메뉴 건너뛰기




Volumn 8, Issue 10, 2013, Pages

Differential Surface Expression of ADAM10 and ADAM17 on Human T Lymphocytes and Tumor Cells

Author keywords

[No Author keywords available]

Indexed keywords

ADAM10 ENDOPEPTIDASE; CALCIUM IONOPHORE; FAS LIGAND; METALLOPROTEINASE; MITOGEN ACTIVATED PROTEIN KINASE; PHORBOL ESTER; PROTEIN ADAM17; PROTEIN KINASE C; UNCLASSIFIED DRUG;

EID: 84885150942     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0076853     Document Type: Article
Times cited : (30)

References (70)
  • 1
    • 52949099119 scopus 로고    scopus 로고
    • The ADAM metalloproteinases
    • doi:10.1016/j.mam.2008.08.001
    • Edwards DR, Handsley MM, Pennington CJ, (2008) The ADAM metalloproteinases. Mol Aspects Med 29: 258-289. doi:10.1016/j.mam.2008.08.001. PubMed: 18762209.
    • (2008) Mol Aspects Med , vol.29 , pp. 258-289
    • Edwards, D.R.1    Handsley, M.M.2    Pennington, C.J.3
  • 2
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha
    • doi:10.1038/385733a0
    • Moss ML, Jin SL, Milla ME, Bickett DM, Burkhart W, et al. (1997) Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha. Nature 385: 733-736. doi:10.1038/385733a0. PubMed: 9034191.
    • (1997) Nature , vol.385 , pp. 733-736
    • Moss, M.L.1    Jin, S.L.2    Milla, M.E.3    Bickett, D.M.4    Burkhart, W.5
  • 3
    • 0031040432 scopus 로고    scopus 로고
    • Structural features and biochemical properties of TNF-alpha converting enzyme (TACE)
    • doi:10.1016/S0165-5728(96)00180-4
    • Moss ML, Jin SL, Becherer JD, Bickett DM, Burkhart W, et al. (1997) Structural features and biochemical properties of TNF-alpha converting enzyme (TACE). J Neuroimmunol 72: 127-129. doi:10.1016/S0165-5728(96)00180-4. PubMed: 9042103.
    • (1997) J Neuroimmunol , vol.72 , pp. 127-129
    • Moss, M.L.1    Jin, S.L.2    Becherer, J.D.3    Bickett, D.M.4    Burkhart, W.5
  • 4
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells
    • doi:10.1038/385729a0
    • Black RA, Rauch CT, Kozlosky CJ, Peschon JJ, Slack JL, et al. (1997) A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. Nature 385: 729-733. doi:10.1038/385729a0. PubMed: 9034190.
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.A.1    Rauch, C.T.2    Kozlosky, C.J.3    Peschon, J.J.4    Slack, J.L.5
  • 5
    • 79960923986 scopus 로고    scopus 로고
    • ADAM17: a molecular switch to control inflammation and tissue regeneration
    • doi:10.1016/j.it.2011.05.005
    • Scheller J, Chalaris A, Garbers C, Rose-John S, (2011) ADAM17: a molecular switch to control inflammation and tissue regeneration. Trends Immunol 32: 380-387. doi:10.1016/j.it.2011.05.005. PubMed: 21752713.
    • (2011) Trends Immunol , vol.32 , pp. 380-387
    • Scheller, J.1    Chalaris, A.2    Garbers, C.3    Rose-John, S.4
  • 6
    • 79955470772 scopus 로고    scopus 로고
    • The "A Disintegrin And Metalloproteases" ADAM10 and ADAM17: novel drug targets with therapeutic potential?
    • doi:10.1016/j.ejcb.2010.11.005
    • Saftig P, Reiss K, (2011) The "A Disintegrin And Metalloproteases" ADAM10 and ADAM17: novel drug targets with therapeutic potential? Eur J Cell Biol 90: 527-535. doi:10.1016/j.ejcb.2010.11.005. PubMed: 21194787.
    • (2011) Eur J Cell Biol , vol.90 , pp. 527-535
    • Saftig, P.1    Reiss, K.2
  • 7
    • 70350536784 scopus 로고    scopus 로고
    • Selective use of ADAM10 and ADAM17 in activation of Notch1 signaling
    • doi:10.1128/MCB.00406-09
    • Bozkulak EC, Weinmaster G, (2009) Selective use of ADAM10 and ADAM17 in activation of Notch1 signaling. Mol Cell Biol 29: 5679-5695. doi:10.1128/MCB.00406-09. PubMed: 19704010.
    • (2009) Mol Cell Biol , vol.29 , pp. 5679-5695
    • Bozkulak, E.C.1    Weinmaster, G.2
  • 8
    • 77949528417 scopus 로고    scopus 로고
    • ADAM10 is essential for Notch2-dependent marginal zone B cell development and CD23 cleavage in vivo
    • doi:10.1084/jem.20091990
    • Gibb DR, El SM, Kang DJ, Rowe WJ, El SR, et al. (2010) ADAM10 is essential for Notch2-dependent marginal zone B cell development and CD23 cleavage in vivo. J Exp Med 207: 623-635. doi:10.1084/jem.20091990. PubMed: 20156974.
    • (2010) J Exp Med , vol.207 , pp. 623-635
    • Gibb, D.R.1    El, S.M.2    Kang, D.J.3    Rowe, W.J.4    El, S.R.5
  • 9
    • 53749096966 scopus 로고    scopus 로고
    • ADAM10 is essential for proteolytic activation of Notch during thymocyte development
    • doi:10.1093/intimm/dxn076
    • Tian L, Wu X, Chi C, Han M, Xu T, et al. (2008) ADAM10 is essential for proteolytic activation of Notch during thymocyte development. Int Immunol 20: 1181-1187. doi:10.1093/intimm/dxn076. PubMed: 18635581.
    • (2008) Int Immunol , vol.20 , pp. 1181-1187
    • Tian, L.1    Wu, X.2    Chi, C.3    Han, M.4    Xu, T.5
  • 10
    • 71449113533 scopus 로고    scopus 로고
    • Metalloprotease ADAM10 is required for Notch1 site 2 cleavage
    • doi:10.1074/jbc.M109.006775
    • van Tetering G, van Diest P, Verlaan I, van der Wall E, Kopan R, Vooijs Mvan TG, van DP, Verlaan I, van der WE, Kopan R,et al (2009) Metalloprotease ADAM10 is required for Notch1 site 2 cleavage. J Biol Chem 284: 31018-31027. doi:10.1074/jbc.M109.006775. PubMed: 19726682.
    • (2009) J Biol Chem , vol.284 , pp. 31018-31027
    • van Tetering, G.1    van Diest, P.2    Verlaan, I.3    van der Wall, E.4    Kopan, R.5    Vooijs Mvan, T.G.6
  • 11
    • 78751520783 scopus 로고    scopus 로고
    • The disintegrin/metalloproteinase Adam10 is essential for epidermal integrity and Notch-mediated signaling
    • doi:10.1242/dev.055210
    • Weber S, Niessen MT, Prox J, Lüllmann-Rauch R, Schmitz A, et al. (2011) The disintegrin/metalloproteinase Adam10 is essential for epidermal integrity and Notch-mediated signaling. Development 138: 495-505. doi:10.1242/dev.055210. PubMed: 21205794.
    • (2011) Development , vol.138 , pp. 495-505
    • Weber, S.1    Niessen, M.T.2    Prox, J.3    Lüllmann-Rauch, R.4    Schmitz, A.5
  • 12
    • 79952559441 scopus 로고    scopus 로고
    • Adam10 is essential for early embryonic cardiovascular development
    • doi:10.1002/dvdy.22391
    • Zhang C, Tian L, Chi C, Wu X, Yang X, et al. (2010) Adam10 is essential for early embryonic cardiovascular development. Dev Dyn 239: 2594-2602. doi:10.1002/dvdy.22391. PubMed: 20803506.
    • (2010) Dev Dyn , vol.239 , pp. 2594-2602
    • Zhang, C.1    Tian, L.2    Chi, C.3    Wu, X.4    Yang, X.5
  • 13
    • 34247382029 scopus 로고    scopus 로고
    • ADAM10 regulates FasL cell surface expression and modulates FasL-induced cytotoxicity and activation-induced cell death
    • 17290285
    • Schulte M, Reiss K, Lettau M, Maretzky T, Ludwig A, et al. (2007) ADAM10 regulates FasL cell surface expression and modulates FasL-induced cytotoxicity and activation-induced cell death. Cell Death Differ 14: 1040-1049. PubMed: 17290285.
    • (2007) Cell Death Differ , vol.14 , pp. 1040-1049
    • Schulte, M.1    Reiss, K.2    Lettau, M.3    Maretzky, T.4    Ludwig, A.5
  • 14
    • 34548040200 scopus 로고    scopus 로고
    • The Fas ligand intracellular domain is released by ADAM10 and SPPL2a cleavage in T-cells
    • doi:10.1038/sj.cdd.4402175
    • Kirkin V, Cahuzac N, Guardiola-Serrano F, Huault S, Lückerath K, et al. (2007) The Fas ligand intracellular domain is released by ADAM10 and SPPL2a cleavage in T-cells. Cell Death Differ 14: 1678-1687. doi:10.1038/sj.cdd.4402175. PubMed: 17557115.
    • (2007) Cell Death Differ , vol.14 , pp. 1678-1687
    • Kirkin, V.1    Cahuzac, N.2    Guardiola-Serrano, F.3    Huault, S.4    Lückerath, K.5
  • 15
    • 68949216147 scopus 로고    scopus 로고
    • Posttranslational regulation of Fas ligand function
    • doi:10.1186/1478-811X-6-11
    • Voss M, Lettau M, Paulsen M, Janssen O, (2008) Posttranslational regulation of Fas ligand function. Cell Commun Signal 6: 11. doi:10.1186/1478-811X-6-11. PubMed: 19114018.
    • (2008) Cell Commun Signal , vol.6 , pp. 11
    • Voss, M.1    Lettau, M.2    Paulsen, M.3    Janssen, O.4
  • 16
    • 79953742967 scopus 로고    scopus 로고
    • Pro- and anti-apoptotic CD95 signaling in T cells
    • doi:10.1186/1478-811X-9-7
    • Paulsen M, Janssen O, (2011) Pro- and anti-apoptotic CD95 signaling in T cells. Cell Commun Signal 9: 7. doi:10.1186/1478-811X-9-7. PubMed: 21477291.
    • (2011) Cell Commun Signal , vol.9 , pp. 7
    • Paulsen, M.1    Janssen, O.2
  • 17
    • 79955467862 scopus 로고    scopus 로고
    • Insights into the molecular regulation of FasL (CD178) biology
    • doi:10.1016/j.ejcb.2010.10.006
    • Lettau M, Paulsen M, Schmidt H, Janssen O, (2011) Insights into the molecular regulation of FasL (CD178) biology. Eur J Cell Biol 90: 456-466. doi:10.1016/j.ejcb.2010.10.006. PubMed: 21126798.
    • (2011) Eur J Cell Biol , vol.90 , pp. 456-466
    • Lettau, M.1    Paulsen, M.2    Schmidt, H.3    Janssen, O.4
  • 18
    • 38349144907 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b
    • 17965014
    • Martin L, Fluhrer R, Reiss K, Kremmer E, Saftig P, et al. (2008) Regulated intramembrane proteolysis of Bri2 (Itm2b) by ADAM10 and SPPL2a/SPPL2b. J Biol Chem 283: 1644-1652. PubMed: 17965014.
    • (2008) J Biol Chem , vol.283 , pp. 1644-1652
    • Martin, L.1    Fluhrer, R.2    Reiss, K.3    Kremmer, E.4    Saftig, P.5
  • 19
    • 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 gamma-secretase
    • 19213735
    • Tousseyn T, Thathiah A, Jorissen E, Raemaekers T, Konietzko U, et al. (2009) ADAM10, the rate-limiting protease of regulated intramembrane proteolysis of Notch and other proteins, is processed by ADAMS-9, ADAMS-15, and the gamma-secretase. J Biol Chem 284: 11738-11747. PubMed: 19213735.
    • (2009) J Biol Chem , vol.284 , pp. 11738-11747
    • Tousseyn, T.1    Thathiah, A.2    Jorissen, E.3    Raemaekers, T.4    Konietzko, U.5
  • 20
    • 64149096375 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis--a story about sheddases and I-CliPs
    • doi:10.1016/j.semcdb.2009.03.005
    • Annaert WG, Saftig P, (2009) Regulated intramembrane proteolysis--a story about sheddases and I-CliPs. Semin Cell Dev Biol 20: 125. doi:10.1016/j.semcdb.2009.03.005. PubMed: 19429493.
    • (2009) Semin Cell Dev Biol , vol.20 , pp. 125
    • Annaert, W.G.1    Saftig, P.2
  • 21
    • 0033535504 scopus 로고    scopus 로고
    • A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain
    • doi:10.1038/19083
    • de Strooper B, Annaert W, Cupers P, Saftig P, Craessaerts K, et al. (1999) A presenilin-1-dependent gamma-secretase-like protease mediates release of Notch intracellular domain. Nature 398: 518-522. doi:10.1038/19083. PubMed: 10206645.
    • (1999) Nature , vol.398 , pp. 518-522
    • de Strooper, B.1    Annaert, W.2    Cupers, P.3    Saftig, P.4    Craessaerts, K.5
  • 22
    • 0038610845 scopus 로고    scopus 로고
    • The Notch ligand Delta1 is sequentially cleaved by an ADAM protease and gamma-secretase
    • doi:10.1073/pnas.1230693100
    • Six E, Ndiaye D, Laabi Y, Brou C, Gupta-Rossi N, et al. (2003) The Notch ligand Delta1 is sequentially cleaved by an ADAM protease and gamma-secretase. Proc Natl Acad Sci U S A 100: 7638-7643. doi:10.1073/pnas.1230693100. PubMed: 12794186.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 7638-7643
    • Six, E.1    Ndiaye, D.2    Laabi, Y.3    Brou, C.4    Gupta-Rossi, N.5
  • 23
    • 33746618450 scopus 로고    scopus 로고
    • SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 production
    • doi:10.1038/ncb1440
    • Friedmann E, Hauben E, Maylandt K, Schleeger S, Vreugde S, et al. (2006) SPPL2a and SPPL2b promote intramembrane proteolysis of TNFalpha in activated dendritic cells to trigger IL-12 production. Nat Cell Biol 8: 843-848. doi:10.1038/ncb1440. PubMed: 16829952.
    • (2006) Nat Cell Biol , vol.8 , pp. 843-848
    • Friedmann, E.1    Hauben, E.2    Maylandt, K.3    Schleeger, S.4    Vreugde, S.5
  • 24
    • 35649020520 scopus 로고    scopus 로고
    • The shedding activity of ADAM17 is sequestered in lipid rafts
    • doi:10.1016/j.yexcr.2006.08.027
    • Tellier E, Canault M, Rebsomen L, Bonardo B, Juhan-Vague I, et al. (2006) The shedding activity of ADAM17 is sequestered in lipid rafts. Exp Cell Res 312: 3969-3980. doi:10.1016/j.yexcr.2006.08.027. PubMed: 17010968.
    • (2006) Exp Cell Res , vol.312 , pp. 3969-3980
    • Tellier, E.1    Canault, M.2    Rebsomen, L.3    Bonardo, B.4    Juhan-Vague, I.5
  • 25
    • 78649583249 scopus 로고    scopus 로고
    • Ectodomain shedding of the Notch ligand Jagged1 is mediated by ADAM17, but is not a lipid-raft-associated event
    • doi:10.1042/BJ20100321
    • Parr-Sturgess CA, Rushton DJ, Parkin ET, (2010) Ectodomain shedding of the Notch ligand Jagged1 is mediated by ADAM17, but is not a lipid-raft-associated event. Biochem J 432: 283-294. doi:10.1042/BJ20100321. PubMed: 20819075.
    • (2010) Biochem J , vol.432 , pp. 283-294
    • Parr-Sturgess, C.A.1    Rushton, D.J.2    Parkin, E.T.3
  • 26
    • 33645829585 scopus 로고    scopus 로고
    • The adaptor protein Nck interacts with Fas ligand: Guiding the death factor to the cytotoxic immunological synapse
    • doi:10.1073/pnas.0508562103
    • Lettau M, Qian J, Linkermann A, Latreille M, Larose L, et al. (2006) The adaptor protein Nck interacts with Fas ligand: Guiding the death factor to the cytotoxic immunological synapse. Proc Natl Acad Sci U S A 103: 5911-5916. doi:10.1073/pnas.0508562103. PubMed: 16595635.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 5911-5916
    • Lettau, M.1    Qian, J.2    Linkermann, A.3    Latreille, M.4    Larose, L.5
  • 27
    • 0038459055 scopus 로고    scopus 로고
    • A comprehensive characterization of pancreatic ductal carcinoma cell lines: towards the establishment of an in vitro research platform
    • 12692724
    • Sipos B, Möser S, Kalthoff H, Török V, Löhr M, et al. (2003) A comprehensive characterization of pancreatic ductal carcinoma cell lines: towards the establishment of an in vitro research platform. Virchows Arch 442: 444-452. PubMed: 12692724.
    • (2003) Virchows Arch , vol.442 , pp. 444-452
    • Sipos, B.1    Möser, S.2    Kalthoff, H.3    Török, V.4    Löhr, M.5
  • 28
    • 79960954632 scopus 로고    scopus 로고
    • Development of sandwich ELISA for detection and quantification of human and murine a disintegrin and metalloproteinase17
    • doi:10.1016/j.jim.2011.06.015
    • Trad A, Hedemann N, Shomali M, Pawlak V, Grötzinger J, et al. (2011) Development of sandwich ELISA for detection and quantification of human and murine a disintegrin and metalloproteinase17. J Immunol Methods 371: 91-96. doi:10.1016/j.jim.2011.06.015. PubMed: 21726562.
    • (2011) J Immunol Methods , vol.371 , pp. 91-96
    • Trad, A.1    Hedemann, N.2    Shomali, M.3    Pawlak, V.4    Grötzinger, J.5
  • 29
    • 1442358746 scopus 로고    scopus 로고
    • Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands
    • doi:10.1083/jcb.200307137
    • Sahin U, Weskamp G, Kelly K, Zhou HM, Higashiyama S, et al. (2004) Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands. J Cell Biol 164: 769-779. doi:10.1083/jcb.200307137. PubMed: 14993236.
    • (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
  • 30
    • 12544257436 scopus 로고    scopus 로고
    • ADAM10 mediates ectodomain shedding of the betacellulin precursor activated by p-aminophenylmercuric acetate and extracellular calcium influx
    • 15507448
    • Sanderson MP, Erickson SN, Gough PJ, Garton KJ, Wille PT, et al. (2005) ADAM10 mediates ectodomain shedding of the betacellulin precursor activated by p-aminophenylmercuric acetate and extracellular calcium influx. J Biol Chem 280: 1826-1837. PubMed: 15507448.
    • (2005) J Biol Chem , vol.280 , pp. 1826-1837
    • Sanderson, M.P.1    Erickson, S.N.2    Gough, P.J.3    Garton, K.J.4    Wille, P.T.5
  • 31
    • 12144251368 scopus 로고    scopus 로고
    • Activation-dependent FasL expression in T lymphocytes and Natural Killer cells
    • doi:10.1002/sita.200400037
    • Lettau M, Qian J, Kabelitz D, Janssen O, (2004) Activation-dependent FasL expression in T lymphocytes and Natural Killer cells. Signal Transduct 4: 206-211. doi:10.1002/sita.200400037.
    • (2004) Signal Transduct , vol.4 , pp. 206-211
    • Lettau, M.1    Qian, J.2    Kabelitz, D.3    Janssen, O.4
  • 32
    • 33845781550 scopus 로고    scopus 로고
    • Secretory lysosomes and their cargo in T and NK cells
    • doi:10.1016/j.imlet.2006.10.001
    • Lettau M, Schmidt H, Kabelitz D, Janssen O, (2007) Secretory lysosomes and their cargo in T and NK cells. Immunol Lett 108: 10-19. doi:10.1016/j.imlet.2006.10.001. PubMed: 17097742.
    • (2007) Immunol Lett , vol.108 , pp. 10-19
    • Lettau, M.1    Schmidt, H.2    Kabelitz, D.3    Janssen, O.4
  • 33
    • 31544437691 scopus 로고    scopus 로고
    • A role for exosomes in the constitutive and stimulus-induced ectodomain cleavage of L1 and CD44
    • doi:10.1042/BJ20051013
    • Stoeck A, Keller S, Riedle S, Sanderson MP, Runz S, et al. (2006) A role for exosomes in the constitutive and stimulus-induced ectodomain cleavage of L1 and CD44. Biochem J 393: 609-618. doi:10.1042/BJ20051013. PubMed: 16229685.
    • (2006) Biochem J , vol.393 , pp. 609-618
    • Stoeck, A.1    Keller, S.2    Riedle, S.3    Sanderson, M.P.4    Runz, S.5
  • 34
    • 3042554386 scopus 로고    scopus 로고
    • Cell-matrix interaction via CD44 is independently regulated by different metalloproteinases activated in response to extracellular Ca(2+) influx and PKC activation
    • doi:10.1083/jcb.200310024
    • Nagano O, Murakami D, Hartmann D, De SB, Saftig P, et al. (2004) Cell-matrix interaction via CD44 is independently regulated by different metalloproteinases activated in response to extracellular Ca(2+) influx and PKC activation. J Cell Biol 165: 893-902. doi:10.1083/jcb.200310024. PubMed: 15197174.
    • (2004) J Cell Biol , vol.165 , pp. 893-902
    • Nagano, O.1    Murakami, D.2    Hartmann, D.3    De, S.B.4    Saftig, P.5
  • 35
    • 33846056925 scopus 로고    scopus 로고
    • Substrate selectivity of epidermal growth factor-receptor ligand sheddases and their regulation by phorbol esters and calcium influx
    • 17079736
    • Horiuchi K, Le GS, Schulte M, Yamaguchi T, Reiss K, et al. (2007) Substrate selectivity of epidermal growth factor-receptor ligand sheddases and their regulation by phorbol esters and calcium influx. Mol Cell Biol 18: 176-188. PubMed: 17079736.
    • (2007) Mol Cell Biol , vol.18 , pp. 176-188
    • Horiuchi, K.1    Le, G.S.2    Schulte, M.3    Yamaguchi, T.4    Reiss, K.5
  • 36
    • 84866286420 scopus 로고    scopus 로고
    • Role of ADAM10 and ADAM17 in CD16b shedding mediated by different stimulators
    • 22770404
    • Guo S, Peng M, Zhao Q, Zhang W, (2012) Role of ADAM10 and ADAM17 in CD16b shedding mediated by different stimulators. Chin Med Sci J 27: 73-79. PubMed: 22770404.
    • (2012) Chin Med Sci J , vol.27 , pp. 73-79
    • Guo, S.1    Peng, M.2    Zhao, Q.3    Zhang, W.4
  • 37
    • 81755171473 scopus 로고    scopus 로고
    • ADAM9 inhibition increases membrane activity of ADAM10 and controls alpha-secretase processing of amyloid precursor protein
    • doi:10.1074/jbc.M111.280495
    • Moss ML, Powell G, Miller MA, Edwards L, Qi B, et al. (2011) ADAM9 inhibition increases membrane activity of ADAM10 and controls alpha-secretase processing of amyloid precursor protein. J Biol Chem 286: 40443-40451. doi:10.1074/jbc.M111.280495. PubMed: 21956108.
    • (2011) J Biol Chem , vol.286 , pp. 40443-40451
    • Moss, M.L.1    Powell, G.2    Miller, M.A.3    Edwards, L.4    Qi, B.5
  • 38
    • 21044444181 scopus 로고    scopus 로고
    • ERK-mediated phosphorylation of Thr735 in TNFalpha-converting enzyme and its potential role in TACE protein trafficking
    • doi:10.1242/jcs.02357
    • Soond SM, Everson B, Riches DW, Murphy G, (2005) ERK-mediated phosphorylation of Thr735 in TNFalpha-converting enzyme and its potential role in TACE protein trafficking. J Cell Sci 118: 2371-2380. doi:10.1242/jcs.02357. PubMed: 15923650.
    • (2005) J Cell Sci , vol.118 , pp. 2371-2380
    • Soond, S.M.1    Everson, B.2    Riches, D.W.3    Murphy, G.4
  • 39
    • 84855822415 scopus 로고    scopus 로고
    • Tumor necrosis factor signaling requires iRhom2 to promote trafficking and activation of TACE
    • doi:10.1126/science.1214400
    • Adrain C, Zettl M, Christova Y, Taylor N, Freeman M, (2012) Tumor necrosis factor signaling requires iRhom2 to promote trafficking and activation of TACE. Science 335: 225-228. doi:10.1126/science.1214400. PubMed: 22246777.
    • (2012) Science , vol.335 , pp. 225-228
    • Adrain, C.1    Zettl, M.2    Christova, Y.3    Taylor, N.4    Freeman, M.5
  • 40
    • 84862909285 scopus 로고    scopus 로고
    • iRhom2 regulation of TACE controls TNF-mediated protection against Listeria and responses to LPS
    • doi:10.1126/science.1214448
    • McIlwain DR, Lang PA, Maretzky T, Hamada K, Ohishi K, et al. (2012) iRhom2 regulation of TACE controls TNF-mediated protection against Listeria and responses to LPS. Science 335: 229-232. doi:10.1126/science.1214448. PubMed: 22246778.
    • (2012) Science , vol.335 , pp. 229-232
    • McIlwain, D.R.1    Lang, P.A.2    Maretzky, T.3    Hamada, K.4    Ohishi, K.5
  • 41
    • 0037318306 scopus 로고    scopus 로고
    • ADAM10-mediated cleavage of L1 adhesion molecule at the cell surface and in released membrane vesicles
    • 12475894
    • Gutwein P, Mechtersheimer S, Riedle S, Stoeck A, Gast D, et al. (2003) ADAM10-mediated cleavage of L1 adhesion molecule at the cell surface and in released membrane vesicles. FASEB J 17: 292-294. PubMed: 12475894.
    • (2003) FASEB J , vol.17 , pp. 292-294
    • Gutwein, P.1    Mechtersheimer, S.2    Riedle, S.3    Stoeck, A.4    Gast, D.5
  • 42
    • 0034723418 scopus 로고    scopus 로고
    • Protein kinase C-dependent alpha-secretase competes with beta-secretase for cleavage of amyloid-beta precursor protein in the trans-golgi network
    • doi:10.1074/jbc.275.4.2568
    • Skovronsky DM, Moore DB, Milla ME, Doms RW, Lee VM, (2000) Protein kinase C-dependent alpha-secretase competes with beta-secretase for cleavage of amyloid-beta precursor protein in the trans-golgi network. J Biol Chem 275: 2568-2575. doi:10.1074/jbc.275.4.2568. PubMed: 10644715.
    • (2000) J Biol Chem , vol.275 , pp. 2568-2575
    • Skovronsky, D.M.1    Moore, D.B.2    Milla, M.E.3    Doms, R.W.4    Lee, V.M.5
  • 43
    • 0035937787 scopus 로고    scopus 로고
    • Roles of Meltrin beta/ADAM19 in the processing of neuregulin
    • doi:10.1074/jbc.M007913200
    • Shirakabe K, Wakatsuki S, Kurisaki T, Fujisawa-Sehara A, (2001) Roles of Meltrin beta/ADAM19 in the processing of neuregulin. J Biol Chem 276: 9352-9358. doi:10.1074/jbc.M007913200. PubMed: 11116142.
    • (2001) J Biol Chem , vol.276 , pp. 9352-9358
    • Shirakabe, K.1    Wakatsuki, S.2    Kurisaki, T.3    Fujisawa-Sehara, A.4
  • 44
    • 48949087726 scopus 로고    scopus 로고
    • 2-D DIGE analyses of enriched secretory lysosomes reveal heterogeneous profiles of functionally relevant proteins in leukemic and activated human NK cells
    • doi:10.1002/pmic.200800170
    • Schmidt H, Gelhaus C, Nebendahl M, Lettau M, Watzl C, et al. (2008) 2-D DIGE analyses of enriched secretory lysosomes reveal heterogeneous profiles of functionally relevant proteins in leukemic and activated human NK cells. Proteomics 8: 2911-2925. doi:10.1002/pmic.200800170. PubMed: 18655029.
    • (2008) Proteomics , vol.8 , pp. 2911-2925
    • Schmidt, H.1    Gelhaus, C.2    Nebendahl, M.3    Lettau, M.4    Watzl, C.5
  • 45
    • 68949197486 scopus 로고    scopus 로고
    • Enrichment and analysis of secretory lysosomes from lymphocyte populations
    • doi:10.1186/1471-2172-10-41
    • Schmidt H, Gelhaus C, Lucius R, Nebendahl M, Leippe M, et al. (2009) Enrichment and analysis of secretory lysosomes from lymphocyte populations. BMC Immunol 10: 41. doi:10.1186/1471-2172-10-41. PubMed: 19640298.
    • (2009) BMC Immunol , vol.10 , pp. 41
    • Schmidt, H.1    Gelhaus, C.2    Lucius, R.3    Nebendahl, M.4    Leippe, M.5
  • 46
    • 78651590924 scopus 로고    scopus 로고
    • Effector granules in human T lymphocytes: the luminal proteome of secretory lysosomes from human T cells
    • doi:10.1186/1478-811X-9-4
    • Schmidt H, Gelhaus C, Nebendahl M, Lettau M, Lucius R, et al. (2011) Effector granules in human T lymphocytes: the luminal proteome of secretory lysosomes from human T cells. Cell Commun Signal 9: 4. doi:10.1186/1478-811X-9-4. PubMed: 21255389.
    • (2011) Cell Commun Signal , vol.9 , pp. 4
    • Schmidt, H.1    Gelhaus, C.2    Nebendahl, M.3    Lettau, M.4    Lucius, R.5
  • 47
    • 79953693933 scopus 로고    scopus 로고
    • Effector granules in human T lymphocytes: proteomic evidence for two distinct species of cytotoxic effector vesicles
    • doi:10.1021/pr100967v
    • Schmidt H, Gelhaus C, Nebendahl M, Lettau M, Lucius R, et al. (2011) Effector granules in human T lymphocytes: proteomic evidence for two distinct species of cytotoxic effector vesicles. J Proteome Res 10: 1603-1620. doi:10.1021/pr100967v. PubMed: 21247065.
    • (2011) J Proteome Res , vol.10 , pp. 1603-1620
    • Schmidt, H.1    Gelhaus, C.2    Nebendahl, M.3    Lettau, M.4    Lucius, R.5
  • 48
    • 84876110045 scopus 로고    scopus 로고
    • ADAM17, shedding, TACE as therapeutic targets
    • doi:10.1016/j.phrs.2013.01.012
    • Rose-John S, (2013) ADAM17, shedding, TACE as therapeutic targets. Pharmacol Res 71: 19-22. doi:10.1016/j.phrs.2013.01.012. PubMed: 23415892.
    • (2013) Pharmacol Res , vol.71 , pp. 19-22
    • Rose-John, S.1
  • 49
    • 63649141727 scopus 로고    scopus 로고
    • The "a disintegrin and metalloprotease" (ADAM) family of sheddases: physiological and cellular functions
    • doi:10.1016/j.semcdb.2008.11.002
    • Reiss K, Saftig P, (2009) The "a disintegrin and metalloprotease" (ADAM) family of sheddases: physiological and cellular functions. Semin Cell Dev Biol 20: 126-137. doi:10.1016/j.semcdb.2008.11.002. PubMed: 19049889.
    • (2009) Semin Cell Dev Biol , vol.20 , pp. 126-137
    • Reiss, K.1    Saftig, P.2
  • 50
    • 73849141240 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species mediate GPCR-induced TACE/ADAM17-dependent transforming growth factor-alpha shedding
    • doi:10.1091/mbc.E08-12-1256
    • Myers TJ, Brennaman LH, Stevenson M, Higashiyama S, Russell WE, et al. (2009) Mitochondrial reactive oxygen species mediate GPCR-induced TACE/ADAM17-dependent transforming growth factor-alpha shedding. Mol Cell Biol 20: 5236-5249. doi:10.1091/mbc.E08-12-1256. PubMed: 19846666.
    • (2009) Mol Cell Biol , vol.20 , pp. 5236-5249
    • Myers, T.J.1    Brennaman, L.H.2    Stevenson, M.3    Higashiyama, S.4    Russell, W.E.5
  • 51
    • 58249092162 scopus 로고    scopus 로고
    • ERK1/2 mediate wounding- and G-protein-coupled receptor ligands-induced EGFR activation via regulating ADAM17 and HB-EGF shedding
    • 18658095
    • Yin J, Yu FS, (2009) ERK1/2 mediate wounding- and G-protein-coupled receptor ligands-induced EGFR activation via regulating ADAM17 and HB-EGF shedding. Invest Ophthalmol Vis Sci 50: 132-139. PubMed: 18658095.
    • (2009) Invest Ophthalmol Vis Sci , vol.50 , pp. 132-139
    • Yin, J.1    Yu, F.S.2
  • 52
    • 36249000086 scopus 로고    scopus 로고
    • PI3-K- and PKC-dependent up-regulation of APP processing enzymes by retinoic acid
    • doi:10.1016/j.bbrc.2007.10.167
    • Holback S, Adlerz L, Gatsinzi T, Jacobsen KT, Iverfeldt K, (2008) PI3-K- and PKC-dependent up-regulation of APP processing enzymes by retinoic acid. Biochem Biophys Res Commun 365: 298-303. doi:10.1016/j.bbrc.2007.10.167. PubMed: 17986385.
    • (2008) Biochem Biophys Res Commun , vol.365 , pp. 298-303
    • Holback, S.1    Adlerz, L.2    Gatsinzi, T.3    Jacobsen, K.T.4    Iverfeldt, K.5
  • 53
    • 79952220937 scopus 로고    scopus 로고
    • PKCalpha and PKCdelta regulate ADAM17-mediated ectodomain shedding of heparin binding-EGF through separate pathways
    • doi:10.1371/journal.pone.0017168
    • Kveiborg M, Instrell R, Rowlands C, Howell M, Parker PJ, (2011) PKCalpha and PKCdelta regulate ADAM17-mediated ectodomain shedding of heparin binding-EGF through separate pathways. PLOS ONE 6: e17168. doi:10.1371/journal.pone.0017168. PubMed: 21386996.
    • (2011) PLOS ONE , vol.6
    • Kveiborg, M.1    Instrell, R.2    Rowlands, C.3    Howell, M.4    Parker, P.J.5
  • 54
    • 79952654912 scopus 로고    scopus 로고
    • TACE/ADAM-17 phosphorylation by PKC-epsilon mediates premalignant changes in tobacco smoke-exposed lung cells
    • doi:10.1371/journal.pone.0017489
    • Lemjabbar-Alaoui H, Sidhu SS, Mengistab A, Gallup M, Basbaum C, (2011) TACE/ADAM-17 phosphorylation by PKC-epsilon mediates premalignant changes in tobacco smoke-exposed lung cells. PLOS ONE 6: e17489. doi:10.1371/journal.pone.0017489. PubMed: 21423656.
    • (2011) PLOS ONE , vol.6
    • Lemjabbar-Alaoui, H.1    Sidhu, S.S.2    Mengistab, A.3    Gallup, M.4    Basbaum, C.5
  • 55
    • 0029795014 scopus 로고    scopus 로고
    • Pore-forming toxins trigger shedding of receptors for interleukin 6 and lipopolysaccharide
    • doi:10.1073/pnas.93.15.7882
    • Walev I, Vollmer P, Palmer M, Bhakdi S, Rose-John S, (1996) Pore-forming toxins trigger shedding of receptors for interleukin 6 and lipopolysaccharide. Proc Natl Acad Sci U S A 93: 7882-7887. doi:10.1073/pnas.93.15.7882. PubMed: 8755571.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 7882-7887
    • Walev, I.1    Vollmer, P.2    Palmer, M.3    Bhakdi, S.4    Rose-John, S.5
  • 56
    • 34548856204 scopus 로고    scopus 로고
    • Apoptosis is a natural stimulus of IL6R shedding and contributes to the proinflammatory trans-signaling function of neutrophils
    • doi:10.1182/blood-2007-01-067918
    • Chalaris A, Rabe B, Paliga K, Lange H, Laskay T, et al. (2007) Apoptosis is a natural stimulus of IL6R shedding and contributes to the proinflammatory trans-signaling function of neutrophils. Blood 110: 1748-1755. doi:10.1182/blood-2007-01-067918. PubMed: 17567983.
    • (2007) Blood , vol.110 , pp. 1748-1755
    • Chalaris, A.1    Rabe, B.2    Paliga, K.3    Lange, H.4    Laskay, T.5
  • 57
    • 26444448409 scopus 로고    scopus 로고
    • L1 is sequentially processed by two differently activated metalloproteases and presenilin/gamma-secretase and regulates neural cell adhesion, cell migration, and neurite outgrowth
    • doi:10.1128/MCB.25.20.9040-9053.2005
    • Maretzky T, Schulte M, Ludwig A, Rose-John S, Blobel C, et al. (2005) L1 is sequentially processed by two differently activated metalloproteases and presenilin/gamma-secretase and regulates neural cell adhesion, cell migration, and neurite outgrowth. Mol Cell Biol 25: 9040-9053. doi:10.1128/MCB.25.20.9040-9053.2005. PubMed: 16199880.
    • (2005) Mol Cell Biol , vol.25 , pp. 9040-9053
    • Maretzky, T.1    Schulte, M.2    Ludwig, A.3    Rose-John, S.4    Blobel, C.5
  • 58
    • 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
    • doi:10.2174/1386207053258488
    • Ludwig A, Hundhausen C, Lambert MH, Broadway N, Andrews RC, et al. (2005) 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. doi:10.2174/1386207053258488. PubMed: 15777180.
    • (2005) Comb Chem High Throughput Screen , vol.8 , pp. 161-171
    • Ludwig, A.1    Hundhausen, C.2    Lambert, M.H.3    Broadway, N.4    Andrews, R.C.5
  • 59
    • 0034726669 scopus 로고    scopus 로고
    • Trafficking of human ADAM 12-L: retention in the trans-Golgi network
    • doi:10.1006/bbrc.2000.3295
    • Hougaard S, Loechel F, Xu X, Tajima R, Albrechtsen R, et al. (2000) Trafficking of human ADAM 12-L: retention in the trans-Golgi network. Biochem Biophys Res Commun 275: 261-267. doi:10.1006/bbrc.2000.3295. PubMed: 10964655.
    • (2000) Biochem Biophys Res Commun , vol.275 , pp. 261-267
    • Hougaard, S.1    Loechel, F.2    Xu, X.3    Tajima, R.4    Albrechtsen, R.5
  • 60
    • 10944243611 scopus 로고    scopus 로고
    • Regulation of ADAM12 cell-surface expression by protein kinase C epsilon
    • doi:10.1074/jbc.M403753200
    • Sundberg C, Thodeti CK, Kveiborg M, Larsson C, Parker P, et al. (2004) Regulation of ADAM12 cell-surface expression by protein kinase C epsilon. J Biol Chem 279: 51601-51611. doi:10.1074/jbc.M403753200. PubMed: 15364951.
    • (2004) J Biol Chem , vol.279 , pp. 51601-51611
    • Sundberg, C.1    Thodeti, C.K.2    Kveiborg, M.3    Larsson, C.4    Parker, P.5
  • 61
    • 84869121252 scopus 로고    scopus 로고
    • TspanC8 tetraspanins regulate ADAM10/Kuzbanian trafficking and promote Notch activation in flies and mammals
    • doi:10.1083/jcb.201201133
    • Dornier E, Coumailleau F, Ottavi JF, Moretti J, Boucheix C, et al. (2012) TspanC8 tetraspanins regulate ADAM10/Kuzbanian trafficking and promote Notch activation in flies and mammals. J Cell Biol 199: 481-496. doi:10.1083/jcb.201201133. PubMed: 23091066.
    • (2012) J Cell Biol , vol.199 , pp. 481-496
    • Dornier, E.1    Coumailleau, F.2    Ottavi, J.F.3    Moretti, J.4    Boucheix, C.5
  • 62
    • 84869211737 scopus 로고    scopus 로고
    • The TspanC8 subgroup of tetraspanins interacts with A disintegrin and metalloprotease 10 (ADAM10) and regulates its maturation and cell surface expression
    • doi:10.1074/jbc.M112.416503
    • Haining EJ, Yang J, Bailey RL, Khan K, Collier R, et al. (2012) The TspanC8 subgroup of tetraspanins interacts with A disintegrin and metalloprotease 10 (ADAM10) and regulates its maturation and cell surface expression. J Biol Chem 287: 39753-39765. doi:10.1074/jbc.M112.416503. PubMed: 23035126.
    • (2012) J Biol Chem , vol.287 , pp. 39753-39765
    • Haining, E.J.1    Yang, J.2    Bailey, R.L.3    Khan, K.4    Collier, R.5
  • 63
    • 70350528991 scopus 로고    scopus 로고
    • Tetraspanin12 regulates ADAM10-dependent cleavage of amyloid precursor protein
    • doi:10.1096/fj.09-133462
    • Xu D, Sharma C, Hemler ME, (2009) Tetraspanin12 regulates ADAM10-dependent cleavage of amyloid precursor protein. FASEB J 23: 3674-3681. doi:10.1096/fj.09-133462. PubMed: 19587294.
    • (2009) FASEB J , vol.23 , pp. 3674-3681
    • Xu, D.1    Sharma, C.2    Hemler, M.E.3
  • 64
    • 80052953314 scopus 로고    scopus 로고
    • The sheddase activity of ADAM17/TACE is regulated by the tetraspanin CD9
    • doi:10.1007/s00018-011-0639-0
    • Gutiérrez-López MD, Gilsanz A, Yáñez-Mó M, Ovalle S, Lafuente EM, et al. (2011) The sheddase activity of ADAM17/TACE is regulated by the tetraspanin CD9. Cell Mol Life Sci 68: 3275-3292. doi:10.1007/s00018-011-0639-0. PubMed: 21365281.
    • (2011) Cell Mol Life Sci , vol.68 , pp. 3275-3292
    • Gutiérrez-López, M.D.1    Gilsanz, A.2    Yáñez-Mó, M.3    Ovalle, S.4    Lafuente, E.M.5
  • 65
    • 77049118038 scopus 로고    scopus 로고
    • ADAM-17 is activated by the mitogenic protein kinase ERK in a model of kidney fibrosis
    • doi:10.1097/MAJ.0b013e3181cb4487
    • Bell HL, Gööz M, (2010) ADAM-17 is activated by the mitogenic protein kinase ERK in a model of kidney fibrosis. Am J Med Sci 339: 105-107. doi:10.1097/MAJ.0b013e3181cb4487. PubMed: 20087163.
    • (2010) Am J Med Sci , vol.339 , pp. 105-107
    • Bell, H.L.1    Gööz, M.2
  • 66
    • 33746328093 scopus 로고    scopus 로고
    • 5-HT2A receptor induces ERK phosphorylation and proliferation through ADAM-17 tumor necrosis factor-alpha-converting enzyme (TACE) activation and heparin-bound epidermal growth factor-like growth factor (HB-EGF) shedding in mesangial cells
    • doi:10.1074/jbc.M512096200
    • Göoz M, Göoz P, Luttrell LM, Raymond JR, (2006) 5-HT2A receptor induces ERK phosphorylation and proliferation through ADAM-17 tumor necrosis factor-alpha-converting enzyme (TACE) activation and heparin-bound epidermal growth factor-like growth factor (HB-EGF) shedding in mesangial cells. J Biol Chem 281: 21004-21012. doi:10.1074/jbc.M512096200. PubMed: 16737974.
    • (2006) J Biol Chem , vol.281 , pp. 21004-21012
    • Göoz, M.1    Göoz, P.2    Luttrell, L.M.3    Raymond, J.R.4
  • 67
    • 84860289206 scopus 로고    scopus 로고
    • ADAM17 targets MMP-2 and MMP-9 via EGFR-MEK-ERK pathway activation to promote prostate cancer cell invasion
    • 22200661
    • Xiao LJ, Lin P, Lin F, Liu X, Qin W, et al. (2012) ADAM17 targets MMP-2 and MMP-9 via EGFR-MEK-ERK pathway activation to promote prostate cancer cell invasion. Int J Oncol 40: 1714-1724. PubMed: 22200661.
    • (2012) Int J Oncol , vol.40 , pp. 1714-1724
    • Xiao, L.J.1    Lin, P.2    Lin, F.3    Liu, X.4    Qin, W.5
  • 68
    • 0034640428 scopus 로고    scopus 로고
    • Stimulation-induced down-regulation of tumor necrosis factor-alpha converting enzyme
    • doi:10.1074/jbc.275.19.14598
    • Doedens JR, Black RA, (2000) Stimulation-induced down-regulation of tumor necrosis factor-alpha converting enzyme. J Biol Chem 275: 14598-14607. doi:10.1074/jbc.275.19.14598. PubMed: 10799546.
    • (2000) J Biol Chem , vol.275 , pp. 14598-14607
    • Doedens, J.R.1    Black, R.A.2
  • 69
    • 0036481624 scopus 로고    scopus 로고
    • Secretory lysosomes
    • doi:10.1038/nrm732
    • Blott EJ, Griffiths GM, (2002) Secretory lysosomes. Nat Rev Mol Cell Biol 3: 122-131. doi:10.1038/nrm732. PubMed: 11836514.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 122-131
    • Blott, E.J.1    Griffiths, G.M.2
  • 70
    • 9644275363 scopus 로고    scopus 로고
    • CTL secretory lysosomes: biogenesis and secretion of a harmful organelle
    • doi:10.1016/j.smim.2004.09.007
    • Bossi G, Griffiths GM, (2005) CTL secretory lysosomes: biogenesis and secretion of a harmful organelle. Semin Immunol 17: 87-94. doi:10.1016/j.smim.2004.09.007. PubMed: 15582491.
    • (2005) Semin Immunol , vol.17 , pp. 87-94
    • Bossi, G.1    Griffiths, G.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.