proliferation by a specific protein (EGF)
    • Cohen, S. 1965. The stimulation of epidermal proliferation by a specific protein (EGF). Dev. Biol. 12:394-407.
    • (1965) Dev. Biol. , vol.12 , pp. 394-407
    • Cohen, S.1
  • 8
    • 0000201238 scopus 로고
    • Growth factors from murine sarcoma virus-transformed cells
    • de Larco, J.E., and G.J. Todaro. 1978. Growth factors from murine sarcoma virus-transformed cells. Proc. Natl. Acad. Sci. USA. 75:4001-4005.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4001-4005
    • De Larco, J.E.1    Todaro, G.J.2
  • 9
    • 0030857115 scopus 로고    scopus 로고
    • Apical enrichment of human EGF precursor in Madin-Darby canine kidney cells involves preferential basolateral ectodomain cleavage sensitive to a metalloprotease inhibitor
    • Dempsey, P.J., K.S. Meise, Y. Yoshitake, K. Nishikawa, and R.J. Coffey. 1997. Apical enrichment of human EGF precursor in Madin-Darby canine kidney cells involves preferential basolateral ectodomain cleavage sensitive to a metalloprotease inhibitor. J. Cell Biol. 138:747-758.
    • (1997) J. Cell Biol. , vol.138 , pp. 747-758
    • Dempsey, P.J.1    Meise, K.S.2    Yoshitake, Y.3    Nishikawa, K.4    Coffey, R.J.5
  • 10
    • 0021752924 scopus 로고
    • Human transforming growth factor-α: Precursor structure and expression in E. coli
    • Derynck, R., A.B. Roberts, M.E. Winkler, E.Y. Chen, and D.V. Goeddel. 1984. Human transforming growth factor-α: precursor structure and expression in E. coli. Cell. 38:287-297.
    • (1984) Cell , vol.38 , pp. 287-297
    • Derynck, R.1    Roberts, A.B.2    Winkler, M.E.3    Chen, E.Y.4    Goeddel, D.V.5
  • 11
    • 0032991651 scopus 로고    scopus 로고
    • Metalloprotease-mediated ligand release regulates autocrine signaling through the epidermal growth factor receptor
    • Dong, J., L.K. Opresko, P.J. Dempsey, D.A. Lauffenburger, R.J. Coffey, and H.S. Wiley. 1999. Metalloprotease-mediated ligand release regulates autocrine signaling through the epidermal growth factor receptor. Proc. Natl. Acad. Sci. USA. 96:6235-6240.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6235-6240
    • Dong, J.1    Opresko, L.K.2    Dempsey, P.J.3    Lauffenburger, D.A.4    Coffey, R.J.5    Wiley, H.S.6
  • 12
    • 0036339998 scopus 로고    scopus 로고
    • Mechanism of activation of the Drosophila EGF receptor by the TGFα ligand Gurken during oogenesis
    • Ghiglione, C., E.A. Bach, Y. Paraiso, K.L. Carraway, III, S. Noselli, and N. Perrimon. 2002. Mechanism of activation of the Drosophila EGF receptor by the TGFα ligand Gurken during oogenesis. Development. 129:175-186.
    • (2002) Development , vol.129 , pp. 175-186
    • Ghiglione, C.1    Bach, E.A.2    Paraiso, Y.3    Carraway III, K.L.4    Noselli, S.5    Perrimon, N.6
  • 13
    • 0038581051 scopus 로고    scopus 로고
    • TACE cleavage of proamphiregulin regulates GPCR-induced proliferation and motility of cancer cells
    • Gschwind, A., S. Hart, O.M. Fischer, and A. Ullrich. 2003. TACE cleavage of proamphiregulin regulates GPCR-induced proliferation and motility of cancer cells. EMBO J. 22:2411-2421.
    • (2003) EMBO J. , vol.22 , pp. 2411-2421
    • Gschwind, A.1    Hart, S.2    Fischer, O.M.3    Ullrich, A.4
  • 16
    • 0025904265 scopus 로고
    • A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF
    • Higashiyama, S., J.A. Abraham, J. Miller, J.C. Fiddes, and M. Klagsbrun. 1991. A heparin-binding growth factor secreted by macrophage-like cells that is related to EGF. Science. 251:936-939.
    • (1991) Science , vol.251 , pp. 936-939
    • Higashiyama, S.1    Abraham, J.A.2    Miller, J.3    Fiddes, J.C.4    Klagsbrun, M.5
  • 20
    • 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., M. Hirata, H. Hasuwa, R. Iwamoto, T. Umata, K. Miyado, Y. Tamai, T. Kurisaki, A. Sehara-Fujisawa, S. Ohno, and E. Mekada. 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    Hirata, M.2    Hasuwa, H.3    Iwamoto, R.4    Umata, T.5    Miyado, K.6    Tamai, Y.7    Kurisaki, T.8    Sehara-Fujisawa, A.9    Ohno, S.10    Mekada, E.11
  • 21
    • 0037507267 scopus 로고    scopus 로고
    • Defective valvulogenesis in HB-EGF and TACE-null mice is associated with aberrant BMP signaling
    • Jackson, L.F., T.H. Qiu, S.W. Sunnarborg, A. Chang, C. Zhang, C. Patterson, and D.C. Lee. 2003. Defective valvulogenesis in HB-EGF and TACE-null mice is associated with aberrant BMP signaling. EMBO J. 22:2704-2716.
    • (2003) EMBO J. , vol.22 , pp. 2704-2716
    • Jackson, L.F.1    Qiu, T.H.2    Sunnarborg, S.W.3    Chang, A.4    Zhang, C.5    Patterson, C.6    Lee, D.C.7
  • 23
    • 0035913906 scopus 로고    scopus 로고
    • Regulated intracellular ligand transport and proteolysis control EGF signal activation in Drosophila
    • Lee, J.R., S. Urban, C.F. Garvey, and M. Freeman. 2001. Regulated intracellular ligand transport and proteolysis control EGF signal activation in Drosophila. Cell. 107:161-171.
    • (2001) Cell , vol.107 , pp. 161-171
    • Lee, J.R.1    Urban, S.2    Garvey, C.F.3    Freeman, M.4
  • 24
    • 0036152681 scopus 로고    scopus 로고
    • Platelet-activating factor receptor and ADAM10 mediate responses to Staphylococcus aureus in epithelial cells
    • Lemjabbar, H., and 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
  • 25
    • 0038506712 scopus 로고    scopus 로고
    • Tobacco smoke-induced lung cell proliferation mediated by tumor necrosis factor α-converting enzyme and amphiregulin
    • Lemjabbar, H., D. Li, M. Gallup, S. Sidhu, E. Drori, and C. Basbaum. 2003. Tobacco smoke-induced lung cell proliferation mediated by tumor necrosis factor α-converting enzyme and amphiregulin. J. Biol. Chem. 278:26202-26207.
    • (2003) J. Biol. Chem. , vol.278 , pp. 26202-26207
    • Lemjabbar, H.1    Li, D.2    Gallup, M.3    Sidhu, S.4    Drori, E.5    Basbaum, C.6
  • 26
    • 0027315183 scopus 로고
    • Mice with a null mutation of the TGF α gene have abnormal skin architecture, wavy hair, and curly whiskers and often develop corneal inflammation
    • Mann, G.B., K.J. Fowler, A. Gabriel, E.C. Nice, R.L. Williams, and A.R. Dunn. 1993. Mice with a null mutation of the TGF α gene have abnormal skin architecture, wavy hair, and curly whiskers and often develop corneal inflammation. Cell. 73:249-261.
    • (1993) Cell , vol.73 , pp. 249-261
    • Mann, G.B.1    Fowler, K.J.2    Gabriel, A.3    Nice, E.C.4    Williams, R.L.5    Dunn, A.R.6
  • 27
  • 28
    • 0035930617 scopus 로고    scopus 로고
    • Metalloprotease-dependent protransforming growth factor-α ectodomain shedding in the absence of tumor necrosis factor-α-converting enzyme
    • Merlos-Suarez, A., S. Ruiz-Paz, J. Baselga, and J. Arribas. 2001. Metalloprotease-dependent protransforming growth factor-α ectodomain shedding in the absence of tumor necrosis factor-α-converting enzyme. J. Biol. Chem. 276:48510-48517.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48510-48517
    • Merlos-Suarez, A.1    Ruiz-Paz, S.2    Baselga, J.3    Arribas, J.4
  • 29
    • 0029074587 scopus 로고
    • Epithelial immaturity and multiorgan failure in mice lacking epidermal growth factor receptor
    • Miettinen, P.J., J.E. Berger, J. Meneses, Y. Phung, R.A. Pedersen, Z. Werb, and R. Derynck. 1995. Epithelial immaturity and multiorgan failure in mice lacking epidermal growth factor receptor. Nature. 376:337-341.
    • (1995) Nature , vol.376 , pp. 337-341
    • Miettinen, P.J.1    Berger, J.E.2    Meneses, J.3    Phung, Y.4    Pedersen, R.A.5    Werb, Z.6    Derynck, R.7
  • 31
    • 0033599039 scopus 로고    scopus 로고
    • EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF
    • Prenzel, N., E. Zwick, H. Daub, M. Leserer, R. Abraham, C. Wallasch, and A. Ullrich. 1999. EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF. Nature. 402:884-888.
    • (1999) Nature , vol.402 , pp. 884-888
    • Prenzel, N.1    Zwick, E.2    Daub, H.3    Leserer, M.4    Abraham, R.5    Wallasch, C.6    Ullrich, A.7
  • 32
    • 0034141195 scopus 로고    scopus 로고
    • The ADAM gene family: Surface proteins with an adhesion and protease activity packed into a single molecule
    • Primakoff, P., and D.G. Myles. 2000. The ADAM gene family: surface proteins with an adhesion and protease activity packed into a single molecule. Trends Genet. 16:83-87.
    • (2000) Trends Genet. , vol.16 , pp. 83-87
    • Primakoff, P.1    Myles, D.G.2
  • 33
    • 0032741143 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: Modular proteins capable of promoting cell-cell interactions and triggering signals by protein ectodomain shedding
    • Schlöndorff, J., and C.P. Blobel. 1999. Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein ectodomain shedding. J. Cell Sci. 112:3603-3617.
    • (1999) J. Cell Sci. , vol.112 , pp. 3603-3617
    • Schlöndorff, J.1    Blobel, C.P.2
  • 34
    • 0038541768 scopus 로고    scopus 로고
    • Intracellular maturation and localization of the tumour necrosis factor α convertase (TACE)
    • Schlöndorff, J., J.D. Becherer, and C.P. Blobel. 2000. Intracellular maturation and localization of the tumour necrosis factor α convertase (TACE). Biochem. J. 347:131-138.
    • (2000) Biochem. J. , vol.347 , pp. 131-138
    • Schlöndorff, J.1    Becherer, J.D.2    Blobel, C.P.3
  • 35
    • 0037224740 scopus 로고    scopus 로고
    • The ADAMs family of metalloproteases: Multidomain proteins with multiple functions
    • Seals, D.F., and 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
  • 36
    • 0037429688 scopus 로고    scopus 로고
    • Signaling by the Drosophila epidermal growth factor receptor pathway during development
    • Shilo, B.Z. 2003. Signaling by the Drosophila epidermal growth factor receptor pathway during development. Exp. Cell Res. 284:140-149.
    • (2003) Exp. Cell Res. , vol.284 , pp. 140-149
    • Shilo, B.Z.1
  • 38
    • 0024593476 scopus 로고
    • Structure and function of human amphiregulin: A member of the epidermal growth factor family
    • Shoyab, M., G.D. Plowman, V.L. McDonald, J.G. Bradley, and G.J. Todaro. 1989. Structure and function of human amphiregulin: a member of the epidermal growth factor family. Science. 243:1074-1076.
    • (1989) Science , vol.243 , pp. 1074-1076
    • Shoyab, M.1    Plowman, G.D.2    McDonald, V.L.3    Bradley, J.G.4    Todaro, G.J.5
  • 39
    • 0029045856 scopus 로고
    • Strain-dependent epithelial defects in mice lacking the EGF receptor
    • Sibilia, M., and E.F. Wagner. 1995. Strain-dependent epithelial defects in mice lacking the EGF receptor. Science. 269:234-238.
    • (1995) Science , vol.269 , pp. 234-238
    • Sibilia, M.1    Wagner, E.F.2
  • 40
    • 0035947578 scopus 로고    scopus 로고
    • Cloning and biological activity of epigen, a novel member of the epidermal growth factor superfamily
    • Strachan, L., J.G. Murison, R.L. Prestidge, M.A. Sleeman, J.D. Watson, and K.D. Kumble. 2001. Cloning and biological activity of epigen, a novel member of the epidermal growth factor superfamily. J. Biol. Chem. 276:18265-18271.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18265-18271
    • Strachan, L.1    Murison, J.G.2    Prestidge, R.L.3    Sleeman, M.A.4    Watson, J.D.5    Kumble, K.D.6
  • 42
    • 0032562703 scopus 로고    scopus 로고
    • Complex, two-way traffic of molecules across the membrane of the endoplasmic reticulum
    • Suzuki, T., Q. Yan, and W.J. Lennarz. 1998. Complex, two-way traffic of molecules across the membrane of the endoplasmic reticulum. J. Biol. Chem. 273:10083-10086.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10083-10086
    • Suzuki, T.1    Yan, Q.2    Lennarz, W.J.3
  • 44
    • 0013543749 scopus 로고
    • Transforming growth factors produced by certain human tumor cells: Polypeptides that interact with epidermal growth factor receptors
    • Todaro, G.J., C. Fryling, and J.E. De Larco. 1980. Transforming growth factors produced by certain human tumor cells: polypeptides that interact with epidermal growth factor receptors. Proc. Natl. Acad. Sci. USA. 77:5258-5262.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5258-5262
    • Todaro, G.J.1    Fryling, C.2    De Larco, J.E.3
  • 46
    • 0028937620 scopus 로고
    • Epiregulin. A novel epidermal growth factor with mitogenic activity for rat primary hepatocytes
    • Toyoda, H., T. Komurasaki, D. Uchida, Y. Takayama, T. Isobe, T. Okuyama, and K. Hanada. 1995. Epiregulin. A novel epidermal growth factor with mitogenic activity for rat primary hepatocytes. J. Biol. Chem. 270:7495-7500.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7495-7500
    • Toyoda, H.1    Komurasaki, T.2    Uchida, D.3    Takayama, Y.4    Isobe, T.5    Okuyama, T.6    Hanada, K.7
  • 47
    • 0037080869 scopus 로고    scopus 로고
    • Intracellular trafficking by Star regulates cleavage of the Drosophila EGF receptor ligand Spitz
    • Tsruya, R., A. Schlesinger, A. Reich, L. Gabay, A. Sapir, and B.Z. Shilo. 2002. Intracellular trafficking by Star regulates cleavage of the Drosophila EGF receptor ligand Spitz. Genes Dev. 16:222-234.
    • (2002) Genes Dev. , vol.16 , pp. 222-234
    • Tsruya, R.1    Schlesinger, A.2    Reich, A.3    Gabay, L.4    Sapir, A.5    Shilo, B.Z.6
  • 48
    • 0035913908 scopus 로고    scopus 로고
    • Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases
    • Urban, S., J.R. Lee, and M. Freeman. 2001. Drosophila rhomboid-1 defines a family of putative intramembrane serine proteases. Cell. 107:173-182.
    • (2001) Cell , vol.107 , pp. 173-182
    • Urban, S.1    Lee, J.R.2    Freeman, M.3
  • 49
    • 0037102238 scopus 로고    scopus 로고
    • A family of Rhomboid intramembrane proteases activates all Drosophila membrane-tethered EGF ligands
    • Urban, S., J.R. Lee, and M. Freeman. 2002. A family of Rhomboid intramembrane proteases activates all Drosophila membrane-tethered EGF ligands. EMBO J. 21:4277-4286.
    • (2002) EMBO J. , vol.21 , pp. 4277-4286
    • Urban, S.1    Lee, J.R.2    Freeman, M.3
  • 50
    • 0028355410 scopus 로고
    • A family of cellular proteins related to snake venom disintegrins
    • Weskamp, G., and C.P. Blobel. 1994. A family of cellular proteins related to snake venom disintegrins. Proc. Natl. Acad. Sci. USA. 91:2748-2751.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2748-2751
    • Weskamp, G.1    Blobel, C.P.2
  • 51
    • 0030049705 scopus 로고    scopus 로고
    • MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains
    • Weskamp, G., J.R. Krätzschmar, M. Reid, and C.P. Blobel. 1996. MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains. J. Cell Biol. 132:717-726.
    • (1996) J. Cell Biol. , vol.132 , pp. 717-726
    • Weskamp, G.1    Krätzschmar, J.R.2    Reid, M.3    Blobel, C.P.4
  • 52
    • 0036170534 scopus 로고    scopus 로고
    • Mice lacking the metalloprotease-disintegrin MDC9 (ADAM9) have no evident major abnormalities during development or adult life
    • Weskamp, G., H. Cai, T.A. Brodie, S. Higashyama, K. Manova, T. Ludwig, and C.P. Blobel. 2002. Mice lacking the metalloprotease-disintegrin MDC9 (ADAM9) have no evident major abnormalities during development or adult life. Mol. Cell. Biol. 22:1537-1544.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1537-1544
    • Weskamp, G.1    Cai, H.2    Brodie, T.A.3    Higashyama, S.4    Manova, K.5    Ludwig, T.6    Blobel, C.P.7
  • 53
    • 0024504360 scopus 로고
    • The TGF-α precursor expressed on the cell surface binds to the EGF receptor on adjacent cells, leading to signal transduction
    • Wong, S.T., L.F. Winchell, B.K. McCune, H.S. Earp, J. Teixido, J. Massague, B. Herman, and D.C. Lee. 1989. The TGF-α precursor expressed on the cell surface binds to the EGF receptor on adjacent cells, leading to signal transduction. Cell. 56:495-506.
    • (1989) Cell , vol.56 , pp. 495-506
    • Wong, S.T.1    Winchell, L.F.2    McCune, B.K.3    Earp, H.S.4    Teixido, J.5    Massague, J.6    Herman, B.7    Lee, D.C.8
  • 55
    • 0037157854 scopus 로고    scopus 로고
    • The metalloprotease Kuzbanian (ADAM10) mediates the transactivation of EGF receptor by G protein-coupled receptors
    • Yan, Y., K. Shirakabe, and Z. Werb. 2002. The metalloprotease Kuzbanian (ADAM10) 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
  • 57
    • 0037044786 scopus 로고    scopus 로고
    • Evidence for regulation of the tumor necrosis factor α-convertase (TACE) by protein-tyrosine phosphatase PTPH1
    • Zheng, Y., J. Schlöndorff, and C.P. Blobel. 2002. Evidence for regulation of the tumor necrosis factor α-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    Schlöndorff, J.2    Blobel, C.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.