메뉴 건너뛰기




Volumn 9, Issue 2, 2012, Pages 140-156

α-secretase in Alzheimer's disease and beyond: Mechanistic, regulation and function in the shedding of membrane proteins

Author keywords

Alzheimer; Disintegrin; Metabolism; Metalloprotease; Regulation; Transmembrane proteins

Indexed keywords

ADAM10 ENDOPEPTIDASE; ADAM15 PROTEIN; ADAM9 PROTEIN; ALPHA SECRETASE; BETA SECRETASE 1; EPHRIN; G PROTEIN COUPLED RECEPTOR; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; MEMBRANE PROTEIN; METALLOPROTEINASE; NONSTEROID ANTIINFLAMMATORY AGENT; PRESENILIN; TESTOSTERONE; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME; UNCLASSIFIED DRUG;

EID: 84857704802     PISSN: 15672050     EISSN: 18755828     Source Type: Journal    
DOI: 10.2174/156720512799361646     Document Type: Review
Times cited : (33)

References (219)
  • 1
    • 0026510747 scopus 로고
    • A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
    • Blobel CP, Wolfsberg TG, Turck CW, Myles DG, Primakoff P, White, JM. A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature 256: 248-252 (1992).
    • (1992) Nature , vol.256 , pp. 248-252
    • Blobel, C.P.1    Wolfsberg, T.G.2    Turck, C.W.3    Myles, D.G.4    Primakoff, P.5    White, J.M.6
  • 2
    • 0027431501 scopus 로고
    • The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: Structural, functional, and evolutionary implications
    • Wolfsberg TG, Bazan JF, Blobel CP, Myles DG, Primakoff P, White JM. The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: structural, functional, and evolutionary implications. Proc Natl Acad Sci USA 90: 10783-10787 (1993).
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10783-10787
    • Wolfsberg, T.G.1    Bazan, J.F.2    Blobel, C.P.3    Myles, D.G.4    Primakoff, P.5    White, J.M.6
  • 3
    • 0029995478 scopus 로고    scopus 로고
    • Molecular cloning of MADM: A catalytically active mammalian disintegrinmetalloprotease expressed in various cell types
    • Howard L, Lu X, Mitchell S, Griffiths S, Glynn P. Molecular cloning of MADM: a catalytically active mammalian disintegrinmetalloprotease expressed in various cell types. Biochem J 317: 45-50 (1996).
    • (1996) Biochem J , vol.317 , pp. 45-50
    • Howard, L.1    Lu, X.2    Mitchell, S.3    Griffiths, S.4    Glynn, P.5
  • 4
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumournecrosis factor-α from cells
    • Black RA, Rauch CT, Kozlosky CJ, Peshon JJ, Slack JL, Wolfson MF, et al. A metalloproteinase disintegrin that releases tumournecrosis factor-α from cells. Nature 385: 729-733 (1997).
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.A.1    Rauch, C.T.2    Kozlosky, C.J.3    Peshon, J.J.4    Slack, J.L.5    Wolfson, M.F.6
  • 5
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α
    • Moss ML, Jin SLC, Milla ME, Burkhart W, Carter HL, Chen WJ, et al. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α. Nature 385: 733-736 (1997).
    • (1997) Nature , vol.385 , pp. 733-736
    • Moss, M.L.1    Jin, S.L.C.2    Milla, M.E.3    Burkhart, W.4    Carter, H.L.5    Chen, W.J.6
  • 7
    • 9844253890 scopus 로고    scopus 로고
    • Identification and characterization of a pro-tumor necrosis factor-α-processing enzyme from the ADAM family of zinc metalloproteases
    • Rosendahl MS, Ko SC, Long DL, Brewer MT, Rosenzweig B, Hedl E, et al. Identification and characterization of a pro-tumor necrosis factor-α-processing enzyme from the ADAM family of zinc metalloproteases. J Biol Chem 272: 24588-24593 (1997).
    • (1997) J Biol Chem , vol.272 , pp. 24588-24593
    • Rosendahl, M.S.1    Ko, S.C.2    Long, D.L.3    Brewer, M.T.4    Rosenzweig, B.5    Hedl, E.6
  • 8
    • 18644384411 scopus 로고    scopus 로고
    • Transmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMs
    • Franzke CW, Tasanen K, Schäcke H, Zhou Z, Tryggvason K, Mauch C, et al. Transmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMs. EMBO J 21: 5026-5035 (2002).
    • (2002) EMBO J , vol.21 , pp. 5026-5035
    • Franzke, C.W.1    Tasanen, K.2    Schäcke, H.3    Zhou, Z.4    Tryggvason, K.5    Mauch, C.6
  • 9
    • 0036152681 scopus 로고    scopus 로고
    • Platelet-activating factor receptor and ADAM10 mediate responses to Staphylococcus aureus in epithelial cells
    • Lemjabbar H, Basbaum C. Platelet-activating factor receptor and ADAM10 mediate responses to Staphylococcus aureus in epithelial cells. Nature Med 8: 41-46 (2002).
    • (2002) Nature Med , vol.8 , pp. 41-46
    • Lemjabbar, H.1    Basbaum, C.2
  • 10
    • 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 158: 221-226 (2002).
    • (2002) J Cell Biol , vol.158 , pp. 221-226
    • Yan, Y.1    Shirakabe, K.2    Werb, Z.3
  • 11
    • 2642541715 scopus 로고    scopus 로고
    • Selective roles for tumor necrosis factor α- converting enzyme/ADAM17 in the shedding of the epidermal growth factor receptor ligand family
    • Hinkle CL, Sunnaborg SW, Loiselle D, Parker CE, Stevenson M, Russell WE, et al. Selective roles for tumor necrosis factor α- converting enzyme/ADAM17 in the shedding of the epidermal growth factor receptor ligand family. J Biol Chem 279: 24179-24188 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 24179-24188
    • Hinkle, C.L.1    Sunnaborg, S.W.2    Loiselle, D.3    Parker, C.E.4    Stevenson, M.5    Russell, W.E.6
  • 12
    • 66549086638 scopus 로고    scopus 로고
    • Regulated release and functional modulation of junctional adhesion molecule A by disintegrin metalloproteinases
    • Koenen RR, Pruessmeyer J, Soehnlein O, Fraemohs L, Zernecke A, Schwarz N, et al. Regulated release and functional modulation of junctional adhesion molecule A by disintegrin metalloproteinases. Blood 113: 4799-4809 (2009).
    • (2009) Blood , vol.113 , pp. 4799-4809
    • Koenen, R.R.1    Pruessmeyer, J.2    Soehnlein, O.3    Fraemohs, L.4    Zernecke, A.5    Schwarz, N.6
  • 13
    • 33750807736 scopus 로고    scopus 로고
    • Metalloproteaseinduced ectodomain shedding of neural cell adhesion molecule (NCAM)
    • Hinkle CL, Diestel S, Lieberman J, Maness PF. Metalloproteaseinduced ectodomain shedding of neural cell adhesion molecule (NCAM). J Neurobiol 66: 1378-1395 (2006).
    • (2006) J Neurobiol , vol.66 , pp. 1378-1395
    • Hinkle, C.L.1    Diestel, S.2    Lieberman, J.3    Maness, P.F.4
  • 14
    • 33745477470 scopus 로고    scopus 로고
    • Proteomic identification of desmoglin 2 and activated leukocyte cell adhesion molecule as substrates of ADAM17 and ADAM10 by difference gel electrophoresis
    • Bech-Serra JJ, Santiago-Josefat B, Esselens C, Saftig P, Baselga J, Arribas J, et al. Proteomic identification of desmoglin 2 and activated leukocyte cell adhesion molecule as substrates of ADAM17 and ADAM10 by difference gel electrophoresis. Mol Cell Biol 26: 5086-5095 (2006).
    • (2006) Mol Cell Biol , vol.26 , pp. 5086-5095
    • Bech-Serra, J.J.1    Santiago-Josefat, B.2    Esselens, C.3    Saftig, P.4    Baselga, J.5    Arribas, J.6
  • 16
    • 33846551969 scopus 로고    scopus 로고
    • Metalloproteases regulate T-cell proliferation and effector function via LAG-3
    • Li N, Wang Y, Forbes K, Vignali KM, Heale BS, Saftig P, et al. Metalloproteases regulate T-cell proliferation and effector function via LAG-3. EMBO J 26: 494-504 (2007).
    • (2007) EMBO J , vol.26 , pp. 494-504
    • Li, N.1    Wang, Y.2    Forbes, K.3    Vignali, K.M.4    Heale, B.S.5    Saftig, P.6
  • 18
    • 0035851151 scopus 로고    scopus 로고
    • The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein
    • Vincent B, Paitel E, Saftig P, Frobert Y, Hartmann D, De Strooper B, et al. The disintegrins ADAM10 and TACE contribute to the constitutive and phorbol ester-regulated normal cleavage of the cellular prion protein. J Biol Chem 276: 37743-37746 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 37743-37746
    • Vincent, B.1    Paitel, E.2    Saftig, P.3    Frobert, Y.4    Hartmann, D.5    de Strooper, B.6
  • 19
    • 38349144907 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b
    • Martin L, Fluhrer R, Reiss K, Kremmer E, Saftig, Haass C. Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b. J Biol Chem 283: 1644-1652 (2008).
    • (2008) J Biol Chem , vol.283 , pp. 1644-1652
    • Martin, L.1    Fluhrer, R.2    Reiss, K.3    Kremmer, E.4    Saftig5    Haass, C.6
  • 20
    • 0032540170 scopus 로고    scopus 로고
    • The metallodisintegrin ADAM10 (MADM) from bovine kidney has type IV collagenase activity in vitro
    • Millichip MI, Dallas DJ, Wu E, Dale S, McKie N. The metallodisintegrin ADAM10 (MADM) from bovine kidney has type IV collagenase activity in vitro. Biochem Biophys Res Commun 245: 594-598 (1998).
    • (1998) Biochem Biophys Res Commun , vol.245 , pp. 594-598
    • Millichip, M.I.1    Dallas, D.J.2    Wu, E.3    Dale, S.4    McKie, N.5
  • 21
    • 1442358746 scopus 로고    scopus 로고
    • Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands
    • Sahin U, Weskamp G, Kelly K, Zhou HM, Higashiyama S, Peschon J, et al. Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands. J Cell Biol 164: 769-779 (2004).
    • (2004) J Cell Biol , vol.164 , pp. 769-779
    • Sahin, U.1    Weskamp, G.2    Kelly, K.3    Zhou, H.M.4    Higashiyama, S.5    Peschon, J.6
  • 23
    • 33746331700 scopus 로고    scopus 로고
    • ADAM10-mediated release of complement membrane cofactor protein during apoptosis of epithelial cells
    • Hakulinen J, Keski-Oja J. ADAM10-mediated release of complement membrane cofactor protein during apoptosis of epithelial cells. J Biol Chem 281: 21369-21376 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 21369-21376
    • Hakulinen, J.1    Keski-Oja, J.2
  • 24
    • 34548749917 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-1 promotes liver metastasis by induction of hepatocyte growth factor signaling
    • Kopitz C, Gerg M, Bandapalli OR, Ister D, Pennington CJ, Hauser S, et al. Tissue inhibitor of metalloproteinases-1 promotes liver metastasis by induction of hepatocyte growth factor signaling. Cancer Res 67: 8615-8623 (2007).
    • (2007) Cancer Res , vol.67 , pp. 8615-8623
    • Kopitz, C.1    Gerg, M.2    Bandapalli, O.R.3    Ister, D.4    Pennington, C.J.5    Hauser, S.6
  • 25
    • 33746826046 scopus 로고    scopus 로고
    • Regulated ADAM10-dependent ectodomain shedding of γ- protocadherin C3 modulates cell-cell adhesion
    • Reiss K, Maretzky T, Haas IG, Schulte M, Ludwig A, Frank M, et al. Regulated ADAM10-dependent ectodomain shedding of γ- protocadherin C3 modulates cell-cell adhesion. J Biol Chem 281: 21735-21744 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 21735-21744
    • Reiss, K.1    Maretzky, T.2    Haas, I.G.3    Schulte, M.4    Ludwig, A.5    Frank, M.6
  • 26
    • 27144492960 scopus 로고    scopus 로고
    • Soluble Axl is generated by ADAM10-dependent cleavage and associates with Gas6 in mouse serum
    • Budagian V, Bulanova E, Orinska Z, Duitman E, Brandt K, Ludwig A, et al. Soluble Axl is generated by ADAM10-dependent cleavage and associates with Gas6 in mouse serum. Mol Cell Biol 25: 9324-9339 (2005).
    • (2005) Mol Cell Biol , vol.25 , pp. 9324-9339
    • Budagian, V.1    Bulanova, E.2    Orinska, Z.3    Duitman, E.4    Brandt, K.5    Ludwig, A.6
  • 27
    • 33845994375 scopus 로고    scopus 로고
    • Negative regulation of osteoclastogenesis by ectodomain shedding of receptor activator of NF-κB ligand
    • Hikita A, Yana I, Wakeyama H, Nakamura M, Kadono Y, Oshima Y, et al. Negative regulation of osteoclastogenesis by ectodomain shedding of receptor activator of NF-κB ligand. J Biol Chem 281: 36846-36855 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 36846-36855
    • Hikita, A.1    Yana, I.2    Wakeyama, H.3    Nakamura, M.4    Kadono, Y.5    Oshima, Y.6
  • 28
    • 37549003693 scopus 로고    scopus 로고
    • Cleavage of the human thyrotropin receptor by ADAM10 is regulated by thyrotropin
    • Kaczur V, Puskas LG, Zu N, Rebai A, Miled N, Juhasz F, et al. Cleavage of the human thyrotropin receptor by ADAM10 is regulated by thyrotropin. J Mol Recognit 20: 392-404 (2007).
    • (2007) J Mol Recognit , vol.20 , pp. 392-404
    • Kaczur, V.1    Puskas, L.G.2    Zu, N.3    Rebai, A.4    Miled, N.5    Juhasz, F.6
  • 29
    • 0141704284 scopus 로고    scopus 로고
    • Characterization of the ectodomain shedding of the β-site amyloid precursor protein-cleaving enzyme 1 (BACE1)
    • Hussein I, Hawkins J, Shikotra A, Riddell DR, Faller A, Dingwall C. Characterization of the ectodomain shedding of the β-site amyloid precursor protein-cleaving enzyme 1 (BACE1). J Biol Chem 278: 36264-36268 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 36264-36268
    • Hussein, I.1    Hawkins, J.2    Shikotra, A.3    Riddell, D.R.4    Faller, A.5    Dingwall, C.6
  • 30
    • 0034914811 scopus 로고    scopus 로고
    • The function of leak and kuzbanian during growth cone and cell migration
    • Schimmelpfeng K, Gögel S and Klämbt C. The function of leak and kuzbanian during growth cone and cell migration. Mech Dev 106: 25-36 (2001).
    • (2001) Mech Dev , vol.106 , pp. 25-36
    • Schimmelpfeng, K.1    Gögel, S.2    Klämbt, C.3
  • 31
    • 0034714357 scopus 로고    scopus 로고
    • Regulated cleavage of a contact-mediated axon repellent
    • Hattori M, Osterfield M, Flanagan JG. Regulated cleavage of a contact-mediated axon repellent. Science 289: 1360-1365 (2000).
    • (2000) Science , vol.289 , pp. 1360-1365
    • Hattori, M.1    Osterfield, M.2    Flanagan, J.G.3
  • 32
    • 26844448800 scopus 로고    scopus 로고
    • Adam meets Eph: An ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans
    • Janes PW, Saha N, Barton WA, Kolev MV, Wimmer-Kleikamp SH, Nievergall E, et al. Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans. Cell 123: 291-304 (2005).
    • (2005) Cell , vol.123 , pp. 291-304
    • Janes, P.W.1    Saha, N.2    Barton, W.A.3    Kolev, M.V.4    Wimmer-Kleikamp, S.H.5    Nievergall, E.6
  • 33
    • 0033616716 scopus 로고    scopus 로고
    • Constitutive and regulated α-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease
    • Lammich S, Kojro E, Postina R, Gilbert S, Pfeiffer R, Jasionowski M, et al. Constitutive and regulated α-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease. Proc Natl Acad Sci USA 96: 3922-3927 (1999).
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3922-3927
    • Lammich, S.1    Kojro, E.2    Postina, R.3    Gilbert, S.4    Pfeiffer, R.5    Jasionowski, M.6
  • 34
    • 0343196671 scopus 로고    scopus 로고
    • Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during drosophila and vertebrate neurogenesis
    • Pan D, Rubin GM. Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during drosophila and vertebrate neurogenesis. Cell 90: 271-280 (1997).
    • (1997) Cell , vol.90 , pp. 271-280
    • Pan, D.1    Rubin, G.M.2
  • 35
    • 0032923759 scopus 로고    scopus 로고
    • Processing of the Notch ligand delta by the metalloprotease kuzbanian
    • Qi H, Rand MD, Wu X, Sestan N, Wang W, Rakic P, et al. Processing of the Notch ligand delta by the metalloprotease kuzbanian. Science 283: 91-94 (1999).
    • (1999) Science , vol.283 , pp. 91-94
    • Qi, H.1    Rand, M.D.2    Wu, X.3    Sestan, N.4    Wang, W.5    Rakic, P.6
  • 36
    • 0035969235 scopus 로고    scopus 로고
    • Ectodomain shedding of L1 adhesion molecule promotes cell migration by autocrine binding to integrins
    • Mechtersheimer S, Gutwein P, Agmon-Levin N, Stoeck A, Oleszweski M, Riedle S, et al. Ectodomain shedding of L1 adhesion molecule promotes cell migration by autocrine binding to integrins. J Cell Biol 155: 661-673 (2001).
    • (2001) J Cell Biol , vol.155 , pp. 661-673
    • Mechtersheimer, S.1    Gutwein, P.2    Agmon-Levin, N.3    Stoeck, A.4    Oleszweski, M.5    Riedle, S.6
  • 37
    • 0042237924 scopus 로고    scopus 로고
    • The disintegrin-like metalloprotease ADAM10 is involved in constitutive cleavage of CX3CL1 (fractalkine) and regulates CX3CL1-mediated cell-cell adhesion
    • Hundhausen C, Misztela D, Berkhout TA, Broadway N, Saftig P, Reiss, et al. The disintegrin-like metalloprotease ADAM10 is involved in constitutive cleavage of CX3CL1 (fractalkine) and regulates CX3CL1-mediated cell-cell adhesion. Blood 102: 1186-1195 (2003).
    • (2003) Blood , vol.102 , pp. 1186-1195
    • Hundhausen, C.1    Misztela, D.2    Berkhout, T.A.3    Broadway, N.4    Saftig, P.5    Reiss6
  • 38
    • 59049094283 scopus 로고    scopus 로고
    • Formation of Pmel17 amyloid is regulated by juxtamembrane metalloproteinase cleavage, and the resulting C-terminal fragment is a substrate for γ -secretase
    • Kummer MP, Maruyama H, Huelsmann C, Baches S, Weggen S, Koo EH. Formation of Pmel17 amyloid is regulated by juxtamembrane metalloproteinase cleavage, and the resulting C-terminal fragment is a substrate for γ -secretase. J Biol Chem 284: 2296-2306 (2009).
    • (2009) J Biol Chem , vol.284 , pp. 2296-2306
    • Kummer, M.P.1    Maruyama, H.2    Huelsmann, C.3    Baches, S.4    Weggen, S.5    Koo, E.H.6
  • 39
    • 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 USA 104: 19796-19801 (2007).
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19796-19801
    • Chen, C.D.1    Podvin, S.2    Gillespie, E.3    Leeman, S.E.4    Abraham, C.R.5
  • 40
    • 0141866756 scopus 로고    scopus 로고
    • Cellular cholesterol depletion triggers shedding of the human interleukin-6 receptor by ADAM10 and ADAM17 (TACE)
    • Matthews V, Schuster B, Schütze S, Bussmeyer I, Ludwig A, Hundhausen C, et al. Cellular cholesterol depletion triggers shedding of the human interleukin-6 receptor by ADAM10 and ADAM17 (TACE). J Biol Chem 278: 38829-38839 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 38829-38839
    • Matthews, V.1    Schuster, B.2    Schütze, S.3    Bussmeyer, I.4    Ludwig, A.5    Hundhausen, C.6
  • 41
    • 77954917968 scopus 로고    scopus 로고
    • Activity-dependent α-cleavage of nectin-1 is mediated by a disintegrin and metalloprorease 10 (ADAM10)
    • Kim J, Lilliehook C, Dudak A, Prox J, Saftig P, Federoff HJ, Lim ST. Activity-dependent α-cleavage of nectin-1 is mediated by a disintegrin and metalloprorease 10 (ADAM10). J Biol Chem 285: 22919-22926 (2010).
    • (2010) J Biol Chem , vol.285 , pp. 22919-22926
    • Kim, J.1    Lilliehook, C.2    Dudak, A.3    Prox, J.4    Saftig, P.5    Federoff, H.J.6    Lim, S.T.7
  • 42
    • 2442527640 scopus 로고    scopus 로고
    • The transmembrane CXC-chemokine ligand 16 is induced by IFN-γ and TNFα and shed by the activity of the disintegrin-like metalloproteinase ADAM10
    • Abel S, Hundhausen C, Mentlein R, Schulte A, Berkhout TA, Broadway N, et al. The transmembrane CXC-chemokine ligand 16 is induced by IFN-γ and TNFα and shed by the activity of the disintegrin-like metalloproteinase ADAM10. J Immunol 172: 6362-6372 (2004).
    • (2004) J Immunol , vol.172 , pp. 6362-6372
    • Abel, S.1    Hundhausen, C.2    Mentlein, R.3    Schulte, A.4    Berkhout, T.A.5    Broadway, N.6
  • 43
    • 1542724429 scopus 로고    scopus 로고
    • A disintegrin and metalloproteinase 10-mediated cleavage and shedding regulates the cell surface expression of CXC chemokine ligand 16
    • Gough PJ, Garton KJ, Wille PT, Rychlewski M, Dempsey PJ, Raines EW. A disintegrin and metalloproteinase 10-mediated cleavage and shedding regulates the cell surface expression of CXC chemokine ligand 16. J Immunol 172: 3678-3685 (2004).
    • (2004) J Immunol , vol.172 , pp. 3678-3685
    • Gough, P.J.1    Garton, K.J.2    Wille, P.T.3    Rychlewski, M.4    Dempsey, P.J.5    Raines, E.W.6
  • 44
    • 33646587981 scopus 로고    scopus 로고
    • Furin-, ADAM10-, and γ -secretase-mediated cleavage of a receptor tyrosine phosphatase and regulation of β -catenin's transcriptional activity
    • Anders L, Mertins P, Lammich S, Murgia M, Hartmann D, Saftig P, et al. Furin-, ADAM10-, and γ -secretase-mediated cleavage of a receptor tyrosine phosphatase and regulation of β -catenin's transcriptional activity. Mol Cell Biol 26: 3917-3934 (2006).
    • (2006) Mol Cell Biol , vol.26 , pp. 3917-3934
    • Anders, L.1    Mertins, P.2    Lammich, S.3    Murgia, M.4    Hartmann, D.5    Saftig, P.6
  • 45
    • 15444371289 scopus 로고    scopus 로고
    • ADAM10 cleavage of N-cadherin and regulation of cell-cell and β-catenin nuclear signalling
    • Reiss K, Maretzky T, Ludwig A, Tousseyn T, de Strooper B, Hartmann D, et al. ADAM10 cleavage of N-cadherin and regulation of cell-cell and β-catenin nuclear signalling. EMBO J 24: 742-752 (2005).
    • (2005) EMBO J , vol.24 , pp. 742-752
    • Reiss, K.1    Maretzky, T.2    Ludwig, A.3    Tousseyn, T.4    de Strooper, B.5    Hartmann, D.6
  • 46
    • 21544467772 scopus 로고    scopus 로고
    • ADAM10 mediates E-cadherin shedding and regulates epithelial cell-cell adhesion, migration, and β-catenin translocation
    • Maretzky T, Reiss K, Ludwig A, Buchholz J, Scholz F, Proksch E, et al. ADAM10 mediates E-cadherin shedding and regulates epithelial cell-cell adhesion, migration, and β-catenin translocation. Proc Natl Acad Sci USA 102: 9182-9187 (2005).
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 9182-9187
    • Maretzky, T.1    Reiss, K.2    Ludwig, A.3    Buchholz, J.4    Scholz, F.5    Proksch, E.6
  • 47
    • 45149117638 scopus 로고    scopus 로고
    • ADAM10 regulates endothelial permeability and T-cell transmigration by proteolysis of vascular endothelial cadherin
    • Schulz B, Pruessmeyer J, Maretzky T, Ludwig A, Blobel CP, Saftig, et al. ADAM10 regulates endothelial permeability and T-cell transmigration by proteolysis of vascular endothelial cadherin. Circ Res 102: 1192-1201 (2008).
    • (2008) Circ Res , vol.102 , pp. 1192-1201
    • Schulz, B.1    Pruessmeyer, J.2    Maretzky, T.3    Ludwig, A.4    Blobel, C.P.5    Saftig6
  • 48
    • 33645575688 scopus 로고    scopus 로고
    • Epidermal growth factor-regulated activation of Rac GTPase enhances CD44 cleavage by metalloproteinase disintegrin ADAM10
    • Murai T, Miyauchi T, Yanagida T, Sako Y. Epidermal growth factor-regulated activation of Rac GTPase enhances CD44 cleavage by metalloproteinase disintegrin ADAM10. Biochem J 395: 65-71 (2006).
    • (2006) Biochem J , vol.395 , pp. 65-71
    • Murai, T.1    Miyauchi, T.2    Yanagida, T.3    Sako, Y.4
  • 49
    • 33745765680 scopus 로고    scopus 로고
    • Identification of ADAM10 as a major source of HER2 ectodomain sheddase activity in HER2 overexpressing breast cancer cells
    • Liu PC, Liu X, Li Y, Covington M, Wynn R, Huber R, et al. Identification of ADAM10 as a major source of HER2 ectodomain sheddase activity in HER2 overexpressing breast cancer cells. Cancer Biol Ther 5: 657-664 (2006).
    • (2006) Cancer Biol Ther , vol.5 , pp. 657-664
    • Liu, P.C.1    Liu, X.2    Li, Y.3    Covington, M.4    Wynn, R.5    Huber, R.6
  • 50
    • 54049108485 scopus 로고    scopus 로고
    • A soluble form of the receptor for advanced glycation endproducts (RAGE) is produced by proteolytic cleavage of the membrane-bound form by the sheddase a disintegrin and metalloprotease 10 (ADAM10)
    • Raucci A, Cugusi S, Antonelli A, Barabino SM, Monti L, Bierhaus A, et al. A soluble form of the receptor for advanced glycation endproducts (RAGE) is produced by proteolytic cleavage of the membrane-bound form by the sheddase a disintegrin and metalloprotease 10 (ADAM10). FASEB J 22: 3716-3727 (2008).
    • (2008) FASEB J , vol.22 , pp. 3716-3727
    • Raucci, A.1    Cugusi, S.2    Antonelli, A.3    Barabino, S.M.4    Monti, L.5    Bierhaus, A.6
  • 51
    • 58149101483 scopus 로고    scopus 로고
    • Receptor for advanced end products is subjected to protein ectodomain shedding by metalloproteinases
    • Zhang L, Bukulin M, Kojro E, Roth A, Metz VV, Fahrenholz F, et al. Receptor for advanced end products is subjected to protein ectodomain shedding by metalloproteinases. J Biol Chem 283: 35507-35516 (2008).
    • (2008) J Biol Chem , vol.283 , pp. 35507-35516
    • Zhang, L.1    Bukulin, M.2    Kojro, E.3    Roth, A.4    Metz, V.V.5    Fahrenholz, F.6
  • 52
    • 34247382029 scopus 로고    scopus 로고
    • ADAM10 regulates FasL cell surface expression and modulates FasL-induced cytotoxicity and activation-induced cell death
    • Schulte M, Reiss K, Lettau M, Maretzky T, Ludwig A, Hartmann D et al. ADAM10 regulates FasL cell surface expression and modulates FasL-induced cytotoxicity and activation-induced cell death. Cell Death Differ 14: 1040-1049 (2007).
    • (2007) Cell Death Differ , vol.14 , pp. 1040-1049
    • Schulte, M.1    Reiss, K.2    Lettau, M.3    Maretzky, T.4    Ludwig, A.5    Hartmann, D.6
  • 54
    • 33745086859 scopus 로고    scopus 로고
    • Proteolytic cleavage of the neural cell adhesion molecule by ADAM17/TACE is involved in neurite outgrowth
    • Kalus I, Bormann U, Mzoughi M, Schachner M, Kleene R. Proteolytic cleavage of the neural cell adhesion molecule by ADAM17/TACE is involved in neurite outgrowth. J Neurochem 98: 78-88 (2006).
    • (2006) J Neurochem , vol.98 , pp. 78-88
    • Kalus, I.1    Bormann, U.2    Mzoughi, M.3    Schachner, M.4    Kleene, R.5
  • 55
    • 0034671566 scopus 로고    scopus 로고
    • CD30 shedding from Karpas 299 lymphoma cells is mediated by TNF-α-converting enzyme
    • Hansen HP, Dietrich S, Kisseleva T, Mokros T, Mentlein R, Lange HH, et al. CD30 shedding from Karpas 299 lymphoma cells is mediated by TNF-α-converting enzyme. J Immunol 165: 6703-6709 (2000).
    • (2000) J Immunol , vol.165 , pp. 6703-6709
    • Hansen, H.P.1    Dietrich, S.2    Kisseleva, T.3    Mokros, T.4    Mentlein, R.5    Lange, H.H.6
  • 56
    • 0034640286 scopus 로고    scopus 로고
    • Functional analysis of the domain structure of tumor necrosis factor-α converting enzyme
    • Reddy P, Slack JL, Davis R, Cerretti DP, Kozlosky CJ, Blanton RA, et al. Functional analysis of the domain structure of tumor necrosis factor-α converting enzyme. J Biol Chem 275: 14608-14614 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 14608-14614
    • Reddy, P.1    Slack, J.L.2    Davis, R.3    Cerretti, D.P.4    Kozlosky, C.J.5    Blanton, R.A.6
  • 57
    • 0032846604 scopus 로고    scopus 로고
    • A dominant negative form of TNF-α converting enzyme inhibits ProTNF and TNFRII secretion
    • Solomon KA, Pesti N, Wu G, Newton RC. A dominant negative form of TNF-α converting enzyme inhibits ProTNF and TNFRII secretion. J Immunol 163: 4105-4108 (1999).
    • (1999) J Immunol , vol.163 , pp. 4105-4108
    • Solomon, K.A.1    Pesti, N.2    Wu, G.3    Newton, R.C.4
  • 58
    • 73649109903 scopus 로고    scopus 로고
    • A disintegrin and metalloproteinase 17 (ADAM17) mediates inflammation-induced shedding of syndecan-1 and-4 by lung epithelial cells
    • Pruessmeyer J, Martin C, Hess FM, Schwarz N, Schmidt S, Kogel T, et al. A disintegrin and metalloproteinase 17 (ADAM17) mediates inflammation-induced shedding of syndecan-1 and-4 by lung epithelial cells. J Biol Chem 285: 555-564.
    • J Biol Chem , vol.285 , pp. 555-564
    • Pruessmeyer, J.1    Martin, C.2    Hess, F.M.3    Schwarz, N.4    Schmidt, S.5    Kogel, T.6
  • 59
    • 0033532191 scopus 로고    scopus 로고
    • Evidence for a role of a tumor necrosis factor-α (TNF-α)-converting enzyme-like protease in shedding of TRANCE, a TNF family member involved in osteoclastogenesis and dendritic cell survival
    • Lum L, Wong BR, Josien R, Becherer JD, Erdjument-Bromage, H, Schlöndorff J, et al. Evidence for a role of a tumor necrosis factor-α (TNF-α)-converting enzyme-like protease in shedding of TRANCE, a TNF family member involved in osteoclastogenesis and dendritic cell survival. J Biol Chem 274: 13613-13618 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 13613-13618
    • Lum, L.1    Wong, B.R.2    Josien, R.3    Becherer, J.D.4    Erdjument-Bromage, H.5    Schlöndorff, J.6
  • 61
    • 0037066757 scopus 로고    scopus 로고
    • Tumor necrosis factor-α converting enzyme (TACE) regulates epidermal growth factor receptor ligand availability
    • Sunnarborg SW, Hinkle CL, Stevenson M, Russell WE, Raska CS, Peschon JJ, et al. Tumor necrosis factor-α converting enzyme (TACE) regulates epidermal growth factor receptor ligand availability. J Biol Chem 277: 12838-12845 (2002).
    • (2002) J Biol Chem , vol.277 , pp. 12838-12845
    • Sunnarborg, S.W.1    Hinkle, C.L.2    Stevenson, M.3    Russell, W.E.4    Raska, C.S.5    Peschon, J.J.6
  • 62
    • 33845729910 scopus 로고    scopus 로고
    • Ectodomain shedding of the EGF-receptor ligand epigen is mediated by ADAM17
    • Sahin U, Blobel CP. Ectodomain shedding of the EGF-receptor ligand epigen is mediated by ADAM17. FEBS Lett 581: 41-44 (2007).
    • (2007) FEBS Lett , vol.581 , pp. 41-44
    • Sahin, U.1    Blobel, C.P.2
  • 63
    • 0141509970 scopus 로고    scopus 로고
    • Stimulated shedding of vascular cell adhesion molecule 1 (VCAM-1) is mediated by tumor necrosis factor-α-converting enzyme (ADAM17)
    • Garton KJ, Gough PJ, Philalay J, Wille PT, Blobel CP, Whitehead RH, et al. Stimulated shedding of vascular cell adhesion molecule 1 (VCAM-1) is mediated by tumor necrosis factor-α-converting enzyme (ADAM17). J Biol Chem 278: 37459-37464 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 37459-37464
    • Garton, K.J.1    Gough, P.J.2    Philalay, J.3    Wille, P.T.4    Blobel, C.P.5    Whitehead, R.H.6
  • 64
    • 21244497783 scopus 로고    scopus 로고
    • Nectin-4, a new serological breast cancer marker, is a substrate for tumor necrosis factor-a-converting enzyme (TACE)/ADAM17
    • Fabre-Lafay S, Garrido-Urbani S, Reymond N, Gonçalves A, Dubreuil P and Lopez M. Nectin-4, a new serological breast cancer marker, is a substrate for tumor necrosis factor-a-converting enzyme (TACE)/ADAM17. J Biol Chem 280: 19543-19550 (2005).
    • (2005) J Biol Chem , vol.280 , pp. 19543-19550
    • Fabre-Lafay, S.1    Garrido-Urbani, S.2    Reymond, N.3    Gonçalves, A.4    Dubreuil, P.5    Lopez, M.6
  • 65
    • 33645643886 scopus 로고    scopus 로고
    • Tumor necrosis factor-α-converting enzyme (TACE/ADAM-17) mediates the ectodomain cleavage of intercellular adhesion molecule-1 (ICAM-1)
    • Tsakadze NL, Sithu SD, Sen U, English WR, Murphy G, D'Souza SE. Tumor necrosis factor-α-converting enzyme (TACE/ADAM-17) mediates the ectodomain cleavage of intercellular adhesion molecule-1 (ICAM-1). J Biol Chem 281: 3157-3164 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 3157-3164
    • Tsakadze, N.L.1    Sithu, S.D.2    Sen, U.3    English, W.R.4    Murphy, G.5    D'Souza, S.E.6
  • 66
    • 4944248857 scopus 로고    scopus 로고
    • Tumor necrosis factor-α-converting enzyme (ADAM17) mediates GPIbα shedding from platelets in vitro and in vivo
    • Bergmeier W, Piffath CL, Cheng G, Dole VS, Zhang Y, von Andrian UH, et al. Tumor necrosis factor-α-converting enzyme (ADAM17) mediates GPIbα shedding from platelets in vitro and in vivo. Circ Res 95: 677-683 (2004).
    • (2004) Circ Res , vol.95 , pp. 677-683
    • Bergmeier, W.1    Piffath, C.L.2    Cheng, G.3    Dole, V.S.4    Zhang, Y.5    von Andrian, U.H.6
  • 67
    • 33846850498 scopus 로고    scopus 로고
    • Regulated surface expression and shedding support a dual role for semaphoring 4D in platelet responses to vascular injury
    • Zhu L, Bergmeier W, Wu J, Jiang H, Stalker TJ, Cieslak M, et al. Regulated surface expression and shedding support a dual role for semaphoring 4D in platelet responses to vascular injury. Proc Natl Acad Sci USA 104: 1621-1626 (2007).
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 1621-1626
    • Zhu, L.1    Bergmeier, W.2    Wu, J.3    Jiang, H.4    Stalker, T.J.5    Cieslak, M.6
  • 68
    • 0034533443 scopus 로고    scopus 로고
    • Differential shedding of transmembrane neuregulin isoforms by the tumor necrosis factor-α-converting enzyme
    • Montero JC, Yuste L, Diaz-Rodriguez E, Esparis-Ogando A, Pandiella A. Differential shedding of transmembrane neuregulin isoforms by the tumor necrosis factor-α-converting enzyme. Mol Cell Neurosci 16: 631-648 (2000).
    • (2000) Mol Cell Neurosci , vol.16 , pp. 631-648
    • Montero, J.C.1    Yuste, L.2    Diaz-Rodriguez, E.3    Esparis-Ogando, A.4    Pandiella, A.5
  • 69
    • 22144454605 scopus 로고    scopus 로고
    • Evaluation of the contributions of ADAMs 9, 12, 15, 17, and 19 to heart development and ectodomain shedding of neuregulins β1 and β2
    • Horiuchi K, Zhou HM, Kelly K, Manova K, Blobel CP. Evaluation of the contributions of ADAMs 9, 12, 15, 17, and 19 to heart development and ectodomain shedding of neuregulins β1 and β2. Dev Biol 283: 459-471 (2005).
    • (2005) Dev Biol , vol.283 , pp. 459-471
    • Horiuchi, K.1    Zhou, H.M.2    Kelly, K.3    Manova, K.4    Blobel, C.P.5
  • 70
    • 67649664111 scopus 로고    scopus 로고
    • TACE-mediated ectodomain shedding of the typeI TGF-b receptor downregulates TGF-β signaling
    • Liu C, Xu P, Lamouille S, Xu J, Derynck R. TACE-mediated ectodomain shedding of the typeI TGF-b receptor downregulates TGF-β signaling. Mol Cell 35: 26-36 (2009).
    • (2009) Mol Cell , vol.35 , pp. 26-36
    • Liu, C.1    Xu, P.2    Lamouille, S.3    Xu, J.4    Derynck, R.5
  • 71
    • 0035253355 scopus 로고    scopus 로고
    • TNF-α-converting enzyme cleaves the macrophage colonystimulating factor receptor in macrophages undergoing activation
    • Rovida E, Paccagnini A, Del Rosso M, Peschon JJ, Sbarba PD. TNF-α-converting enzyme cleaves the macrophage colonystimulating factor receptor in macrophages undergoing activation. J Immunol 166: 1583-1589 (2001).
    • (2001) J Immunol , vol.166 , pp. 1583-1589
    • Rovida, E.1    Paccagnini, A.2    Del Rosso, M.3    Peschon, J.J.4    Sbarba, P.D.5
  • 72
    • 38449111957 scopus 로고    scopus 로고
    • Cell surface colony-stimulating factor 1 can be cleaved by TNF-αconverting enzyme or endocytosed in a clathrindependent manner
    • Horiuchi K, Miyamoto T, Takaishi H, Hakozaki A, Kosaki N, Miyauchi Y, et al. Cell surface colony-stimulating factor 1 can be cleaved by TNF-αconverting enzyme or endocytosed in a clathrindependent manner. J Immunol 179: 6715-6724 (2007).
    • (2007) J Immunol , vol.179 , pp. 6715-6724
    • Horiuchi, K.1    Miyamoto, T.2    Takaishi, H.3    Hakozaki, A.4    Kosaki, N.5    Miyauchi, Y.6
  • 73
    • 0035985185 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase phosphorylates tumor necrosis factor α-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 α-converting enzyme at threonine 735: a potential role in regulated shedding. Mol Biol Cell 13: 2031-2044 (2002).
    • (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
  • 74
    • 34247363315 scopus 로고    scopus 로고
    • Different ADAMs have distinct influences on kit ligand processing: Phorbol-ester-stimulated ectodomain shedding of kitl1 by ADAM17 is reduced by ADAM19
    • Kawaguchi N, Horiuchi K, Becherer JD, Toyama Y, Besmer P, Blobel CP. Different ADAMs have distinct influences on kit ligand processing: phorbol-ester-stimulated ectodomain shedding of kitl1 by ADAM17 is reduced by ADAM19. J Cell Sci 120: 943-952 (2007).
    • (2007) J Cell Sci , vol.120 , pp. 943-952
    • Kawaguchi, N.1    Horiuchi, K.2    Becherer, J.D.3    Toyama, Y.4    Besmer, P.5    Blobel, C.P.6
  • 75
    • 0042858460 scopus 로고    scopus 로고
    • Membrane-anchored CD40 is processed by the tumor necrosis factor-α-converting enzyme
    • Contin C, Pitard V, Itai T, Nagata S, Moreau JF, Déchanet-Merville J. Membrane-anchored CD40 is processed by the tumor necrosis factor-α-converting enzyme. J Biol Chem 278: 32801-32809 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 32801-32809
    • Contin, C.1    Pitard, V.2    Itai, T.3    Nagata, S.4    Moreau, J.F.5    Déchanet-Merville, J.6
  • 76
    • 1242317010 scopus 로고    scopus 로고
    • Tumor necrosis factor-α-converting enzyme controls surface expression of c-kit and survival of embryonic stem cell-derived mast cells
    • Cruz AC, Frank BT, Edwards ST, Dazin PF, Peschon JJ, Fang KC. Tumor necrosis factor-α-converting enzyme controls surface expression of c-kit and survival of embryonic stem cell-derived mast cells. J Biol Chem 279: 5612-5620 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 5612-5620
    • Cruz, A.C.1    Frank, B.T.2    Edwards, S.T.3    Dazin, P.F.4    Peschon, J.J.5    Fang, K.C.6
  • 77
    • 4644367922 scopus 로고    scopus 로고
    • Natural soluble interleukin-15Rα is generated by cleavage that involves the tumor necrosis factor-α-converting enzyme (TACE/ADAM17)
    • Budagian V, Bulanova E, Orinska Z, Ludwig A, Rose-John S, Saftig, et al. Natural soluble interleukin-15Rα is generated by cleavage that involves the tumor necrosis factor-α-converting enzyme (TACE/ADAM17). J Biol Chem 279: 40368-40375 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 40368-40375
    • Budagian, V.1    Bulanova, E.2    Orinska, Z.3    Ludwig, A.4    Rose-John, S.5    Saftig6
  • 79
    • 24044444558 scopus 로고    scopus 로고
    • Tumor necrosis factor-α-convertase (ADAM17) mediates regulated ectodomain shedding of the severe-acute respiratory syndrome-coronavirus (SARS-CoV) receptor, angiotensin-converting enzyme-2 (ACE2)
    • Lambert DW, Yarski M, Warner FJ, Thornhill P, Parkin ET, Smith AI, et al. Tumor necrosis factor-α-convertase (ADAM17) mediates regulated ectodomain shedding of the severe-acute respiratory syndrome-coronavirus (SARS-CoV) receptor, angiotensin-converting enzyme-2 (ACE2). J Biol Chem 280: 30113-30119 (2005).
    • (2005) J Biol Chem , vol.280 , pp. 30113-30119
    • Lambert, D.W.1    Yarski, M.2    Warner, F.J.3    Thornhill, P.4    Parkin, E.T.5    Smith, A.I.6
  • 80
    • 33745866965 scopus 로고    scopus 로고
    • Ectodomain shedding of preadipocyte factor 1 (Pref-1) by tumor necrosis factor alpha converting enzyme (TACE) and inhibition of adipocyte differentiation
    • Wang Y, Sul HS. Ectodomain shedding of preadipocyte factor 1 (Pref-1) by tumor necrosis factor alpha converting enzyme (TACE) and inhibition of adipocyte differentiation. Mol Cell Biol 26: 5421-5435 (2006).
    • (2006) Mol Cell Biol , vol.26 , pp. 5421-5435
    • Wang, Y.1    Sul, H.S.2
  • 81
    • 40849119744 scopus 로고    scopus 로고
    • mGluR1/5-dependent long-term depression requires the regulated ectodomain cleavage of neuronal pentraxin NPR by TACE
    • Cho RW, Park JM, Wolff SBE, Xu D, Hopf C, Kim JA, et al. mGluR1/5-dependent long-term depression requires the regulated ectodomain cleavage of neuronal pentraxin NPR by TACE. Neuron 57: 858-871 (2008).
    • (2008) Neuron , vol.57 , pp. 858-871
    • Cho, R.W.1    Park, J.M.2    Wolff, S.B.E.3    Xu, D.4    Hopf, C.5    Kim, J.A.6
  • 82
    • 0242384939 scopus 로고    scopus 로고
    • Phorbol 12-myristate 13-acetate-induced ectodomain shedding and phosphorylation of the human meprinβ metalloprotease
    • Han D, Pischitzis A, Roesmann S, Hansen MK, Leuenberger B, Luginbuehl U, et al. Phorbol 12-myristate 13-acetate-induced ectodomain shedding and phosphorylation of the human meprinβ metalloprotease. J Biol Chem 278: 42829-42839 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 42829-42839
    • Han, D.1    Pischitzis, A.2    Roesmann, S.3    Hansen, M.K.4    Leuenberger, B.5    Luginbuehl, U.6
  • 83
    • 33744813041 scopus 로고    scopus 로고
    • EGFR signaling leads to downregulation of PTP-LAR via TACE-mediated proteolytic processing
    • Ruhe JE, Streit S, Hart S, Ullrich A. EGFR signaling leads to downregulation of PTP-LAR via TACE-mediated proteolytic processing. Cell Signal 18: 1515-1527 (2006).
    • (2006) Cell Signal , vol.18 , pp. 1515-1527
    • Ruhe, J.E.1    Streit, S.2    Hart, S.3    Ullrich, A.4
  • 84
    • 14444272986 scopus 로고    scopus 로고
    • Evidence that tumor necrosis factor α-converting enzyme is involved in regulated α-secretase cleavage of the Alzheimer amyloid protein precursor
    • Buxbaum JD, Liu KN, Luo Y, Slack JL, Stocking KL, Peschon JJ, et al. Evidence that tumor necrosis factor α-converting enzyme is involved in regulated α-secretase cleavage of the Alzheimer amyloid protein precursor. J Biol Chem 273: 27765-27767 (1998).
    • (1998) J Biol Chem , vol.273 , pp. 27765-27767
    • Buxbaum, J.D.1    Liu, K.N.2    Luo, Y.3    Slack, J.L.4    Stocking, K.L.5    Peschon, J.J.6
  • 85
    • 0033868818 scopus 로고    scopus 로고
    • A novel proteolytic cleavage involved in Notch signaling: The role of the disintegrin-metalloprotease TACE
    • Brou C, Logeat F, Gupta N, Bessia C, LeBail O, Doedens JR, et al. A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE. Mol Cell 5: 207-216 (2000).
    • (2000) Mol Cell , vol.5 , pp. 207-216
    • Brou, C.1    Logeat, F.2    Gupta, N.3    Bessia, C.4    Lebail, O.5    Doedens, J.R.6
  • 87
    • 26444448409 scopus 로고    scopus 로고
    • L1 is sequentially processed by two differently activated metalloproteases and presenilin/γ -secretase and regulates neural cell adhesion, cell migration, and neurite outgrowth
    • Maretzky T, Schulte M, Ludwig A, Rose-John S, Blobel CP, Hartmann D, et al. L1 is sequentially processed by two differently activated metalloproteases and presenilin/γ -secretase and regulates neural cell adhesion, cell migration, and neurite outgrowth. Mol Cell Biol 25: 9040-9053 (2005).
    • (2005) Mol Cell Biol , vol.25 , pp. 9040-9053
    • Maretzky, T.1    Schulte, M.2    Ludwig, A.3    Rose-John, S.4    Blobel, C.P.5    Hartmann, D.6
  • 88
    • 0035851124 scopus 로고    scopus 로고
    • Tumor necrosis factor-α-converting enzyme (ADAM17) mediates the cleavage and shedding of fractalkine (CX3CL1)
    • Garton KJ, Gough PJ, Blobel CP, Murphy G, Greaves DR, Dempsey PJ, et al. Tumor necrosis factor-α-converting enzyme (ADAM17) mediates the cleavage and shedding of fractalkine (CX3CL1). J Biol Chem 276: 37993-38001 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 37993-38001
    • Garton, K.J.1    Gough, P.J.2    Blobel, C.P.3    Murphy, G.4    Greaves, D.R.5    Dempsey, P.J.6
  • 89
    • 0035976986 scopus 로고    scopus 로고
    • Tumor necrosis factor-α- converting enzyme mediates the inducible cleavage of fractalkine
    • Tsou CL, Haskell CA, Charo IF. Tumor necrosis factor-α- converting enzyme mediates the inducible cleavage of fractalkine. J Biol Chem 276: 44622-44626 (2001).
    • (2001) J Biol Chem , vol.276 , pp. 44622-44626
    • Tsou, C.L.1    Haskell, C.A.2    Charo, I.F.3
  • 91
    • 0141817915 scopus 로고    scopus 로고
    • The Notch ligands, jagged and delta are sequentially processed by γ-secretase and presenilin/α-secretase and release signaling fragments
    • LaVoie MJ, Selkoe DJ. The Notch ligands, jagged and delta are sequentially processed by γ-secretase and presenilin/α-secretase and release signaling fragments. J Biol Chem 278: 34427-34437 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 34427-34437
    • Lavoie, M.J.1    Selkoe, D.J.2
  • 92
    • 1042278167 scopus 로고    scopus 로고
    • Evidence for a critical role of the tumor necrosis factor α convertase (TACE) in ectodomain shedding of the p75 neurotrophin receptor (p75NTR)
    • Weskamp G, Schlöndorff J, Lum L, Becherer JD, Kim TW, Saftig P, et al. Evidence for a critical role of the tumor necrosis factor α convertase (TACE) in ectodomain shedding of the p75 neurotrophin receptor (p75NTR). J Biol Chem 279: 4241-4249 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 4241-4249
    • Weskamp, G.1    Schlöndorff, J.2    Lum, L.3    Becherer, J.D.4    Kim, T.W.5    Saftig, P.6
  • 93
    • 33645763676 scopus 로고    scopus 로고
    • Tumour necrosis factor α-converting enzyme mediates ectodomain shedding of Vps10p-domain receptor family members
    • Hermey G, Sjogaard SS, Petersen CM, Nykjaer A, Gliemann J. Tumour necrosis factor α-converting enzyme mediates ectodomain shedding of Vps10p-domain receptor family members. Biochem J 395: 285-293 (2006).
    • (2006) Biochem J , vol.395 , pp. 285-293
    • Hermey, G.1    Sjogaard, S.S.2    Petersen, C.M.3    Nykjaer, A.4    Gliemann, J.5
  • 94
    • 0034616385 scopus 로고    scopus 로고
    • Tumor necrosis factor-α-converting enzyme is required for cleavage of erb4/HER4
    • Rio C, Buxbaum JD, Peschon JJ and Corfas G. Tumor necrosis factor-α-converting enzyme is required for cleavage of erb4/HER4. J Biol Chem 275: 10379-10387 (2000).
    • (2000) J Biol Chem , vol.275 , pp. 10379-10387
    • Rio, C.1    Buxbaum, J.D.2    Peschon, J.J.3    Corfas, G.4
  • 95
    • 0034520154 scopus 로고    scopus 로고
    • Tumor necrosis factor-α-converting enzyme (TACE) is a growth hormone binding protein (GHBP) sheddase: The metalloprotease TACE/ADAM17 is critical for (PMA-induced) GH receptor proteolysis and GHBP generation
    • Zhang Y, Jiang J, Black RA, Baumann S, Frank SJ. Tumor necrosis factor-α-converting enzyme (TACE) is a growth hormone binding protein (GHBP) sheddase: the metalloprotease TACE/ADAM17 is critical for (PMA-induced) GH receptor proteolysis and GHBP generation. Endocrinol 141: 4342-4248 (2000).
    • (2000) Endocrinol , vol.141 , pp. 4248-4342
    • Zhang, Y.1    Jiang, J.2    Black, R.A.3    Baumann, S.4    Frank, S.J.5
  • 96
    • 0037474312 scopus 로고    scopus 로고
    • Tumor necrosis factor-α- converting enzyme/ADAM17 mediates MUC1 shedding
    • Thathiah A, Blobel CP, Carson DD. Tumor necrosis factor-α- converting enzyme/ADAM17 mediates MUC1 shedding. J Biol Chem 278: 3386-3394 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 3386-3394
    • Thathiah, A.1    Blobel, C.P.2    Carson, D.D.3
  • 97
    • 85047690140 scopus 로고    scopus 로고
    • A disintegrin-matalloprotease prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model
    • Postina R, Schroeder A, Dewachter I, Bohl J, Schmitt U, Kojro E, et al. A disintegrin-matalloprotease prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model. J Clin Invest 113: 1456-1464 (2004).
    • (2004) J Clin Invest , vol.113 , pp. 1456-1464
    • Postina, R.1    Schroeder, A.2    Dewachter, I.3    Bohl, J.4    Schmitt, U.5    Kojro, E.6
  • 98
    • 77950613181 scopus 로고    scopus 로고
    • The disintegrin/metalloproteinase ADAM10 is essential for the establishment of the brain cortex
    • Jorissen E, Prox J, Bernreuther C, Weber S, Schwanbeck R, Serneels L, et al. The disintegrin/metalloproteinase ADAM10 is essential for the establishment of the brain cortex. J Neurosci 30: 4833-4844 (2010).
    • (2010) J Neurosci , vol.30 , pp. 4833-4844
    • Jorissen, E.1    Prox, J.2    Bernreuther, C.3    Weber, S.4    Schwanbeck, R.5    Serneels, L.6
  • 99
    • 77956392552 scopus 로고    scopus 로고
    • ADAM10 is the physiologically relevant, constitutive α- secretase of the amyloid precursor protein in primary neurons
    • Kuhn PH, Wang H, Dislich B, Colombo A, Zeitschel U, Ellwart JW, et al. ADAM10 is the physiologically relevant, constitutive α- secretase of the amyloid precursor protein in primary neurons. EMBO J 29: 3020-3032 (2010).
    • (2010) EMBO J , vol.29 , pp. 3020-3032
    • Kuhn, P.H.1    Wang, H.2    Dislich, B.3    Colombo, A.4    Zeitschel, U.5    Ellwart, J.W.6
  • 100
    • 58149343356 scopus 로고    scopus 로고
    • Effects of TNFα-converting enzyme inhibition on amyloid β production and APP processing in vitro and in vivo
    • Kim ML, Zhang B, Mills IP, Milla ME, Brunden KR, Lee VMY. Effects of TNFα-converting enzyme inhibition on amyloid β production and APP processing in vitro and in vivo. J Neurosci 28: 12052-12061.
    • J Neurosci , vol.28 , pp. 12052-12061
    • Kim, M.L.1    Zhang, B.2    Mills, I.P.3    Milla, M.E.4    Brunden, K.R.5    Lee, V.M.Y.6
  • 101
    • 0024818172 scopus 로고
    • A novel metalloproteinase associated with brain myelin membranes
    • Chantry A, Gregson NA, Glynn P. A novel metalloproteinase associated with brain myelin membranes. J Biol Chem 264: 21603-21607 (1989).
    • (1989) J Biol Chem , vol.264 , pp. 21603-21607
    • Chantry, A.1    Gregson, N.A.2    Glynn, P.3
  • 102
    • 0029788321 scopus 로고    scopus 로고
    • KUZ, a conserved metalloprotease-disintegrin protein with two roles in drosophila neurogenesis
    • Rooke J, Pan D, Xu T, Rubin GM. KUZ, a conserved metalloprotease-disintegrin protein with two roles in drosophila neurogenesis. Science 273: 1227-1231 (1996).
    • (1996) Science , vol.273 , pp. 1227-1231
    • Rooke, J.1    Pan, D.2    Xu, T.3    Rubin, G.M.4
  • 103
    • 48349085043 scopus 로고    scopus 로고
    • The amyloid precursor protein intracellular domain (AICD) as modulator of gene expression, apoptosis, and cytoskeletal dynamics - Relevance for Alzheimer's disease
    • Müller TM, Meyer HE, Egensperger R, Marcus K. The amyloid precursor protein intracellular domain (AICD) as modulator of gene expression, apoptosis, and cytoskeletal dynamics - Relevance for Alzheimer's disease. Prog Neurobiol 85: 393-406 (2008).
    • (2008) Prog Neurobiol , vol.85 , pp. 393-406
    • Müller, T.M.1    Meyer, H.E.2    Egensperger, R.3    Marcus, K.4
  • 104
    • 67349183264 scopus 로고    scopus 로고
    • Intracellular trafficking of Notch receptors and ligands
    • Brou C. Intracellular trafficking of Notch receptors and ligands. Exp Cell Res 315: 1549-1555 (2008).
    • (2008) Exp Cell Res , vol.315 , pp. 1549-1555
    • Brou, C.1
  • 105
    • 0038610845 scopus 로고    scopus 로고
    • The Notch ligand Delta 1 is sequentially cleaved by an ADAM protease and γ-secretase
    • Six E, Ndiaye D, Laâbi Y, Brou C, Gupta-Rossi N, Israël A, et al. The Notch ligand Delta 1 is sequentially cleaved by an ADAM protease and γ-secretase. Proc Natl Acad Sci USA 100: 7638-7643 (2003).
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7638-7643
    • Six, E.1    Ndiaye, D.2    Laâbi, Y.3    Brou, C.4    Gupta-Rossi, N.5    Israël, A.6
  • 106
    • 1642524321 scopus 로고    scopus 로고
    • Dual mechanisms for shedding of the cellular prion protein
    • Parkin ET, Watt NT, Turner AJ, Hooper NM. Dual mechanisms for shedding of the cellular prion protein. J Biol Chem 279: 11170-11178 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 11170-11178
    • Parkin, E.T.1    Watt, N.T.2    Turner, A.J.3    Hooper, N.M.4
  • 109
    • 72149127389 scopus 로고    scopus 로고
    • The α-secretase-derived N-terminal product of cellular prion protein, N1 displays neuroprotective function, in vitro and in vivo
    • Guillot-Sestier MV, Sunyach C, Druon C, Scarzello S, Checler F. The α-secretase-derived N-terminal product of cellular prion protein, N1 displays neuroprotective function, in vitro and in vivo. J Biol Chem 284: 35973-35986 (2009).
    • (2009) J Biol Chem , vol.284 , pp. 35973-35986
    • Guillot-Sestier, M.V.1    Sunyach, C.2    Druon, C.3    Scarzello, S.4    Checler, F.5
  • 111
    • 0037855771 scopus 로고    scopus 로고
    • Cellular prion protein sensitizes neurons to apoptotic stimuli through Mdm2-regulated and p53- dependent caspase 3-like activation
    • Paitel E, Fahreus R, Checler F. Cellular prion protein sensitizes neurons to apoptotic stimuli through Mdm2-regulated and p53- dependent caspase 3-like activation. J Biol Chem 278: 10061-10066 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 10061-10066
    • Paitel, E.1    Fahreus, R.2    Checler, F.3
  • 112
    • 33645277094 scopus 로고    scopus 로고
    • Metalloproteinase/presenilin1 processing of ephrinB regulates EphB-induced Src phosphorylation and signaling
    • Georgakopoulos A, Litterst C, Ghersi E, Baki L, Xu CJ, Serban G, et al. Metalloproteinase/presenilin1 processing of ephrinB regulates EphB-induced Src phosphorylation and signaling. EMBO J 25: 1242-1252 (2006).
    • (2006) EMBO J , vol.25 , pp. 1242-1252
    • Georgakopoulos, A.1    Litterst, C.2    Ghersi, E.3    Baki, L.4    Xu, C.J.5    Serban, G.6
  • 113
    • 70350536784 scopus 로고    scopus 로고
    • Selective use of ADAM10 and ADAM17 in activation of Notch1 signaling
    • Bozkulak EC, Weinmaster G. Selective use of ADAM10 and ADAM17 in activation of Notch1 signaling. Mol Cell Biol 29: 5679-5695 (2009).
    • (2009) Mol Cell Biol , vol.29 , pp. 5679-5695
    • Bozkulak, E.C.1    Weinmaster, G.2
  • 115
    • 0036796421 scopus 로고    scopus 로고
    • The disintegrin/metalloprotease ADAM10 is essential for Notch signaling but not for α-secretase activity in fibroblasts
    • Hartmann D, De Strooper B, Serneels L, Craessaerts K, Herreman A, Annaert W, et al. The disintegrin/metalloprotease ADAM10 is essential for Notch signaling but not for α-secretase activity in fibroblasts. Hum Mol Genet 11: 1-10 (2002).
    • (2002) Hum Mol Genet , vol.11 , pp. 1-10
    • Hartmann, D.1    de Strooper, B.2    Serneels, L.3    Craessaerts, K.4    Herreman, A.5    Annaert, W.6
  • 117
    • 63649105591 scopus 로고    scopus 로고
    • The good, the bad and the ugly substrates for ADAM10 and ADAM17 in brain pathology, inflammation and cancer
    • Pruessmeyer J, Ludwig A. The good, the bad and the ugly substrates for ADAM10 and ADAM17 in brain pathology, inflammation and cancer. Sem Cell Dev Biol 20: 164-174 (2009).
    • (2009) Sem Cell Dev Biol , vol.20 , pp. 164-174
    • Pruessmeyer, J.1    Ludwig, A.2
  • 118
    • 0036890486 scopus 로고    scopus 로고
    • Alzheimer's and prion diseases: Distinct pathologies, common proteolytic denominators
    • Checler F, Vincent B. Alzheimer's and prion diseases: distinct pathologies, common proteolytic denominators. Trends in Neurosci 25: 616-620 (2002).
    • (2002) Trends in Neurosci , vol.25 , pp. 616-620
    • Checler, F.1    Vincent, B.2
  • 119
    • 37249079599 scopus 로고    scopus 로고
    • The ADAM10 prodomain is a specific inhibitor of ADAM10 proteolytic activity and inhibits cellular shedding events
    • Moss ML, Bomar M, Liu Q, Sage H, Dempsey P, Lenhart P, et al. The ADAM10 prodomain is a specific inhibitor of ADAM10 proteolytic activity and inhibits cellular shedding events. J Biol Chem 282: 35712-35721 (2007).
    • (2007) J Biol Chem , vol.282 , pp. 35712-35721
    • Moss, M.L.1    Bomar, M.2    Liu, Q.3    Sage, H.4    Dempsey, P.5    Lenhart, P.6
  • 121
    • 18844374886 scopus 로고    scopus 로고
    • Chaperone-like properties of the prodomain of TNFα-converting enzyme (TACE) and the functional role of its cysteine switch
    • Leonard JD, Lin F, Milla ME. Chaperone-like properties of the prodomain of TNFα-converting enzyme (TACE) and the functional role of its cysteine switch. Biochem J 387: 797-805 (2005).
    • (2005) Biochem J , vol.387 , pp. 797-805
    • Leonard, J.D.1    Lin, F.2    Milla, M.E.3
  • 122
    • 0035430436 scopus 로고    scopus 로고
    • Regulation of the α-secretase ADAM10 by its prodomain and proprotein convertases
    • Anders A, Gilbert S, Garten W, Postina R, Fahrenholz F. Regulation of the α-secretase ADAM10 by its prodomain and proprotein convertases. FASEB J 15: 1837-1839 (2001).
    • (2001) FASEB J , vol.15 , pp. 1837-1839
    • Anders, A.1    Gilbert, S.2    Garten, W.3    Postina, R.4    Fahrenholz, F.5
  • 123
    • 0242710747 scopus 로고    scopus 로고
    • TACE/ADAM17 maturation and activation of sheddase activity require proprotein convertase activity
    • Srour N, Lebel A, McMahon S, Fournier I, Fugère M, Day R, et al. TACE/ADAM17 maturation and activation of sheddase activity require proprotein convertase activity. FEBS Lett 554: 275-283 (2003).
    • (2003) FEBS Lett , vol.554 , pp. 275-283
    • Srour, N.1    Lebel, A.2    McMahon, S.3    Fournier, I.4    Fugère, M.5    Day, R.6
  • 124
    • 0032692624 scopus 로고    scopus 로고
    • Proprotein convertase activity contributes to the processing of the Alzheimer's β-amyloid precursor protein in human cells: Evidence for a role of the prohormone convertase PC7 in the constitutive α-secretase pathway
    • Lopez-Perez E, Seidah NG and Checler F. Proprotein convertase activity contributes to the processing of the Alzheimer's β-amyloid precursor protein in human cells: evidence for a role of the prohormone convertase PC7 in the constitutive α-secretase pathway. J Neurochem 73: 2056-2062 (1999).
    • (1999) J Neurochem , vol.73 , pp. 2056-2062
    • Lopez-Perez, E.1    Seidah, N.G.2    Checler, F.3
  • 125
    • 0035089318 scopus 로고    scopus 로고
    • Constitutive α-secretase cleavage of the b-amyloid precursor protein in the furin-deficient LoVo cell line: Involvement of the pro-hormone convertase PC7 and the disintegrin metalloprotease ADAM10
    • Lopez-Perez E, Zhang Y, Frank SJ, Creemers J, Seidah N, Checler F. Constitutive α-secretase cleavage of the b-amyloid precursor protein in the furin-deficient LoVo cell line: involvement of the pro-hormone convertase PC7 and the disintegrin metalloprotease ADAM10. J Neurochem 76: 1532-1539 (2001).
    • (2001) J Neurochem , vol.76 , pp. 1532-1539
    • Lopez-Perez, E.1    Zhang, Y.2    Frank, S.J.3    Creemers, J.4    Seidah, N.5    Checler, F.6
  • 126
    • 0029774746 scopus 로고    scopus 로고
    • APMA (4- aminophenylmercuric acetate) activation of stromelysin-1 involves protein interactions in addition to those with cystein-75 in the propeptide
    • Galazka G, Widsor LJ, Birkedal-Hansen H, Engler JA. APMA (4- aminophenylmercuric acetate) activation of stromelysin-1 involves protein interactions in addition to those with cystein-75 in the propeptide. Biochemistry 35: 11221-11227 (1996).
    • (1996) Biochemistry , vol.35 , pp. 11221-11227
    • Galazka, G.1    Widsor, L.J.2    Birkedal-Hansen, H.3    Engler, J.A.4
  • 127
    • 70350528991 scopus 로고    scopus 로고
    • Tetraspanin12 regulates ADAM10- dependent cleavage of amyloid precursor protein
    • Xu D, Sharma C, Hemler ME. Tetraspanin12 regulates ADAM10- dependent cleavage of amyloid precursor protein. FASEB J 23: 3674-3681 (2009).
    • (2009) FASEB J , vol.23 , pp. 3674-3681
    • Xu, D.1    Sharma, C.2    Hemler, M.E.3
  • 128
    • 0036800192 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors: Biological actions and therapeutic opportunities
    • Baker AH, Edwards DR, Murphy G. Metalloproteinase inhibitors: biological actions and therapeutic opportunities. J Cell Sci 115: 3719-3727 (2002).
    • (2002) J Cell Sci , vol.115 , pp. 3719-3727
    • Baker, A.H.1    Edwards, D.R.2    Murphy, G.3
  • 131
    • 0037093362 scopus 로고    scopus 로고
    • Engineering N-terminal domain of tissue inhibitor of metalloproteinase (TIMP)-3 to be a better inhibitor against tumour necrosis factor-α-converting enzyme
    • Lee MH, Verma V, Maskos K, Nath D, Knaüper V, Dodds P, et al. Engineering N-terminal domain of tissue inhibitor of metalloproteinase (TIMP)-3 to be a better inhibitor against tumour necrosis factor-α-converting enzyme. Biochem J 364: 227-234 (2002).
    • (2002) Biochem J , vol.364 , pp. 227-234
    • Lee, M.H.1    Verma, V.2    Maskos, K.3    Nath, D.4    Knaüper, V.5    Dodds, P.6
  • 133
    • 42449131043 scopus 로고    scopus 로고
    • The isolated N-terminal domains of TIMP-1 and TIMP-3 are insufficient for ADAM10 inhibition
    • Rapti M, Atkinson SJ, Lee MH, Trim A, Moss M, Murphy G. The isolated N-terminal domains of TIMP-1 and TIMP-3 are insufficient for ADAM10 inhibition. Biochem J 411: 433-439 (2008).
    • (2008) Biochem J , vol.411 , pp. 433-439
    • Rapti, M.1    Atkinson, S.J.2    Lee, M.H.3    Trim, A.4    Moss, M.5    Murphy, G.6
  • 135
    • 13144256688 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase-9 and inhibition of tumor invasion by the membrane-anchored glycoprotein RECK
    • Takahashi C, Sheng Z, Horan TP, Kitayama H, Maki M, Hitomi K, et al. Regulation of matrix metalloproteinase-9 and inhibition of tumor invasion by the membrane-anchored glycoprotein RECK. Proc Natl Acad Sci USA 95: 13221-13226 (1998).
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 13221-13226
    • Takahashi, C.1    Sheng, Z.2    Horan, T.P.3    Kitayama, H.4    Maki, M.5    Hitomi, K.6
  • 136
    • 44849120587 scopus 로고    scopus 로고
    • Drug insight: Tumor necrosis factor converting enzyme as a pharmacological target for rheumatoid arthritis
    • Moss ML, Sklair-Tavron L, Nudelman R. Drug insight: tumor necrosis factor converting enzyme as a pharmacological target for rheumatoid arthritis. Nat Clin Pract Rheumatol 4: 300-309 (2008).
    • (2008) Nat Clin Pract Rheumatol , vol.4 , pp. 300-309
    • Moss, M.L.1    Sklair-Tavron, L.2    Nudelman, R.3
  • 137
    • 12144291505 scopus 로고    scopus 로고
    • Inhibition of tumor necrosis factor-alphaconverting enzyme by a selective antagonist protects brain from focal ischemic injury in rats
    • Wang X, Feuerstein GZ, Xu L, Wang H, Schumacher WA, Ogletree ML, et al. Inhibition of tumor necrosis factor-alphaconverting enzyme by a selective antagonist protects brain from focal ischemic injury in rats. Mol Pharmacol 65: 890-896 (2004).
    • (2004) Mol Pharmacol , vol.65 , pp. 890-896
    • Wang, X.1    Feuerstein, G.Z.2    Xu, L.3    Wang, H.4    Schumacher, W.A.5    Ogletree, M.L.6
  • 138
    • 39749085844 scopus 로고    scopus 로고
    • TACE/ADAM-17: A component of the epidermal growth factor eceptor axis and a promising target in colorectal cancer
    • Merchant NB, Voskresensky I, Rogers CM, Lafleur B, Dempsey PJ, Graves-Deal R, et al. TACE/ADAM-17: a component of the epidermal growth factor eceptor axis and a promising target in colorectal cancer. Clin Cancer Res 14: 1182-1191 (2008).
    • (2008) Clin Cancer Res , vol.14 , pp. 1182-1191
    • Merchant, N.B.1    Voskresensky, I.2    Rogers, C.M.3    Lafleur, B.4    Dempsey, P.J.5    Graves-Deal, R.6
  • 139
    • 15244349837 scopus 로고    scopus 로고
    • Metalloproteinase inhibitors for the disintegrin-like metalloproteinases ADAM10 and ADAM17 that differentially block constitutive and phorbol ester-inducible shedding of cell surface molecules
    • Ludwig A, Hundhauser C, Lambert MH, Broadway N, Andrews RC, Bickett DM, et al. Metalloproteinase inhibitors for the disintegrin-like metalloproteinases ADAM10 and ADAM17 that differentially block constitutive and phorbol ester-inducible shedding of cell surface molecules. Comb Chem High Throughput Screen 8: 161-171 (2005).
    • (2005) Comb Chem High Throughput Screen , vol.8 , pp. 161-171
    • Ludwig, A.1    Hundhauser, C.2    Lambert, M.H.3    Broadway, N.4    Andrews, R.C.5    Bickett, D.M.6
  • 140
    • 52049111595 scopus 로고    scopus 로고
    • Synergistic inhibition with a dual epidermal growth factor receptor/ HER-2/neu tyrosine kinase inhibitor and a disintegrin and metalloprotease inhibitor
    • Witters L, Scherle P, Friedman S, Caulder E, Newton R, Lipton A. Synergistic inhibition with a dual epidermal growth factor receptor/ HER-2/neu tyrosine kinase inhibitor and a disintegrin and metalloprotease inhibitor. Cancer Res 68: 7083-7089 (2008).
    • (2008) Cancer Res , vol.68 , pp. 7083-7089
    • Witters, L.1    Scherle, P.2    Friedman, S.3    Caulder, E.4    Newton, R.5    Lipton, A.6
  • 141
    • 34250167944 scopus 로고    scopus 로고
    • Selective inhibition of ADAM metalloproteases as a novel approach for modulating ErbB pathways in cancer
    • Fridman JS, Caulder E, Hansbury M, Liu X, Yang G, Wang Q, et al. Selective inhibition of ADAM metalloproteases as a novel approach for modulating ErbB pathways in cancer. Clin Cancer Res 13: 1892-1902 (2007).
    • (2007) Clin Cancer Res , vol.13 , pp. 1892-1902
    • Fridman, J.S.1    Caulder, E.2    Hansbury, M.3    Liu, X.4    Yang, G.5    Wang, Q.6
  • 142
    • 0033215445 scopus 로고    scopus 로고
    • The effect of a metalloproteinase inhibitor (GI5402) on tumor necrosis factor-alpha (TNF-alpha) and TNFalpha receptors during human endotoxemia
    • Dekkers PE, Lauw FN, ten Hove T, te Velde AA, Lumley P, Becherer D, et al. The effect of a metalloproteinase inhibitor (GI5402) on tumor necrosis factor-alpha (TNF-alpha) and TNFalpha receptors during human endotoxemia. Blood 94: 2252-2258 (1999).
    • (1999) Blood , vol.94 , pp. 2252-2258
    • Dekkers, P.E.1    Lauw, F.N.2    ten Hove, T.3    te Velde, A.A.4    Lumley, P.5    Becherer, D.6
  • 143
    • 24644483112 scopus 로고    scopus 로고
    • Genomic structure and functional characterization of the human ADAM10 promoter
    • Prinzen C, Müller U, Endres K, Fahrenholz F, Postina R. Genomic structure and functional characterization of the human ADAM10 promoter. FASEB J 19: 1522-1524 (2005).
    • (2005) FASEB J , vol.19 , pp. 1522-1524
    • Prinzen, C.1    Müller, U.2    Endres, K.3    Fahrenholz, F.4    Postina, R.5
  • 144
    • 67649359888 scopus 로고    scopus 로고
    • Upregulation of the α-secretase ADAM10 by retinoic acid receptors and acitretin
    • Tippmann F, Hundt J, Schneider A, Endres K, Fahrenholz F. Upregulation of the α-secretase ADAM10 by retinoic acid receptors and acitretin. FASEB J 23: 1643-1654 (2009).
    • (2009) FASEB J , vol.23 , pp. 1643-1654
    • Tippmann, F.1    Hundt, J.2    Schneider, A.3    Endres, K.4    Fahrenholz, F.5
  • 145
    • 0032810596 scopus 로고    scopus 로고
    • cDNA cloning of mouse tumor necrosis factor-α-converting enzyme (TACE) and partial analysis of its promoter
    • Mizui Y, Yamazaki K, Sagane K, Tanaka I. cDNA cloning of mouse tumor necrosis factor-α-converting enzyme (TACE) and partial analysis of its promoter. Gene 233: 67-74 (1999).
    • (1999) Gene , vol.233 , pp. 67-74
    • Mizui, Y.1    Yamazaki, K.2    Sagane, K.3    Tanaka, I.4
  • 146
    • 0033178381 scopus 로고    scopus 로고
    • Characterization of the cDNA and gene for mouse tumour necrosis factor α converting enzyme (TACE/ADAM17) and its location to mouse chromosome 12 and human chromosome 2p25
    • Cerretti DP, Poindexter K, Castner BJ, Means G, Copeland NG, Gilbert DJ, et al. Characterization of the cDNA and gene for mouse tumour necrosis factor α converting enzyme (TACE/ADAM17) and its location to mouse chromosome 12 and human chromosome 2p25. Cytokines 11: 541-551 (1999).
    • (1999) Cytokines , vol.11 , pp. 541-551
    • Cerretti, D.P.1    Poindexter, K.2    Castner, B.J.3    Means, G.4    Copeland, N.G.5    Gilbert, D.J.6
  • 147
    • 44849100231 scopus 로고    scopus 로고
    • Increased ADAM17 mRNA expression and activity is associated with atherosclerosis resistance in LDL-recptor deficient mice
    • Holdt LM, Thiery J, Breslow JL, Teupser D. Increased ADAM17 mRNA expression and activity is associated with atherosclerosis resistance in LDL-recptor deficient mice. Arterioscler Thromb Vasc Biol 28: 1097-1103 (2008).
    • (2008) Arterioscler Thromb Vasc Biol , vol.28 , pp. 1097-1103
    • Holdt, L.M.1    Thiery, J.2    Breslow, J.L.3    Teupser, D.4
  • 148
    • 70350456139 scopus 로고    scopus 로고
    • Transcription factor Sp1 induces ADAM17 and contributes to tumor cell invasiveness under hypoxia
    • Szalad A, Katakowski M, Zheng X, Jiang F, Chopp M. Transcription factor Sp1 induces ADAM17 and contributes to tumor cell invasiveness under hypoxia. J Exp Clin Cancer Res 28: 129 (2009).
    • (2009) J Exp Clin Cancer Res , vol.28 , pp. 129
    • Szalad, A.1    Katakowski, M.2    Zheng, X.3    Jiang, F.4    Chopp, M.5
  • 150
    • 0025296205 scopus 로고
    • Processing of Alzheimer β/A4 amyloid precursor protein: Modulation by agents that regulate protein phosphorylation
    • Buxbaum JD, Gandy SE, Cicchetti P, Ehrlich ME, Czernik AJ, Fracasso RP, et al. Processing of Alzheimer β/A4 amyloid precursor protein: modulation by agents that regulate protein phosphorylation. Proc Natl Acad Sci USA 87: 6003-6006 (1990).
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6003-6006
    • Buxbaum, J.D.1    Gandy, S.E.2    Cicchetti, P.3    Ehrlich, M.E.4    Czernik, A.J.5    Fracasso, R.P.6
  • 151
    • 0027487188 scopus 로고
    • Regulation by phorbol esters of amyloid precursor protein release from Swiss 3T3 fibroblasts overexpressing protein kinase Cα
    • Slack BE, Nitsch RM, Livneh E, Kunz GM, Breu J, Eldar H, et al. Regulation by phorbol esters of amyloid precursor protein release from Swiss 3T3 fibroblasts overexpressing protein kinase Cα. J Biol Chem 268: 21097-21101 (1993).
    • (1993) J Biol Chem , vol.268 , pp. 21097-21101
    • Slack, B.E.1    Nitsch, R.M.2    Livneh, E.3    Kunz, G.M.4    Breu, J.5    Eldar, H.6
  • 152
    • 0028965767 scopus 로고
    • Conventional protein kinase C (PKC)-α and novel PKCe{open}, but not, increase the secretion of an N-terminal fragment of Alzheimer's disease amyloid precursor protein from PKC cDNA transfected 3Y1 cells
    • Kinouchi T, Sorimachi H, Maruyama K, Mizuno K, Ohno S, Ishiura S, et al. Conventional protein kinase C (PKC)-α and novel PKCe{open}, but not, increase the secretion of an N-terminal fragment of Alzheimer's disease amyloid precursor protein from PKC cDNA transfected 3Y1 cells. FEBS Lett 364: 203-206 (1995).
    • (1995) FEBS Lett , vol.364 , pp. 203-206
    • Kinouchi, T.1    Sorimachi, H.2    Maruyama, K.3    Mizuno, K.4    Ohno, S.5    Ishiura, S.6
  • 153
    • 0035319002 scopus 로고    scopus 로고
    • Protein kinase Cα and β1 are regulators of α-secretase secretory proteolytic processing of amyloid precursor protein in vivo
    • Roßner S, Mendla K, Schliebs R, Bigl V. Protein kinase Cα and β1 are regulators of α-secretase secretory proteolytic processing of amyloid precursor protein in vivo. Eur J Neurosci 13: 1644-1648 (2001).
    • (2001) Eur J Neurosci , vol.13 , pp. 1644-1648
    • Roßner, S.1    Mendla, K.2    Schliebs, R.3    Bigl, V.4
  • 155
    • 34247115682 scopus 로고    scopus 로고
    • M1 and M3 muscarinic receptors control physiological processing of cellular prion by modulating ADAM17 phosphorylation and acticity
    • Alfa Cissé M, Sunyach C, Slack BE, Fisher A, Vincent B, Checler F. M1 and M3 muscarinic receptors control physiological processing of cellular prion by modulating ADAM17 phosphorylation and acticity. J Neurosci 27: 4083-4092 (2007).
    • (2007) J Neurosci , vol.27 , pp. 4083-4092
    • Alfa Cissé, M.1    Sunyach, C.2    Slack, B.E.3    Fisher, A.4    Vincent, B.5    Checler, F.6
  • 156
    • 0028295848 scopus 로고
    • Cell cycle-dependent regulation of the phosphorylation and metabolism of the Alzheimer amyloid precursor protein
    • Suzuki T, Oishi M, Marshak DR, Czernik AJ, Nairn AC, Greengard P. Cell cycle-dependent regulation of the phosphorylation and metabolism of the Alzheimer amyloid precursor protein. EMBO J 13: 1114-1122 (1994).
    • (1994) EMBO J , vol.13 , pp. 1114-1122
    • Suzuki, T.1    Oishi, M.2    Marshak, D.R.3    Czernik, A.J.4    Nairn, A.C.5    Greengard, P.6
  • 157
    • 0031453010 scopus 로고    scopus 로고
    • Regulation of amyloid precursor protein catabolism involves the mitogen-activated protein kinase signal transduction pathway
    • Mills J, Charest DL, Lam F, Beyreuther K, Ida N, Pelech SL et al. Regulation of amyloid precursor protein catabolism involves the mitogen-activated protein kinase signal transduction pathway. J Neurosci 17: 9415-9422 (1997).
    • (1997) J Neurosci , vol.17 , pp. 9415-9422
    • Mills, J.1    Charest, D.L.2    Lam, F.3    Beyreuther, K.4    Ida, N.5    Pelech, S.L.6
  • 158
    • 0031952526 scopus 로고    scopus 로고
    • Regulation of Alzheimer amyloid precursor protein by the mitogen-activated protein kinase cascade
    • Desdouits-Magnen J, Desdouits F, Takeda S, Syu LJ, Saltiel AR, Buxbaum JD, et al. Regulation of Alzheimer amyloid precursor protein by the mitogen-activated protein kinase cascade. J Neurochem 70: 524-530 (1998).
    • (1998) J Neurochem , vol.70 , pp. 524-530
    • Desdouits-Magnen, J.1    Desdouits, F.2    Takeda, S.3    Syu, L.J.4    Saltiel, A.R.5    Buxbaum, J.D.6
  • 159
    • 0032708232 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase inhibitor wortmannin alters the metabolism of the Alzheimer's amyloid precursor protein
    • Petanceska SS, Gandy SE. The phosphatidylinositol 3-kinase inhibitor wortmannin alters the metabolism of the Alzheimer's amyloid precursor protein. J Neurochem 73: 2316-2320 (1999).
    • (1999) J Neurochem , vol.73 , pp. 2316-2320
    • Petanceska, S.S.1    Gandy, S.E.2
  • 160
    • 0033588068 scopus 로고    scopus 로고
    • Regulated secretion of amyloid precursor protein by TrkA receptor stimulation in rat pheochromocytoma-12 cells is mitogen activated protein kinase sensitive
    • Roßner S, Ueberham U, Schliebs R, Perez-Polo JR, Bigl V. Regulated secretion of amyloid precursor protein by TrkA receptor stimulation in rat pheochromocytoma-12 cells is mitogen activated protein kinase sensitive. Neurosci Lett 271: 97-100 (1999).
    • (1999) Neurosci Lett , vol.271 , pp. 97-100
    • Roßner, S.1    Ueberham, U.2    Schliebs, R.3    Perez-Polo, J.R.4    Bigl, V.5
  • 161
    • 0035879075 scopus 로고    scopus 로고
    • Dishevelled regulates the metabolism of amyloid precursor protein via protein kinase C/mitogen-activated protein kinase and c-jun terminal kinase
    • Mudher A, Chapman S, Richardson J, Asuni A, Gibb G, Pollard C, et al. Dishevelled regulates the metabolism of amyloid precursor protein via protein kinase C/mitogen-activated protein kinase and c-jun terminal kinase. J Neurosci 21: 4987-4995 (2001).
    • (2001) J Neurosci , vol.21 , pp. 4987-4995
    • Mudher, A.1    Chapman, S.2    Richardson, J.3    Asuni, A.4    Gibb, G.5    Pollard, C.6
  • 162
    • 0038187674 scopus 로고    scopus 로고
    • GSK-3α regulates production of Alzheimer's disease amyloid-β peptides
    • Phiel CJ, Wilson CA, Lee VMY, Klein PS. GSK-3α regulates production of Alzheimer's disease amyloid-β peptides. Nature 423: 435-439 (2003).
    • (2003) Nature , vol.423 , pp. 435-439
    • Phiel, C.J.1    Wilson, C.A.2    Lee, V.M.Y.3    Klein, P.S.4
  • 164
    • 0038439081 scopus 로고    scopus 로고
    • Regulation of amyloid precursor protein expression and secretion via activation of ERK1/2 by hepatocyte growth factor in HEK293 cells transfected with APP751
    • Liu F, Su Y, Li B, Ni B. Regulation of amyloid precursor protein expression and secretion via activation of ERK1/2 by hepatocyte growth factor in HEK293 cells transfected with APP751. Exp Cell Res 287: 387-396 (2003).
    • (2003) Exp Cell Res , vol.287 , pp. 387-396
    • Liu, F.1    Su, Y.2    Li, B.3    Ni, B.4
  • 166
    • 33745793612 scopus 로고    scopus 로고
    • Interleukin-1α stimulates nonamyloidogenic pathway by α-secretase (ADAM-10 and ADAM-17) cleavage of APP in human astrocytic cells involving p38 MAP kinase
    • Bandyopadhyay S, Hartley DM, Cahill CM, Lahiri DK, Chattopadhyay N and Rogers JT. Interleukin-1α stimulates nonamyloidogenic pathway by α-secretase (ADAM-10 and ADAM-17) cleavage of APP in human astrocytic cells involving p38 MAP kinase. J Neurosci Res 84: 106-118 (2006).
    • (2006) J Neurosci Res , vol.84 , pp. 106-118
    • Bandyopadhyay, S.1    Hartley, D.M.2    Cahill, C.M.3    Lahiri, D.K.4    Chattopadhyay, N.5    Rogers, J.T.6
  • 167
    • 0029863203 scopus 로고    scopus 로고
    • Metabolism of Alzheimer β-amyloid precursor protein: Regulation by protein kinase A in intact cells and in a cell-free system
    • Xu H, Sweeney D, Greengard P, Gandy SE. Metabolism of Alzheimer β-amyloid precursor protein: regulation by protein kinase A in intact cells and in a cell-free system. Proc Natl Acad Sci 93: 4081-4084 (1996).
    • (1996) Proc Natl Acad Sci , vol.93 , pp. 4081-4084
    • Xu, H.1    Sweeney, D.2    Greengard, P.3    Gandy, S.E.4
  • 168
    • 0029805807 scopus 로고    scopus 로고
    • Protein kinase A phosphorylation of the proteasome: A contribution to the α-secretase pathway in human cells
    • Marambaud P, Wilk S, Checler F. Protein kinase A phosphorylation of the proteasome: a contribution to the α-secretase pathway in human cells. J Neurochem 67: 2616-2619 (1996).
    • (1996) J Neurochem , vol.67 , pp. 2616-2619
    • Marambaud, P.1    Wilk, S.2    Checler, F.3
  • 169
    • 0030035594 scopus 로고    scopus 로고
    • Intracellular cyclic AMP inhibits constitutive and phorbol ester-stimulated cleavage of amyloid precursor protein
    • Efthimiopoulos S, Punj S, Manolopoulos V, Pangalos M, Wang GP, Refolo LM. et al. Intracellular cyclic AMP inhibits constitutive and phorbol ester-stimulated cleavage of amyloid precursor protein. J Neurochem 67: 872-875 (1996).
    • (1996) J Neurochem , vol.67 , pp. 872-875
    • Efthimiopoulos, S.1    Punj, S.2    Manolopoulos, V.3    Pangalos, M.4    Wang, G.P.5    Refolo, L.M.6
  • 170
    • 0033014431 scopus 로고    scopus 로고
    • Effects of protein kinase A inhibitors on the production of Aβ40 and Aβ42 by human cells expressing normal and Alzheimer's disease-linked mutated βAPP and presenilin 1
    • Marambaud P, Ancolio K, Alves da Costa C and Checler F. Effects of protein kinase A inhibitors on the production of Aβ40 and Aβ42 by human cells expressing normal and Alzheimer's disease-linked mutated βAPP and presenilin 1. Brit J Pharmacol 126: 1186-1190 (1999).
    • (1999) Brit J Pharmacol , vol.126 , pp. 1186-1190
    • Marambaud, P.1    Ancolio, K.2    Alves da Costa, C.3    Checler, F.4
  • 171
    • 0033599039 scopus 로고    scopus 로고
    • EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF
    • Prenzel N, Zwick E, Daub H, Leserer M, Abraham R, Wallasch C et al. EGF receptor transactivation by G-protein-coupled receptors requires metalloproteinase cleavage of proHB-EGF. Nature 402: 884-888 (1999).
    • (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
  • 172
    • 33646468634 scopus 로고    scopus 로고
    • Phosphorylation of TNF-α converting enzyme by gastrinreleasing peptide induces amphiregulin release and EGF receptor activation
    • Zhang Q, Thomas SM, Wai Yan Lui V, Xi S, Siegfried JM, Fan H, et al. Phosphorylation of TNF-α converting enzyme by gastrinreleasing peptide induces amphiregulin release and EGF receptor activation. Proc Natl Acad Sci USA 103: 6901-6906 (2006).
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 6901-6906
    • Zhang, Q.1    Thomas, S.M.2    Wai Yan Lui, V.3    Xi, S.4    Siegfried, J.M.5    Fan, H.6
  • 173
    • 33344458827 scopus 로고    scopus 로고
    • M1 receptors play a central role in modulating ADlike pathology in transgenic mice
    • Caccamo A, Oddo S, Billings LM, Green KN, Martinez-Coria H, Fisher A, et al. M1 receptors play a central role in modulating ADlike pathology in transgenic mice. Neuron 49: 671-682 (2006).
    • (2006) Neuron , vol.49 , pp. 671-682
    • Caccamo, A.1    Oddo, S.2    Billings, L.M.3    Green, K.N.4    Martinez-Coria, H.5    Fisher, A.6
  • 174
    • 0037157854 scopus 로고    scopus 로고
    • The metalloprorease Kuzbanian (ADAM10) mediates the transactivation of EGF receptor by Gprotein-coupled receptors
    • Yan Y, Shirakabe K, Werb Z. The metalloprorease Kuzbanian (ADAM10) mediates the transactivation of EGF receptor by Gprotein-coupled receptors. J Cell Biol 158: 221-226 (2002).
    • (2002) J Cell Biol , vol.158 , pp. 221-226
    • Yan, Y.1    Shirakabe, K.2    Werb, Z.3
  • 175
    • 78649757591 scopus 로고    scopus 로고
    • ADAM17 is regulated by a rapid and reversible mechanism that controls access to its catalytic site
    • Le Gall SM, Maretzky T, Issuree PD, Niu XD, Reiss K, Saftig P, et al. ADAM17 is regulated by a rapid and reversible mechanism that controls access to its catalytic site. J Cell Sci 123: 3913-3922 (2010).
    • (2010) J Cell Sci , vol.123 , pp. 3913-3922
    • Le Gall, S.M.1    Maretzky, T.2    Issuree, P.D.3    Niu, X.D.4    Reiss, K.5    Saftig, P.6
  • 177
    • 33847171931 scopus 로고    scopus 로고
    • Synapse-associated protein-97 mediates α-secretase ADAM10 trafficking and promotes its activity
    • Marcello E, Gardoni F, Mauceri D, Romorini S, Jeromin A, Epis R, et al. Synapse-associated protein-97 mediates α-secretase ADAM10 trafficking and promotes its activity. J Neurosci 27: 1682-1691 (2007).
    • (2007) J Neurosci , vol.27 , pp. 1682-1691
    • Marcello, E.1    Gardoni, F.2    Mauceri, D.3    Romorini, S.4    Jeromin, A.5    Epis, R.6
  • 179
    • 4744355650 scopus 로고    scopus 로고
    • ADAM binding protein eve-1 is required for ectodomain shedding of epidermal growth factor receptor ligands
    • Tanaka M, Nanba D, Mori S, Shiba F, Ishiguro H, Yoshino K, et al. ADAM binding protein eve-1 is required for ectodomain shedding of epidermal growth factor receptor ligands. J Biol Chem 279: 41950-41959 (2004).
    • (2004) J Biol Chem , vol.279 , pp. 41950-41959
    • Tanaka, M.1    Nanba, D.2    Mori, S.3    Shiba, F.4    Ishiguro, H.5    Yoshino, K.6
  • 180
    • 0037085256 scopus 로고    scopus 로고
    • Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and src family protein-tyrosine kinases
    • Poghosyan Z, Robbins SM, Houslay MD, Webster A, Murphy G, Edwards DR. Phosphorylation-dependent interactions between ADAM15 cytoplasmic domain and src family protein-tyrosine kinases. J Biol Chem 277: 4999-5007 (2002).
    • (2002) J Biol Chem , vol.277 , pp. 4999-5007
    • Poghosyan, Z.1    Robbins, S.M.2    Houslay, M.D.3    Webster, A.4    Murphy, G.5    Edwards, D.R.6
  • 181
    • 0037044786 scopus 로고    scopus 로고
    • Evidence for regulation of the tumor necrosis factor alpha-convertase (TACE) by protein-tyrosine phosphatase PTPH1
    • Zheng Y, Schlondorff J, Blobel CP. Evidence for regulation of the tumor necrosis factor alpha-convertase (TACE) by protein-tyrosine phosphatase PTPH1. J Biol Chem 277: 42463-42470 (2002).
    • (2002) J Biol Chem , vol.277 , pp. 42463-42470
    • Zheng, Y.1    Schlondorff, J.2    Blobel, C.P.3
  • 182
    • 0242580234 scopus 로고    scopus 로고
    • PACSIN3 binds ADAM12/meltrin α and upregulates ectodomain shedding of heparin-binding epidermal growth factor-like growth factor
    • Mori S, Tanaka M, Nanba D, Nishiwaki E, Ishiguro H, Higashiyama S, et al. PACSIN3 binds ADAM12/meltrin α and upregulates ectodomain shedding of heparin-binding epidermal growth factor-like growth factor. J Biol Chem 278: 46029-46034 (2003).
    • (2003) J Biol Chem , vol.278 , pp. 46029-46034
    • Mori, S.1    Tanaka, M.2    Nanba, D.3    Nishiwaki, E.4    Ishiguro, H.5    Higashiyama, S.6
  • 183
    • 33745628804 scopus 로고    scopus 로고
    • FHL2 interacts with both ADAM-17 and the cytoskeleton and regulates ADAM-17 localization and activity
    • Canault M, Tellier E, Bonardo B, Mas E, Aumailley M, Juhan-Vague I, et al. FHL2 interacts with both ADAM-17 and the cytoskeleton and regulates ADAM-17 localization and activity. J Cell Physiol 208: 363-372 (2006).
    • (2006) J Cell Physiol , vol.208 , pp. 363-372
    • Canault, M.1    Tellier, E.2    Bonardo, B.3    Mas, E.4    Aumailley, M.5    Juhan-Vague, I.6
  • 184
    • 28844433559 scopus 로고    scopus 로고
    • The disintegrin ADAM9 indirectly contributes to the physiological processing of cellular prion by modulating ADAM10 activity
    • Alfa Cissé M, Sunyach C, Lefranc-Jullien S, Postina R, Vincent B, Checler F. The disintegrin ADAM9 indirectly contributes to the physiological processing of cellular prion by modulating ADAM10 activity. J Biol Chem 280: 40624-40631 (2005).
    • (2005) J Biol Chem , vol.280 , pp. 40624-40631
    • Alfa Cissé, M.1    Sunyach, C.2    Lefranc-Jullien, S.3    Postina, R.4    Vincent, B.5    Checler, F.6
  • 185
    • 61349132079 scopus 로고    scopus 로고
    • A disintegrin and metalloprotease (ADAM)- mediated ectodomain shedding of ADAM10
    • Parkin E, Harris B. A disintegrin and metalloprotease (ADAM)- mediated ectodomain shedding of ADAM10. J Neurochem 108: 1464-1479 (2009).
    • (2009) J Neurochem , vol.108 , pp. 1464-1479
    • Parkin, E.1    Harris, B.2
  • 186
    • 69249128689 scopus 로고    scopus 로고
    • Role of ADAMs in the ectodomain shedding and conformational conversion of the prion protein
    • Taylor DR, Parkin ET, Cocklin SL, Ault JR, Ashcroft AE, Turner AJ, et al. Role of ADAMs in the ectodomain shedding and conformational conversion of the prion protein. J Biol Chem 284: 22590-22600 (2009).
    • (2009) J Biol Chem , vol.284 , pp. 22590-22600
    • Taylor, D.R.1    Parkin, E.T.2    Cocklin, S.L.3    Ault, J.R.4    Ashcroft, A.E.5    Turner, A.J.6
  • 187
    • 66449103810 scopus 로고    scopus 로고
    • ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of notch and other proteins, is processed by ADAMS-9, ADAMS-15, and the γ-secretase
    • Tousseyn T, Thathiah A, Jorissen E, Raemaekers T, Konietzko U, Reiss K, et al. ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of notch and other proteins, is processed by ADAMS-9, ADAMS-15, and the γ-secretase. J Biol Chem 284: 11738-11747 (2009).
    • (2009) J Biol Chem , vol.284 , pp. 11738-11747
    • Tousseyn, T.1    Thathiah, A.2    Jorissen, E.3    Raemaekers, T.4    Konietzko, U.5    Reiss, K.6
  • 188
    • 0033569653 scopus 로고    scopus 로고
    • Membrane-anchored metalloprotease MDC9 has an α-secretase activity responsible for processing the amyloid precursor protein
    • Koike H, Tomioka S, Sorimachi H, Saido TC, Maruyama K, Okuyama A, et al. Membrane-anchored metalloprotease MDC9 has an α-secretase activity responsible for processing the amyloid precursor protein. Biochem J 343: 371-375 (1999).
    • (1999) Biochem J , vol.343 , pp. 371-375
    • Koike, H.1    Tomioka, S.2    Sorimachi, H.3    Saido, T.C.4    Maruyama, K.5    Okuyama, A.6
  • 189
  • 191
    • 0029671454 scopus 로고    scopus 로고
    • Cholesterol modulates α-secretase cleavage of amyloid precursor protein
    • Bodovitz S, Klein WL. Cholesterol modulates α-secretase cleavage of amyloid precursor protein. J Biol Chem 271: 4436-4440 (1996).
    • (1996) J Biol Chem , vol.271 , pp. 4436-4440
    • Bodovitz, S.1    Klein, W.L.2
  • 192
    • 0032568843 scopus 로고    scopus 로고
    • Modulation of secreted β-amyloid precursor protein and amyloid β-peptide in brain by cholesterol
    • Howland DS, Trusko SP, Savage MJ, Reaume AG, Lang DM, Hirsch JD, et al. Modulation of secreted β-amyloid precursor protein and amyloid β-peptide in brain by cholesterol. J Biol Chem 273: 16576-16582 (1998).
    • (1998) J Biol Chem , vol.273 , pp. 16576-16582
    • Howland, D.S.1    Trusko, S.P.2    Savage, M.J.3    Reaume, A.G.4    Lang, D.M.5    Hirsch, J.D.6
  • 193
    • 0034214328 scopus 로고    scopus 로고
    • Cholesterol decreases secretion of the secreted form of amyloid precursor protein by interfering with glycosylation in the protein secretory pathway
    • Galbete JL, Rodriguez-Martin T, Peressini E, Modena P, Bianchi R, Forloni G. Cholesterol decreases secretion of the secreted form of amyloid precursor protein by interfering with glycosylation in the protein secretory pathway. Biochem J 348: 307-313 (2000).
    • (2000) Biochem J , vol.348 , pp. 307-313
    • Galbete, J.L.1    Rodriguez-Martin, T.2    Peressini, E.3    Modena, P.4    Bianchi, R.5    Forloni, G.6
  • 194
    • 0035826909 scopus 로고    scopus 로고
    • Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM10
    • Kojro E, Gimpl G, Lammich S, Marz W, Fahrenholz F. Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM10. Proc Natl Acad Sci USA 98: 5815-5820 (2001).
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5815-5820
    • Kojro, E.1    Gimpl, G.2    Lammich, S.3    Marz, W.4    Fahrenholz, F.5
  • 195
    • 0030591669 scopus 로고    scopus 로고
    • Effect of oestrogen during menopause on risk and age at onset of Alzheimer's disease
    • Tang MX, Jacobs D, Stern Y, Marder K, Schofield P, Gurland B, et al. Effect of oestrogen during menopause on risk and age at onset of Alzheimer's disease. Lancet 348: 429-432 (1996).
    • (1996) Lancet , vol.348 , pp. 429-432
    • Tang, M.X.1    Jacobs, D.2    Stern, Y.3    Marder, K.4    Schofield, P.5    Gurland, B.6
  • 196
    • 0027197451 scopus 로고
    • Androgens and aging men
    • Swerdloff RS, Wang C. Androgens and aging men. Exp Gerontol 28: 435-446 (1993).
    • (1993) Exp Gerontol , vol.28 , pp. 435-446
    • Swerdloff, R.S.1    Wang, C.2
  • 199
    • 0037023687 scopus 로고    scopus 로고
    • Estrogen lowers Alzheimer -amyloid generation by stimulating trans-Golgi network vesicle biogenesis
    • Greenfield JP, Leung LW, Cai D, Kaasik K, Gross RS, Rodriguez-Boulan E et al. Estrogen lowers Alzheimer -amyloid generation by stimulating trans-Golgi network vesicle biogenesis. J Biol Chem 277: 12128-12136 (2002).
    • (2002) J Biol Chem , vol.277 , pp. 12128-12136
    • Greenfield, J.P.1    Leung, L.W.2    Cai, D.3    Kaasik, K.4    Gross, R.S.5    Rodriguez-Boulan, E.6
  • 200
    • 0034818022 scopus 로고    scopus 로고
    • Estrogen induces a rapid secretion of amyloid β precursor protein via the mitogen-activated protein kinase pathway
    • Manthey D, Heck S, Engert S, Behl C. Estrogen induces a rapid secretion of amyloid β precursor protein via the mitogen-activated protein kinase pathway. Eur J Biochem 268: 4285-4291 (2001).
    • (2001) Eur J Biochem , vol.268 , pp. 4285-4291
    • Manthey, D.1    Heck, S.2    Engert, S.3    Behl, C.4
  • 201
    • 0034672411 scopus 로고    scopus 로고
    • Testosterone stimulates rapid secretory amyloid precursor protein release from rat hypothalamic cells via the activation of the mitogen-activated protein kinase pathway
    • Goodenough S, Engert S, Behl C. Testosterone stimulates rapid secretory amyloid precursor protein release from rat hypothalamic cells via the activation of the mitogen-activated protein kinase pathway. Neurosci Lett 296: 49-52 (2000).
    • (2000) Neurosci Lett , vol.296 , pp. 49-52
    • Goodenough, S.1    Engert, S.2    Behl, C.3
  • 202
    • 0037200076 scopus 로고    scopus 로고
    • Non-steroidal antiinflammatory drugs stimulate secretion of non-amyloidogenic precursor protein
    • Avramovich Y, Amit T, Youdim MB. Non-steroidal antiinflammatory drugs stimulate secretion of non-amyloidogenic precursor protein. J Biol Chem 277: 31466-31473 (2002).
    • (2002) J Biol Chem , vol.277 , pp. 31466-31473
    • Avramovich, Y.1    Amit, T.2    Youdim, M.B.3
  • 203
    • 0037064135 scopus 로고    scopus 로고
    • Structure-function relationship and role of tumor necrosis factor α-converting enzyme in the down-regulation of L-selectin by non-steroidal antiinflammatory drugs
    • Gomez-Gaviro MV, Gonzalez-Alvaro I, Dominguez-Jimenez C, Peschon JJ, Black RA, Sanchez-Madrid F, et al. Structure-function relationship and role of tumor necrosis factor α-converting enzyme in the down-regulation of L-selectin by non-steroidal antiinflammatory drugs. J Biol Chem 277: 38212-38221 (2002).
    • (2002) J Biol Chem , vol.277 , pp. 38212-38221
    • Gomez-Gaviro, M.V.1    Gonzalez-Alvaro, I.2    Dominguez-Jimenez, C.3    Peschon, J.J.4    Black, R.A.5    Sanchez-Madrid, F.6
  • 206
    • 2942590470 scopus 로고    scopus 로고
    • Amyloid precursor protein metabolism is regulated toward alpha-secretase pathway by Ginkgo biloba extracts
    • Colciaghi F, Borroni B, Zimmermann M, Bellone C, Longhi A, Padovani A, et al. Amyloid precursor protein metabolism is regulated toward alpha-secretase pathway by Ginkgo biloba extracts. Neurobiol Dis 16: 454-460 (2004).
    • (2004) Neurobiol Dis , vol.16 , pp. 454-460
    • Colciaghi, F.1    Borroni, B.2    Zimmermann, M.3    Bellone, C.4    Longhi, A.5    Padovani, A.6
  • 207
    • 33745209915 scopus 로고    scopus 로고
    • ADAM10 activation is required for green tea (-)- epigallocatechin-3-gallate-induced α-secretase cleavage of amyloid precursor protein
    • Obregon DF, Rezai-Zadeh K, Bai Y, Sun N, Hou H, Ehrhart J, et al. ADAM10 activation is required for green tea (-)- epigallocatechin-3-gallate-induced α-secretase cleavage of amyloid precursor protein. J Biol Chem 281: 16419-16427 (2006).
    • (2006) J Biol Chem , vol.281 , pp. 16419-16427
    • Obregon, D.F.1    Rezai-Zadeh, K.2    Bai, Y.3    Sun, N.4    Hou, H.5    Ehrhart, J.6
  • 208
    • 34547661859 scopus 로고    scopus 로고
    • Identification of two herbal compounds with potential cholesterol-lowering activity
    • Zhang Y, Zhang H, Hua S, Ma L, Chen C, Liu X, et al. Identification of two herbal compounds with potential cholesterol-lowering activity. Biochem Pharmacol 74: 940-947 (2007).
    • (2007) Biochem Pharmacol , vol.74 , pp. 940-947
    • Zhang, Y.1    Zhang, H.2    Hua, S.3    Ma, L.4    Chen, C.5    Liu, X.6
  • 209
    • 0029795014 scopus 로고    scopus 로고
    • Poreforming toxins trigger shedding of receptors for interleukin 6 and lipopolysaccaride
    • Walev I, Vollmer P, Palmer M, Bhakdi S, Rose-John S. Poreforming toxins trigger shedding of receptors for interleukin 6 and lipopolysaccaride. Proc Natl Acad Sci USA 93: 7882-7887 (1996).
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7882-7887
    • Walev, I.1    Vollmer, P.2    Palmer, M.3    Bhakdi, S.4    Rose-John, S.5
  • 210
    • 0033664463 scopus 로고    scopus 로고
    • Streptolysin Opermeabilized granulocytes shed L-selectin concomitantly with ceramide generation via neutral sphingomyelinase
    • Walev I, Tappe D, Gulbins E, Bhakdi S. Streptolysin Opermeabilized granulocytes shed L-selectin concomitantly with ceramide generation via neutral sphingomyelinase. J Leukoc Biol 68: 865-872 (2000).
    • (2000) J Leukoc Biol , vol.68 , pp. 865-872
    • Walev, I.1    Tappe, D.2    Gulbins, E.3    Bhakdi, S.4
  • 211
    • 70349094855 scopus 로고    scopus 로고
    • A natural squamosamide derivative FLZ reduces amyloid-β production by increasing nonamyloidogenic AβPP processing
    • Hou Y, Yu YB, Liu G, Luo Y. A natural squamosamide derivative FLZ reduces amyloid-β production by increasing nonamyloidogenic AβPP processing. J Alz Dis 18: 153-165 (2009).
    • (2009) J Alz Dis , vol.18 , pp. 153-165
    • Hou, Y.1    Yu, Y.B.2    Liu, G.3    Luo, Y.4
  • 212
    • 60249088016 scopus 로고    scopus 로고
    • Cryptotanshinone, a compound from Salvia miltiorrhiza modulates amyloid precursor protein metabolism and attenuates β-amyloid deposition through upregulating α-secretase in vivo and in vitro
    • Mei Z, Zhang F, Tao L, Zheng W, Cao Y, Wang Z, et al. Cryptotanshinone, a compound from Salvia miltiorrhiza modulates amyloid precursor protein metabolism and attenuates β-amyloid deposition through upregulating α-secretase in vivo and in vitro. Neurosci Lett 452: 90-95 (2009).
    • (2009) Neurosci Lett , vol.452 , pp. 90-95
    • Mei, Z.1    Zhang, F.2    Tao, L.3    Zheng, W.4    Cao, Y.5    Wang, Z.6
  • 214
    • 0343628678 scopus 로고    scopus 로고
    • Metalloprotease-disintegrin (ADAM) genes are widely and differentially expressed in the adult CNS
    • Karkkainen I, Rybnikova E, Pelto-Huikko M, Huovila AP. Metalloprotease-disintegrin (ADAM) genes are widely and differentially expressed in the adult CNS. Mol Cell Neurosci 15: 547-560 (2000).
    • (2000) Mol Cell Neurosci , vol.15 , pp. 547-560
    • Karkkainen, I.1    Rybnikova, E.2    Pelto-Huikko, M.3    Huovila, A.P.4
  • 215
    • 0033793248 scopus 로고    scopus 로고
    • Coordinated expression of betaamyloid precursor protein and the putative beta-secretase BACE and alpha-secretase ADAM10 in mouse and human brain
    • Marcinkiewicz M, Seidah NG. Coordinated expression of betaamyloid precursor protein and the putative beta-secretase BACE and alpha-secretase ADAM10 in mouse and human brain. J Neurochem 75: 2133-2143 (2000).
    • (2000) J Neurochem , vol.75 , pp. 2133-2143
    • Marcinkiewicz, M.1    Seidah, N.G.2
  • 216
    • 0034961544 scopus 로고    scopus 로고
    • Astrocyte and endothelial cell expression of ADAM17 (TACE) in adult human CNS
    • Goddard DR, Bunning RA, Woodroofe MN. Astrocyte and endothelial cell expression of ADAM17 (TACE) in adult human CNS. Glia 34: 267-271 (2001).
    • (2001) Glia , vol.34 , pp. 267-271
    • Goddard, D.R.1    Bunning, R.A.2    Woodroofe, M.N.3
  • 217
    • 0034741796 scopus 로고    scopus 로고
    • Neuronal localization of the TNFalpha converting enzyme (TACE) in brain tissue and its correlation to amyloid plaques
    • Skovronsky DM, Fath S, Lee VM, Milla ME. Neuronal localization of the TNFalpha converting enzyme (TACE) in brain tissue and its correlation to amyloid plaques. J Neurobiol 49: 40-46 (2001).
    • (2001) J Neurobiol , vol.49 , pp. 40-46
    • Skovronsky, D.M.1    Fath, S.2    Lee, V.M.3    Milla, M.E.4
  • 218
    • 0030664460 scopus 로고    scopus 로고
    • Radiation hybrid mapping of human ADAM10 gene to chromosome 15
    • Yamazaki K, Mizui Y, Tanaka I. Radiation hybrid mapping of human ADAM10 gene to chromosome 15. Genomics 45: 457-459 (1997).
    • (1997) Genomics , vol.45 , pp. 457-459
    • Yamazaki, K.1    Mizui, Y.2    Tanaka, I.3
  • 219
    • 0032533326 scopus 로고    scopus 로고
    • Chromosomal assignment of two ADAM genes, TACE (ADAM17) and MLTNB (ADAM19), to human chromosome 2 and 5, respectively, and of Mltnb to mouse chromosome 11
    • Hirohata S, Seldin MF, Apte SS. Chromosomal assignment of two ADAM genes, TACE (ADAM17) and MLTNB (ADAM19), to human chromosome 2 and 5, respectively, and of Mltnb to mouse chromosome 11. Genomics 54: 178-179 (1998).
    • (1998) Genomics , vol.54 , pp. 178-179
    • Hirohata, S.1    Seldin, M.F.2    Apte, S.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.