메뉴 건너뛰기




Volumn 20, Issue 2, 2009, Pages 126-137

The "A Disintegrin And Metalloprotease" (ADAM) family of sheddases: Physiological and cellular functions

Author keywords

ADAMs; Cancer; Cell adhesion; Inflammation; Signalling

Indexed keywords

ADAM PROTEIN; CELL ADHESION MOLECULE; CELL SURFACE PROTEIN; CYTOKINE; GROWTH FACTOR; GROWTH FACTOR RECEPTOR; LIGAND; PROTEIN ADAM1; PROTEIN ADAM10; PROTEIN ADAM11; PROTEIN ADAM12; PROTEIN ADAM13; PROTEIN ADAM15; PROTEIN ADAM16; PROTEIN ADAM17; PROTEIN ADAM18; PROTEIN ADAM19; PROTEIN ADAM2; PROTEIN ADAM22; PROTEIN ADAM24; PROTEIN ADAM26; PROTEIN ADAM27; PROTEIN ADAM28; PROTEIN ADAM29; PROTEIN ADAM33; PROTEIN ADAM8; PROTEIN ADAM9; PROTEINASE; SHEDDASE; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 63649141727     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.semcdb.2008.11.002     Document Type: Review
Times cited : (350)

References (184)
  • 1
    • 0037224740 scopus 로고    scopus 로고
    • The ADAMs family of metalloproteases: multidomain proteins with multiple functions
    • Seals D.F., and Courtneidge S.A. The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes Dev 17 (2003) 7-30
    • (2003) Genes Dev , vol.17 , pp. 7-30
    • Seals, D.F.1    Courtneidge, S.A.2
  • 2
    • 11244261160 scopus 로고    scopus 로고
    • ADAMs: key components in EGFR signalling and development
    • Blobel C.P. ADAMs: key components in EGFR signalling and development. Nat Rev Mol Cell Biol 6 (2005) 32-43
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 32-43
    • Blobel, C.P.1
  • 3
    • 33646565312 scopus 로고    scopus 로고
    • (Make) stick and cut loose-disintegrin metalloproteases in development and disease
    • Tousseyn T., Jorissen E., Reiss K., and Hartmann D. (Make) stick and cut loose-disintegrin metalloproteases in development and disease. Birth Defects Res C Embryo Today 78 (2006) 24-46
    • (2006) Birth Defects Res C Embryo Today , vol.78 , pp. 24-46
    • Tousseyn, T.1    Jorissen, E.2    Reiss, K.3    Hartmann, D.4
  • 4
    • 42149110867 scopus 로고    scopus 로고
    • Part-time alpha-secretases: the functional biology of ADAM 9, 10 and 17
    • Deuss M., Reiss K., and Hartmann D. Part-time alpha-secretases: the functional biology of ADAM 9, 10 and 17. Curr Alzheimer Res 5 (2008) 187-201
    • (2008) Curr Alzheimer Res , vol.5 , pp. 187-201
    • Deuss, M.1    Reiss, K.2    Hartmann, D.3
  • 5
    • 33746381184 scopus 로고    scopus 로고
    • Breaking up the tie: disintegrin-like metalloproteinases as regulators of cell migration in inflammation and invasion
    • Reiss K., Ludwig A., and Saftig P. Breaking up the tie: disintegrin-like metalloproteinases as regulators of cell migration in inflammation and invasion. Pharmacol Ther 111 (2006) 985-1006
    • (2006) Pharmacol Ther , vol.111 , pp. 985-1006
    • Reiss, K.1    Ludwig, A.2    Saftig, P.3
  • 7
    • 0029045064 scopus 로고
    • ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain
    • Wolfsberg T.G., Straight P.D., Gerena R.L., Huovila A.P., Primakoff P., Myles D.G., et al. ADAM, a widely distributed and developmentally regulated gene family encoding membrane proteins with a disintegrin and metalloprotease domain. Dev Biol 169 (1995) 378-383
    • (1995) Dev Biol , vol.169 , pp. 378-383
    • Wolfsberg, T.G.1    Straight, P.D.2    Gerena, R.L.3    Huovila, A.P.4    Primakoff, P.5    Myles, D.G.6
  • 8
    • 0347445722 scopus 로고    scopus 로고
    • A genomic analysis of rat proteases and protease inhibitors
    • Puente X.S., and Lopez-Otin C. A genomic analysis of rat proteases and protease inhibitors. Genome Res 14 (2004) 609-622
    • (2004) Genome Res , vol.14 , pp. 609-622
    • Puente, X.S.1    Lopez-Otin, C.2
  • 9
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'
    • Bode W., Gomis-Ruth F.X., and Stockler W. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'. FEBS Lett 331 (1993) 134-140
    • (1993) FEBS Lett , vol.331 , pp. 134-140
    • Bode, W.1    Gomis-Ruth, F.X.2    Stockler, W.3
  • 10
    • 0343196671 scopus 로고    scopus 로고
    • Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis
    • Pan D., and Rubin G.M. Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis. Cell 90 (1997) 271-280
    • (1997) Cell , vol.90 , pp. 271-280
    • Pan, D.1    Rubin, G.M.2
  • 11
    • 0042671434 scopus 로고    scopus 로고
    • UNC-71, a disintegrin and metalloprotease (ADAM) protein, regulates motor axon guidance and sex myoblast migration in C. elegans
    • Huang X., Huang P., Robinson M.K., Stern M.J., and Jin Y. UNC-71, a disintegrin and metalloprotease (ADAM) protein, regulates motor axon guidance and sex myoblast migration in C. elegans. Development 130 (2003) 3147-3161
    • (2003) Development , vol.130 , pp. 3147-3161
    • Huang, X.1    Huang, P.2    Robinson, M.K.3    Stern, M.J.4    Jin, Y.5
  • 12
    • 1242300153 scopus 로고    scopus 로고
    • ADAM family protein Mde10 is essential for development of spore envelopes in the fission yeast Schizosaccharomyces pombe
    • Nakamura T., Abe H., Hirata A., and Shimoda C. ADAM family protein Mde10 is essential for development of spore envelopes in the fission yeast Schizosaccharomyces pombe. Eukaryot Cell 3 (2004) 27-39
    • (2004) Eukaryot Cell , vol.3 , pp. 27-39
    • Nakamura, T.1    Abe, H.2    Hirata, A.3    Shimoda, C.4
  • 13
    • 0037716445 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha converting enzyme is processed by proprotein-convertases to its mature form which is degraded upon phorbol ester stimulation
    • Endres K., Anders A., Kojro E., Gilbert S., Fahrenholz F., and Postina R. Tumor necrosis factor-alpha converting enzyme is processed by proprotein-convertases to its mature form which is degraded upon phorbol ester stimulation. Eur J Biochem 270 (2003) 2386-2393
    • (2003) Eur J Biochem , vol.270 , pp. 2386-2393
    • Endres, K.1    Anders, A.2    Kojro, E.3    Gilbert, S.4    Fahrenholz, F.5    Postina, R.6
  • 14
    • 0035430436 scopus 로고    scopus 로고
    • Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases
    • Anders A., Gilbert S., Garten W., Postina R., and Fahrenholz F. Regulation of the alpha-secretase ADAM10 by its prodomain and proprotein convertases. FASEB J 15 (2001) 1837-1839
    • (2001) FASEB J , vol.15 , pp. 1837-1839
    • Anders, A.1    Gilbert, S.2    Garten, W.3    Postina, R.4    Fahrenholz, F.5
  • 15
    • 37249079599 scopus 로고    scopus 로고
    • The ADAM10 prodomain is a specific inhibitor of ADAM10 proteolytic activity and inhibits cellular shedding events
    • Moss M.L., Bomar M., Liu Q., Sage H., Dempsey P., Lenhart P.M., et al. The ADAM10 prodomain is a specific inhibitor of ADAM10 proteolytic activity and inhibits cellular shedding events. J Biol Chem 282 (2007) 35712-35721
    • (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.M.6
  • 16
    • 3843096112 scopus 로고    scopus 로고
    • Inhibition of the tumor necrosis factor-alpha-converting enzyme by its pro domain
    • Gonzales P.E., Solomon A., Miller A.B., Leesnitzer M.A., Sagi I., and Milla M.E. Inhibition of the tumor necrosis factor-alpha-converting enzyme by its pro domain. J Biol Chem 279 (2004) 31638-31645
    • (2004) J Biol Chem , vol.279 , pp. 31638-31645
    • Gonzales, P.E.1    Solomon, A.2    Miller, A.B.3    Leesnitzer, M.A.4    Sagi, I.5    Milla, M.E.6
  • 17
    • 0033616716 scopus 로고    scopus 로고
    • Constitutive and regulated alpha-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 alpha-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease. Proc Natl Acad Sci U S A 96 (1999) 3922-3927
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 3922-3927
    • Lammich, S.1    Kojro, E.2    Postina, R.3    Gilbert, S.4    Pfeiffer, R.5    Jasionowski, M.6
  • 18
    • 0038541768 scopus 로고    scopus 로고
    • Intracellular maturation and localization of the tumour necrosis factor alpha convertase (TACE)
    • Schlondorff J., Becherer J.D., and Blobel C.P. Intracellular maturation and localization of the tumour necrosis factor alpha convertase (TACE). Biochem J 347 Pt 1 (2000) 131-138
    • (2000) Biochem J , vol.347 , Issue.PART 1 , pp. 131-138
    • Schlondorff, J.1    Becherer, J.D.2    Blobel, C.P.3
  • 19
    • 0037318306 scopus 로고    scopus 로고
    • ADAM10-mediated cleavage of L1 adhesion molecule at the cell surface and in released membrane vesicles
    • Gutwein P., Mechtersheimer S., Riedle S., Stoeck A., Gast D., Joumaa S., et al. ADAM10-mediated cleavage of L1 adhesion molecule at the cell surface and in released membrane vesicles. FASEB J 17 (2003) 292-294
    • (2003) FASEB J , vol.17 , pp. 292-294
    • Gutwein, P.1    Mechtersheimer, S.2    Riedle, S.3    Stoeck, A.4    Gast, D.5    Joumaa, S.6
  • 22
    • 0141533033 scopus 로고    scopus 로고
    • ADAMs: modulators of cell-cell and cell-matrix interactions
    • White J.M. ADAMs: modulators of cell-cell and cell-matrix interactions. Curr Opin Cell Biol 15 (2003) 598-606
    • (2003) Curr Opin Cell Biol , vol.15 , pp. 598-606
    • White, J.M.1
  • 24
    • 0034640286 scopus 로고    scopus 로고
    • Functional analysis of the domain structure of tumor necrosis factor-alpha converting enzyme
    • Reddy P., Slack J.L., Davis R., Cerretti D.P., Kozlosky C.J., Blanton R.A., et al. Functional analysis of the domain structure of tumor necrosis factor-alpha converting enzyme. J Biol Chem 275 (2000) 14608-14614
    • (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
  • 25
    • 26844448800 scopus 로고    scopus 로고
    • Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans
    • Janes P.W., Saha N., Barton W.A., Kolev M.V., Wimmer-Kleikamp S.H., Nievergall E., et al. Adam meets Eph: an ADAM substrate recognition module acts as a molecular switch for ephrin cleavage in trans. Cell 123 (2005) 291-304
    • (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
  • 26
    • 0032724176 scopus 로고    scopus 로고
    • Specific sequence elements are required for the expression of functional tumor necrosis factor-alpha-converting enzyme (TACE)
    • Milla M.E., Leesnitzer M.A., Moss M.L., Clay W.C., Carter H.L., Miller A.B., et al. Specific sequence elements are required for the expression of functional tumor necrosis factor-alpha-converting enzyme (TACE). J Biol Chem 274 (1999) 30563-30570
    • (1999) J Biol Chem , vol.274 , pp. 30563-30570
    • Milla, M.E.1    Leesnitzer, M.A.2    Moss, M.L.3    Clay, W.C.4    Carter, H.L.5    Miller, A.B.6
  • 27
    • 0034729369 scopus 로고    scopus 로고
    • The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreading
    • Iba K., Albrechtsen R., Gilpin B., Frohlich C., Loechel F., Zolkiewska A., et al. The cysteine-rich domain of human ADAM 12 supports cell adhesion through syndecans and triggers signaling events that lead to beta1 integrin-dependent cell spreading. J Cell Biol 149 (2000) 1143-1156
    • (2000) J Cell Biol , vol.149 , pp. 1143-1156
    • Iba, K.1    Albrechtsen, R.2    Gilpin, B.3    Frohlich, C.4    Loechel, F.5    Zolkiewska, A.6
  • 28
    • 0033230156 scopus 로고    scopus 로고
    • Disintegrin-like/cysteine-rich region of ADAM 12 is an active cell adhesion domain
    • Zolkiewska A. Disintegrin-like/cysteine-rich region of ADAM 12 is an active cell adhesion domain. Exp Cell Res 252 (1999) 423-431
    • (1999) Exp Cell Res , vol.252 , pp. 423-431
    • Zolkiewska, A.1
  • 29
    • 0033615602 scopus 로고    scopus 로고
    • Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1
    • Howard L., Nelson K.K., Maciewicz R.A., and Blobel C.P. Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1. J Biol Chem 274 (1999) 31693-31699
    • (1999) J Biol Chem , vol.274 , pp. 31693-31699
    • Howard, L.1    Nelson, K.K.2    Maciewicz, R.A.3    Blobel, C.P.4
  • 30
    • 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 (2004) 41950-41959
    • (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
  • 32
    • 0242580234 scopus 로고    scopus 로고
    • PACSIN3 binds ADAM12/meltrin alpha and up-regulates 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 alpha and up-regulates ectodomain shedding of heparin-binding epidermal growth factor-like growth factor. J Biol Chem 278 (2003) 46029-46034
    • (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
  • 33
    • 33747736649 scopus 로고    scopus 로고
    • A basolateral sorting signal directs ADAM10 to adherens junctions and is required for its function in cell migration
    • Wild-Bode C., Fellerer K., Kugler J., Haass C., and Capell A. A basolateral sorting signal directs ADAM10 to adherens junctions and is required for its function in cell migration. J Biol Chem 281 (2006) 23824-23829
    • (2006) J Biol Chem , vol.281 , pp. 23824-23829
    • Wild-Bode, C.1    Fellerer, K.2    Kugler, J.3    Haass, C.4    Capell, A.5
  • 34
    • 33847171931 scopus 로고    scopus 로고
    • Synapse-associated protein-97 mediates alpha-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 alpha-secretase ADAM10 trafficking and promotes its activity. J Neurosci 27 (2007) 1682-1691
    • (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
  • 36
    • 0035337709 scopus 로고    scopus 로고
    • Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin beta
    • Nishimura H., Cho C., Branciforte D.R., Myles D.G., and Primakoff P. Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin beta. Dev Biol 233 (2001) 204-213
    • (2001) Dev Biol , vol.233 , pp. 204-213
    • Nishimura, H.1    Cho, C.2    Branciforte, D.R.3    Myles, D.G.4    Primakoff, P.5
  • 37
    • 0034681260 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans
    • Brown M.S., Ye J., Rawson R.B., and Goldstein J.L. Regulated intramembrane proteolysis: a control mechanism conserved from bacteria to humans. Cell 100 (2000) 391-398
    • (2000) Cell , vol.100 , pp. 391-398
    • Brown, M.S.1    Ye, J.2    Rawson, R.B.3    Goldstein, J.L.4
  • 38
    • 34347251573 scopus 로고    scopus 로고
    • Signal peptide peptidases and gamma-secretase: cousins of the same protease family?
    • Fluhrer R., and Haass C. Signal peptide peptidases and gamma-secretase: cousins of the same protease family?. Neurodegener Dis 4 (2007) 112-116
    • (2007) Neurodegener Dis , vol.4 , pp. 112-116
    • Fluhrer, R.1    Haass, C.2
  • 39
    • 0034714357 scopus 로고    scopus 로고
    • Regulated cleavage of a contact-mediated axon repellent
    • Hattori M., Osterfield M., and Flanagan J.G. Regulated cleavage of a contact-mediated axon repellent. Science 289 (2000) 1360-1365
    • (2000) Science , vol.289 , pp. 1360-1365
    • Hattori, M.1    Osterfield, M.2    Flanagan, J.G.3
  • 40
    • 21544467772 scopus 로고    scopus 로고
    • ADAM10 mediates E-cadherin shedding and regulates epithelial cell-cell adhesion, migration, and beta-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 beta-catenin translocation. Proc Natl Acad Sci U S A 102 (2005) 9182-9187
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 9182-9187
    • Maretzky, T.1    Reiss, K.2    Ludwig, A.3    Buchholz, J.4    Scholz, F.5    Proksch, E.6
  • 41
    • 15444371289 scopus 로고    scopus 로고
    • ADAM10 cleavage of N-cadherin and regulation of cell-cell adhesion and beta-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 adhesion and beta-catenin nuclear signalling. EMBO J 24 (2005) 742-752
    • (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
  • 42
    • 33746826046 scopus 로고    scopus 로고
    • Regulated ADAM10-dependent ectodomain shedding of {gamma}-protocadherin C3 modulates cell-cell adhesion
    • Reiss K., Maretzky T., Haas I.G., Schulte M., Ludwig A., Frank M., et al. Regulated ADAM10-dependent ectodomain shedding of {gamma}-protocadherin C3 modulates cell-cell adhesion. J Biol Chem 281 (2006) 21735-21744
    • (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
  • 43
    • 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 C.P., Saftig P., et al. ADAM10 regulates endothelial permeability and T-Cell transmigration by proteolysis of vascular endothelial cadherin. Circ Res 102 (2008) 1192-1201
    • (2008) Circ Res , vol.102 , pp. 1192-1201
    • Schulz, B.1    Pruessmeyer, J.2    Maretzky, T.3    Ludwig, A.4    Blobel, C.P.5    Saftig, P.6
  • 44
    • 18344380083 scopus 로고    scopus 로고
    • A presenilin-1/gamma-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions
    • Marambaud P., Shioi J., Serban G., Georgakopoulos A., Sarner S., Nagy V., et al. A presenilin-1/gamma-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions. EMBO J 21 (2002) 1948-1956
    • (2002) EMBO J , vol.21 , pp. 1948-1956
    • Marambaud, P.1    Shioi, J.2    Serban, G.3    Georgakopoulos, A.4    Sarner, S.5    Nagy, V.6
  • 45
    • 0141429160 scopus 로고    scopus 로고
    • A CBP binding transcriptional repressor produced by the PS1/epsilon-cleavage of N-cadherin is inhibited by PS1 FAD mutations
    • Marambaud P., Wen P.H., Dutt A., Shioi J., Takashima A., Siman R., et al. A CBP binding transcriptional repressor produced by the PS1/epsilon-cleavage of N-cadherin is inhibited by PS1 FAD mutations. Cell 114 (2003) 635-645
    • (2003) Cell , vol.114 , pp. 635-645
    • Marambaud, P.1    Wen, P.H.2    Dutt, A.3    Shioi, J.4    Takashima, A.5    Siman, R.6
  • 46
    • 45349091378 scopus 로고    scopus 로고
    • ADAM10-mediated E-cadherin release is regulated by proinflammatory cytokines and modulates keratinocyte cohesion in eczematous dermatitis
    • Maretzky T., Scholz F., Koten B., Proksch E., Saftig P., and Reiss K. ADAM10-mediated E-cadherin release is regulated by proinflammatory cytokines and modulates keratinocyte cohesion in eczematous dermatitis. J Invest Dermatol 128 (2008) 1737-1746
    • (2008) J Invest Dermatol , vol.128 , pp. 1737-1746
    • Maretzky, T.1    Scholz, F.2    Koten, B.3    Proksch, E.4    Saftig, P.5    Reiss, K.6
  • 47
    • 24644498313 scopus 로고    scopus 로고
    • Mammalian cadherins and protocadherins: about cell death, synapses and processing
    • Junghans D., Haas I.G., and Kemler R. Mammalian cadherins and protocadherins: about cell death, synapses and processing. Curr Opin Cell Biol 17 (2005) 446-452
    • (2005) Curr Opin Cell Biol , vol.17 , pp. 446-452
    • Junghans, D.1    Haas, I.G.2    Kemler, R.3
  • 48
    • 15744388308 scopus 로고    scopus 로고
    • Presenilin-dependent processing and nuclear function of gamma-protocadherins
    • Haas I.G., Frank M., Veron N., and Kemler R. Presenilin-dependent processing and nuclear function of gamma-protocadherins. J Biol Chem 280 (2005) 9313-9319
    • (2005) J Biol Chem , vol.280 , pp. 9313-9319
    • Haas, I.G.1    Frank, M.2    Veron, N.3    Kemler, R.4
  • 49
    • 33746928340 scopus 로고    scopus 로고
    • Emerging roles for ectodomain shedding in the regulation of inflammatory responses
    • Garton K.J., Gough P.J., and Raines E.W. Emerging roles for ectodomain shedding in the regulation of inflammatory responses. J Leukoc Biol 79 (2006) 1105-1116
    • (2006) J Leukoc Biol , vol.79 , pp. 1105-1116
    • Garton, K.J.1    Gough, P.J.2    Raines, E.W.3
  • 50
    • 0141509970 scopus 로고    scopus 로고
    • Stimulated shedding of vascular cell adhesion molecule 1 (VCAM-1) is mediated by tumor necrosis factor-alpha-converting enzyme (ADAM 17)
    • Garton K.J., Gough P.J., Philalay J., Wille P.T., Blobel C.P., Whitehead R.H., et al. Stimulated shedding of vascular cell adhesion molecule 1 (VCAM-1) is mediated by tumor necrosis factor-alpha-converting enzyme (ADAM 17). J Biol Chem 278 (2003) 37459-37464
    • (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
  • 51
    • 33645643886 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha-converting enzyme (TACE/ADAM-17) mediates the ectodomain cleavage of intercellular adhesion molecule-1 (ICAM-1)
    • Tsakadze N.L., Sithu S.D., Sen U., English W.R., Murphy G., and D'Souza S.E. Tumor necrosis factor-alpha-converting enzyme (TACE/ADAM-17) mediates the ectodomain cleavage of intercellular adhesion molecule-1 (ICAM-1). J Biol Chem 281 (2006) 3157-3164
    • (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
  • 52
    • 2442527640 scopus 로고    scopus 로고
    • The transmembrane CXC-chemokine ligand 16 is induced by IFN-gamma and TNF-alpha and shed by the activity of the disintegrin-like metalloproteinase ADAM10
    • Abel S., Hundhausen C., Mentlein R., Schulte A., Berkhout T.A., Broadway N., et al. The transmembrane CXC-chemokine ligand 16 is induced by IFN-gamma and TNF-alpha and shed by the activity of the disintegrin-like metalloproteinase ADAM10. J Immunol 172 (2004) 6362-6372
    • (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
  • 53
    • 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., Hundhausen C., Lambert M.H., Broadway N., Andrews R.C., Bickett D.M., 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 (2005) 161-171
    • (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    Bickett, D.M.6
  • 56
    • 0037064135 scopus 로고    scopus 로고
    • Structure-function relationship and role of tumor necrosis factor-alpha-converting enzyme in the down-regulation of L-selectin by non-steroidal anti-inflammatory drugs
    • Gomez-Gaviro M.V., Gonzalez-Alvaro I., Dominguez-Jimenez C., Peschon J., Black R.A., Sanchez-Madrid F., et al. Structure-function relationship and role of tumor necrosis factor-alpha-converting enzyme in the down-regulation of L-selectin by non-steroidal anti-inflammatory drugs. J Biol Chem 277 (2002) 38212-38221
    • (2002) J Biol Chem , vol.277 , pp. 38212-38221
    • Gomez-Gaviro, M.V.1    Gonzalez-Alvaro, I.2    Dominguez-Jimenez, C.3    Peschon, J.4    Black, R.A.5    Sanchez-Madrid, F.6
  • 58
    • 44449127592 scopus 로고    scopus 로고
    • The epidermal growth factor receptor family: biology driving targeted therapeutics
    • Wieduwilt M.J., and Moasser M.M. The epidermal growth factor receptor family: biology driving targeted therapeutics. Cell Mol Life Sci 65 (2008) 1566-1584
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1566-1584
    • Wieduwilt, M.J.1    Moasser, M.M.2
  • 60
    • 33745714456 scopus 로고    scopus 로고
    • ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors
    • Ohtsu H., Dempsey P.J., and Eguchi S. ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors. Am J Physiol Cell Physiol 291 (2006) C1-C10
    • (2006) Am J Physiol Cell Physiol , vol.291
    • Ohtsu, H.1    Dempsey, P.J.2    Eguchi, S.3
  • 61
    • 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 H.M., Higashiyama S., Peschon J., et al. Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands. J Cell Biol 164 (2004) 769-779
    • (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
  • 62
    • 33845729910 scopus 로고    scopus 로고
    • Ectodomain shedding of the EGF-receptor ligand epigen is mediated by ADAM17
    • Sahin U., and Blobel C.P. Ectodomain shedding of the EGF-receptor ligand epigen is mediated by ADAM17. FEBS Lett 581 (2007) 41-44
    • (2007) FEBS Lett , vol.581 , pp. 41-44
    • Sahin, U.1    Blobel, C.P.2
  • 63
    • 0037507267 scopus 로고    scopus 로고
    • Defective valvulogenesis in HB-EGF and TACE-null mice is associated with aberrant BMP signaling
    • Jackson L.F., Qiu T.H., Sunnarborg S.W., Chang A., Zhang C., Patterson C., et al. Defective valvulogenesis in HB-EGF and TACE-null mice is associated with aberrant BMP signaling. EMBO J 22 (2003) 2704-2716
    • (2003) EMBO J , vol.22 , pp. 2704-2716
    • Jackson, L.F.1    Qiu, T.H.2    Sunnarborg, S.W.3    Chang, A.4    Zhang, C.5    Patterson, C.6
  • 64
    • 26244464287 scopus 로고    scopus 로고
    • Mammary ductal morphogenesis requires paracrine activation of stromal EGFR via ADAM17-dependent shedding of epithelial amphiregulin
    • Sternlicht M.D., Sunnarborg S.W., Kouros-Mehr H., Yu Y., Lee D.C., and Werb Z. Mammary ductal morphogenesis requires paracrine activation of stromal EGFR via ADAM17-dependent shedding of epithelial amphiregulin. Development 132 (2005) 3923-3933
    • (2005) Development , vol.132 , pp. 3923-3933
    • Sternlicht, M.D.1    Sunnarborg, S.W.2    Kouros-Mehr, H.3    Yu, Y.4    Lee, D.C.5    Werb, Z.6
  • 65
    • 33846056925 scopus 로고    scopus 로고
    • Substrate selectivity of epidermal growth factor-receptor ligand sheddases and their regulation by phorbol esters and calcium influx
    • Horiuchi K., Le Gall S., Schulte M., Yamaguchi T., Reiss K., Murphy G., et al. Substrate selectivity of epidermal growth factor-receptor ligand sheddases and their regulation by phorbol esters and calcium influx. Mol Biol Cell 18 (2007) 176-188
    • (2007) Mol Biol Cell , vol.18 , pp. 176-188
    • Horiuchi, K.1    Le Gall, S.2    Schulte, M.3    Yamaguchi, T.4    Reiss, K.5    Murphy, G.6
  • 66
    • 0041355557 scopus 로고    scopus 로고
    • Notch and Presenilin: regulated intramembrane proteolysis links development and degeneration
    • Selkoe D., and Kopan R. Notch and Presenilin: regulated intramembrane proteolysis links development and degeneration. Annu Rev Neurosci 26 (2003) 565-597
    • (2003) Annu Rev Neurosci , vol.26 , pp. 565-597
    • Selkoe, D.1    Kopan, R.2
  • 67
    • 2942557122 scopus 로고    scopus 로고
    • Gamma-secretase: proteasome of the membrane?
    • Kopan R., and Ilagan M.X. Gamma-secretase: proteasome of the membrane?. Nat Rev Mol Cell Biol 5 (2004) 499-504
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 499-504
    • Kopan, R.1    Ilagan, M.X.2
  • 68
    • 33747623018 scopus 로고    scopus 로고
    • Notch signalling: a simple pathway becomes complex
    • Bray S.J. Notch signalling: a simple pathway becomes complex. Nat Rev Mol Cell Biol 7 (2006) 678-689
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 678-689
    • Bray, S.J.1
  • 69
    • 0030003538 scopus 로고    scopus 로고
    • Signal transduction by activated mNotch: importance of proteolytic processing and its regulation by the extracellular domain
    • Kopan R., Schroeter E.H., Weintraub H., and Nye J.S. Signal transduction by activated mNotch: importance of proteolytic processing and its regulation by the extracellular domain. Proc Natl Acad Sci U S A 93 (1996) 1683-1688
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 1683-1688
    • Kopan, R.1    Schroeter, E.H.2    Weintraub, H.3    Nye, J.S.4
  • 70
    • 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 J.R., et al. A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE. Mol Cell 5 (2000) 207-216
    • (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
  • 71
    • 0033867521 scopus 로고    scopus 로고
    • A ligand-induced extracellular cleavage regulates gamma-secretase-like proteolytic activation of Notch1
    • Mumm J.S., Schroeter E.H., Saxena M.T., Griesemer A., Tian X., Pan D.J., et al. A ligand-induced extracellular cleavage regulates gamma-secretase-like proteolytic activation of Notch1. Mol Cell 5 (2000) 197-206
    • (2000) Mol Cell , vol.5 , pp. 197-206
    • Mumm, J.S.1    Schroeter, E.H.2    Saxena, M.T.3    Griesemer, A.4    Tian, X.5    Pan, D.J.6
  • 72
    • 0037080699 scopus 로고    scopus 로고
    • kuzbanian-mediated cleavage of Drosophila Notch
    • Lieber T., Kidd S., and Young M.W. kuzbanian-mediated cleavage of Drosophila Notch. Genes Dev 16 (2002) 209-221
    • (2002) Genes Dev , vol.16 , pp. 209-221
    • Lieber, T.1    Kidd, S.2    Young, M.W.3
  • 73
    • 0036796421 scopus 로고    scopus 로고
    • The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for alpha-secretase activity in fibroblasts
    • Hartmann D., de Strooper B., Serneels L., Craessaerts K., Herreman A., Annaert W., et al. The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for alpha-secretase activity in fibroblasts. Hum Mol Genet 11 (2002) 2615-2624
    • (2002) Hum Mol Genet , vol.11 , pp. 2615-2624
    • Hartmann, D.1    de Strooper, B.2    Serneels, L.3    Craessaerts, K.4    Herreman, A.5    Annaert, W.6
  • 74
    • 53749096966 scopus 로고    scopus 로고
    • ADAM10 is essential for proteolytic activation of Notch during thymocyte development
    • Tian L., Wu X., Chi C., Han M., Xu T., and Zhuang Y. ADAM10 is essential for proteolytic activation of Notch during thymocyte development. Int Immunol 20 (2008) 1181-1187
    • (2008) Int Immunol , vol.20 , pp. 1181-1187
    • Tian, L.1    Wu, X.2    Chi, C.3    Han, M.4    Xu, T.5    Zhuang, Y.6
  • 75
    • 0037424348 scopus 로고    scopus 로고
    • The Notch ligands, Delta1 and Jagged2, are substrates for presenilin-dependent "gamma-secretase" cleavage
    • Ikeuchi T., and Sisodia S.S. The Notch ligands, Delta1 and Jagged2, are substrates for presenilin-dependent "gamma-secretase" cleavage. J Biol Chem 278 (2003) 7751-7754
    • (2003) J Biol Chem , vol.278 , pp. 7751-7754
    • Ikeuchi, T.1    Sisodia, S.S.2
  • 76
    • 0038610845 scopus 로고    scopus 로고
    • The Notch ligand Delta1 is sequentially cleaved by an ADAM protease and gamma-secretase
    • Six E., Ndiaye D., Laabi Y., Brou C., Gupta-Rossi N., Israel A., et al. The Notch ligand Delta1 is sequentially cleaved by an ADAM protease and gamma-secretase. Proc Natl Acad Sci U S A 100 (2003) 7638-7643
    • (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    Israel, A.6
  • 78
    • 0029841562 scopus 로고    scopus 로고
    • Increased activity-regulating and neuroprotective efficacy of alpha-secretase-derived secreted amyloid precursor protein conferred by a C-terminal heparin-binding domain
    • Furukawa K., Sopher B.L., Rydel R.E., Begley J.G., Pham D.G., Martin G.M., et al. Increased activity-regulating and neuroprotective efficacy of alpha-secretase-derived secreted amyloid precursor protein conferred by a C-terminal heparin-binding domain. J Neurochem 67 (1996) 1882-1896
    • (1996) J Neurochem , vol.67 , pp. 1882-1896
    • Furukawa, K.1    Sopher, B.L.2    Rydel, R.E.3    Begley, J.G.4    Pham, D.G.5    Martin, G.M.6
  • 79
    • 0035955693 scopus 로고    scopus 로고
    • The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner
    • Kimberly W.T., Zheng J.B., Guenette S.Y., and Selkoe D.J. The intracellular domain of the beta-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner. J Biol Chem 276 (2001) 40288-40292
    • (2001) J Biol Chem , vol.276 , pp. 40288-40292
    • Kimberly, W.T.1    Zheng, J.B.2    Guenette, S.Y.3    Selkoe, D.J.4
  • 80
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao X., and Sudhof T.C. A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 293 (2001) 115-120
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 81
    • 0035909901 scopus 로고    scopus 로고
    • The gamma-secretase-cleaved C-terminal fragment of amyloid precursor protein mediates signaling to the nucleus
    • Gao Y., and Pimplikar S.W. The gamma-secretase-cleaved C-terminal fragment of amyloid precursor protein mediates signaling to the nucleus. Proc Natl Acad Sci U S A 98 (2001) 14979-14984
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 14979-14984
    • Gao, Y.1    Pimplikar, S.W.2
  • 82
    • 33645218231 scopus 로고    scopus 로고
    • A dominant role for FE65 (APBB1) in nuclear signaling
    • Yang Z., Cool B.H., Martin G.M., and Hu Q. A dominant role for FE65 (APBB1) in nuclear signaling. J Biol Chem 281 (2006) 4207-4214
    • (2006) J Biol Chem , vol.281 , pp. 4207-4214
    • Yang, Z.1    Cool, B.H.2    Martin, G.M.3    Hu, Q.4
  • 83
    • 2642582435 scopus 로고    scopus 로고
    • Dissection of amyloid-beta precursor protein-dependent transcriptional transactivation
    • Cao X., and Sudhof T.C. Dissection of amyloid-beta precursor protein-dependent transcriptional transactivation. J Biol Chem 279 (2004) 24601-24611
    • (2004) J Biol Chem , vol.279 , pp. 24601-24611
    • Cao, X.1    Sudhof, T.C.2
  • 84
    • 42149165496 scopus 로고    scopus 로고
    • A closer look at alpha-secretase
    • Postina R. A closer look at alpha-secretase. Curr Alzheimer Res 5 (2008) 179-186
    • (2008) Curr Alzheimer Res , vol.5 , pp. 179-186
    • Postina, R.1
  • 85
    • 0036170534 scopus 로고    scopus 로고
    • Mice lacking the metalloprotease-disintegrin MDC9 (ADAM9) have no evident major abnormalities during development or adult life
    • Weskamp G., Cai H., Brodie T.A., Higashyama S., Manova K., Ludwig T., et al. Mice lacking the metalloprotease-disintegrin MDC9 (ADAM9) have no evident major abnormalities during development or adult life. Mol Cell Biol 22 (2002) 1537-1544
    • (2002) Mol Cell Biol , vol.22 , pp. 1537-1544
    • Weskamp, G.1    Cai, H.2    Brodie, T.A.3    Higashyama, S.4    Manova, K.5    Ludwig, T.6
  • 86
    • 0034961544 scopus 로고    scopus 로고
    • Astrocyte and endothelial cell expression of ADAM 17 (TACE) in adult human CNS
    • Goddard D.R., Bunning R.A., and Woodroofe M.N. Astrocyte and endothelial cell expression of ADAM 17 (TACE) in adult human CNS. Glia 34 (2001) 267-271
    • (2001) Glia , vol.34 , pp. 267-271
    • Goddard, D.R.1    Bunning, R.A.2    Woodroofe, M.N.3
  • 87
    • 0033793248 scopus 로고    scopus 로고
    • Coordinated expression of beta-amyloid precursor protein and the putative beta-secretase BACE and alpha-secretase ADAM10 in mouse and human brain
    • Marcinkiewicz M., and Seidah N.G. Coordinated expression of beta-amyloid precursor protein and the putative beta-secretase BACE and alpha-secretase ADAM10 in mouse and human brain. J Neurochem 75 (2000) 2133-2143
    • (2000) J Neurochem , vol.75 , pp. 2133-2143
    • Marcinkiewicz, M.1    Seidah, N.G.2
  • 88
    • 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., and Huovila A.P. Metalloprotease-disintegrin (ADAM) genes are widely and differentially expressed in the adult CNS. Mol Cell Neurosci 15 (2000) 547-560
    • (2000) Mol Cell Neurosci , vol.15 , pp. 547-560
    • Karkkainen, I.1    Rybnikova, E.2    Pelto-Huikko, M.3    Huovila, A.P.4
  • 89
    • 85047690140 scopus 로고    scopus 로고
    • A disintegrin-metalloproteinase 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-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model. J Clin Invest 113 (2004) 1456-1464
    • (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
  • 91
    • 1942533555 scopus 로고    scopus 로고
    • Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death
    • Naus S., Richter M., Wildeboer D., Moss M., Schachner M., and Bartsch J.W. Ectodomain shedding of the neural recognition molecule CHL1 by the metalloprotease-disintegrin ADAM8 promotes neurite outgrowth and suppresses neuronal cell death. J Biol Chem 279 (2004) 16083-16090
    • (2004) J Biol Chem , vol.279 , pp. 16083-16090
    • Naus, S.1    Richter, M.2    Wildeboer, D.3    Moss, M.4    Schachner, M.5    Bartsch, J.W.6
  • 92
    • 17444373968 scopus 로고    scopus 로고
    • A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor
    • Izumi Y., Hirata M., Hasuwa H., Iwamoto R., Umata T., Miyado K., et al. A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor. EMBO J 17 (1998) 7260-7272
    • (1998) EMBO J , vol.17 , pp. 7260-7272
    • Izumi, Y.1    Hirata, M.2    Hasuwa, H.3    Iwamoto, R.4    Umata, T.5    Miyado, K.6
  • 93
    • 0033569653 scopus 로고    scopus 로고
    • Membrane-anchored metalloprotease MDC9 has an alpha-secretase activity responsible for processing the amyloid precursor protein
    • Koike H., Tomioka S., Sorimachi H., Saido T.C., Maruyama K., Okuyama A., et al. Membrane-anchored metalloprotease MDC9 has an alpha-secretase activity responsible for processing the amyloid precursor protein. Biochem J 343 Pt 2 (1999) 371-375
    • (1999) Biochem J , vol.343 , Issue.PART 2 , pp. 371-375
    • Koike, H.1    Tomioka, S.2    Sorimachi, H.3    Saido, T.C.4    Maruyama, K.5    Okuyama, A.6
  • 94
    • 0029788321 scopus 로고    scopus 로고
    • KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis
    • Rooke J., Pan D., Xu T., and Rubin G.M. KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis. Science 273 (1996) 1227-1231
    • (1996) Science , vol.273 , pp. 1227-1231
    • Rooke, J.1    Pan, D.2    Xu, T.3    Rubin, G.M.4
  • 95
    • 0033678817 scopus 로고    scopus 로고
    • Analysis for transcript expression of meltrin alpha in normal, regenerating, and denervated rat muscle
    • Borneman A., Kuschel R., and Fujisawa-Sehara A. Analysis for transcript expression of meltrin alpha in normal, regenerating, and denervated rat muscle. J Muscle Res Cell Motil 21 (2000) 475-480
    • (2000) J Muscle Res Cell Motil , vol.21 , pp. 475-480
    • Borneman, A.1    Kuschel, R.2    Fujisawa-Sehara, A.3
  • 96
    • 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 beta1 and beta2
    • Horiuchi K., Zhou H.M., Kelly K., Manova K., and Blobel C.P. Evaluation of the contributions of ADAMs 9, 12, 15, 17, and 19 to heart development and ectodomain shedding of neuregulins beta1 and beta2. Dev Biol 283 (2005) 459-471
    • (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
  • 97
    • 15444378403 scopus 로고    scopus 로고
    • Role of meltrin {alpha} (ADAM12) in obesity induced by high-fat diet
    • Masaki M., Kurisaki T., Shirakawa K., and Sehara-Fujisawa A. Role of meltrin {alpha} (ADAM12) in obesity induced by high-fat diet. Endocrinology 146 (2005) 1752-1763
    • (2005) Endocrinology , vol.146 , pp. 1752-1763
    • Masaki, M.1    Kurisaki, T.2    Shirakawa, K.3    Sehara-Fujisawa, A.4
  • 98
  • 99
    • 17244371476 scopus 로고    scopus 로고
    • Homeostatic effects of the metalloproteinase disintegrin ADAM15 in degenerative cartilage remodeling
    • Bohm B.B., Aigner T., Roy B., Brodie T.A., Blobel C.P., and Burkhardt H. Homeostatic effects of the metalloproteinase disintegrin ADAM15 in degenerative cartilage remodeling. Arthritis Rheum 52 (2005) 1100-1109
    • (2005) Arthritis Rheum , vol.52 , pp. 1100-1109
    • Bohm, B.B.1    Aigner, T.2    Roy, B.3    Brodie, T.A.4    Blobel, C.P.5    Burkhardt, H.6
  • 103
    • 33749038646 scopus 로고    scopus 로고
    • Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate synaptic transmission
    • Fukata Y., Adesnik H., Iwanaga T., Bredt D.S., Nicoll R.A., and Fukata M. Epilepsy-related ligand/receptor complex LGI1 and ADAM22 regulate synaptic transmission. Science 313 (2006) 1792-1795
    • (2006) Science , vol.313 , pp. 1792-1795
    • Fukata, Y.1    Adesnik, H.2    Iwanaga, T.3    Bredt, D.S.4    Nicoll, R.A.5    Fukata, M.6
  • 104
    • 8444253005 scopus 로고    scopus 로고
    • Aberrant alternative exon use and increased copy number of human metalloprotease-disintegrin ADAM15 gene in breast cancer cells
    • Ortiz R.M., Karkkainen I., and Huovila A.P. Aberrant alternative exon use and increased copy number of human metalloprotease-disintegrin ADAM15 gene in breast cancer cells. Genes Chromosomes Cancer 41 (2004) 366-378
    • (2004) Genes Chromosomes Cancer , vol.41 , pp. 366-378
    • Ortiz, R.M.1    Karkkainen, I.2    Huovila, A.P.3
  • 105
    • 0141788294 scopus 로고    scopus 로고
    • Structure and expression of the murine ADAM 15 gene and its splice variants, and difference of interaction between their cytoplasmic domains and Src family proteins
    • Shimizu E., Yasui A., Matsuura K., Hijiya N., Higuchi Y., and Yamamoto S. Structure and expression of the murine ADAM 15 gene and its splice variants, and difference of interaction between their cytoplasmic domains and Src family proteins. Biochem Biophys Res Commun 309 (2003) 779-785
    • (2003) Biochem Biophys Res Commun , vol.309 , pp. 779-785
    • Shimizu, E.1    Yasui, A.2    Matsuura, K.3    Hijiya, N.4    Higuchi, Y.5    Yamamoto, S.6
  • 106
    • 33749504736 scopus 로고    scopus 로고
    • MicroRNAs and the hallmarks of cancer
    • Dalmay T., and Edwards D.R. MicroRNAs and the hallmarks of cancer. Oncogene 25 (2006) 6170-6175
    • (2006) Oncogene , vol.25 , pp. 6170-6175
    • Dalmay, T.1    Edwards, D.R.2
  • 107
    • 10744233182 scopus 로고    scopus 로고
    • Substrate specificity and inducibility of TACE (tumour necrosis factor alpha-converting enzyme) revisited: the Ala-Val preference, and induced intrinsic activity
    • Black R.A., Doedens J.R., Mahimkar R., Johnson R., Guo L., Wallace A., et al. Substrate specificity and inducibility of TACE (tumour necrosis factor alpha-converting enzyme) revisited: the Ala-Val preference, and induced intrinsic activity. Biochem Soc Symp (2003) 39-52
    • (2003) Biochem Soc Symp , pp. 39-52
    • Black, R.A.1    Doedens, J.R.2    Mahimkar, R.3    Johnson, R.4    Guo, L.5    Wallace, A.6
  • 110
    • 2942567828 scopus 로고    scopus 로고
    • Therapeutic benefits from targeting of ADAM family members
    • Moss M.L., and Bartsch J.W. Therapeutic benefits from targeting of ADAM family members. Biochemistry 43 (2004) 7227-7235
    • (2004) Biochemistry , vol.43 , pp. 7227-7235
    • Moss, M.L.1    Bartsch, J.W.2
  • 112
    • 0033213984 scopus 로고    scopus 로고
    • The shedding of membrane-anchored heparin-binding epidermal-like growth factor is regulated by the Raf/mitogen-activated protein kinase cascade and by cell adhesion and spreading
    • Gechtman Z., Alonso J.L., Raab G., Ingber D.E., and Klagsbrun M. The shedding of membrane-anchored heparin-binding epidermal-like growth factor is regulated by the Raf/mitogen-activated protein kinase cascade and by cell adhesion and spreading. J Biol Chem 274 (1999) 28828-28835
    • (1999) J Biol Chem , vol.274 , pp. 28828-28835
    • Gechtman, Z.1    Alonso, J.L.2    Raab, G.3    Ingber, D.E.4    Klagsbrun, M.5
  • 113
    • 0036882397 scopus 로고    scopus 로고
    • Protein ectodomain shedding
    • Arribas J., and Borroto A. Protein ectodomain shedding. Chem Rev 102 (2002) 4627-4638
    • (2002) Chem Rev , vol.102 , pp. 4627-4638
    • Arribas, J.1    Borroto, A.2
  • 114
    • 0037073668 scopus 로고    scopus 로고
    • The metalloprotease disintegrin ADAM8. Processing by autocatalysis is required for proteolytic activity and cell adhesion
    • Schlomann U., Wildeboer D., Webster A., Antropova O., Zeuschner D., Knight C.G., et al. The metalloprotease disintegrin ADAM8. Processing by autocatalysis is required for proteolytic activity and cell adhesion. J Biol Chem 277 (2002) 48210-48219
    • (2002) J Biol Chem , vol.277 , pp. 48210-48219
    • Schlomann, U.1    Wildeboer, D.2    Webster, A.3    Antropova, O.4    Zeuschner, D.5    Knight, C.G.6
  • 115
    • 33645020188 scopus 로고    scopus 로고
    • Identification of candidate substrates for ectodomain shedding by the metalloprotease-disintegrin ADAM8
    • Naus S., Reipschlager S., Wildeboer D., Lichtenthaler S.F., Mitterreiter S., Guan Z., et al. Identification of candidate substrates for ectodomain shedding by the metalloprotease-disintegrin ADAM8. Biol Chem 387 (2006) 337-346
    • (2006) Biol Chem , vol.387 , pp. 337-346
    • Naus, S.1    Reipschlager, S.2    Wildeboer, D.3    Lichtenthaler, S.F.4    Mitterreiter, S.5    Guan, Z.6
  • 116
    • 0042232590 scopus 로고    scopus 로고
    • Catalytic activity of ADAM8, ADAM15, and MDC-L (ADAM28) on synthetic peptide substrates and in ectodomain cleavage of CD23
    • Fourie A.M., Coles F., Moreno V., and Karlsson L. Catalytic activity of ADAM8, ADAM15, and MDC-L (ADAM28) on synthetic peptide substrates and in ectodomain cleavage of CD23. J Biol Chem 278 (2003) 30469-30477
    • (2003) J Biol Chem , vol.278 , pp. 30469-30477
    • Fourie, A.M.1    Coles, F.2    Moreno, V.3    Karlsson, L.4
  • 117
    • 34250181263 scopus 로고    scopus 로고
    • Expression and regulation of the metalloproteinase ADAM-8 during human neutrophil pathophysiological activation and its catalytic activity on L-selectin shedding
    • Gomez-Gaviro M., Dominguez-Luis M., Canchado J., Calafat J., Janssen H., Lara-Pezzi E., et al. Expression and regulation of the metalloproteinase ADAM-8 during human neutrophil pathophysiological activation and its catalytic activity on L-selectin shedding. J Immunol 178 (2007) 8053-8063
    • (2007) J Immunol , vol.178 , pp. 8053-8063
    • Gomez-Gaviro, M.1    Dominguez-Luis, M.2    Canchado, J.3    Calafat, J.4    Janssen, H.5    Lara-Pezzi, E.6
  • 119
    • 18644384411 scopus 로고    scopus 로고
    • Transmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMs
    • Franzke C.W., Tasanen K., Schacke 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 (2002) 5026-5035
    • (2002) EMBO J , vol.21 , pp. 5026-5035
    • Franzke, C.W.1    Tasanen, K.2    Schacke, H.3    Zhou, Z.4    Tryggvason, K.5    Mauch, C.6
  • 121
    • 0037168495 scopus 로고    scopus 로고
    • ADAM-9 is an insulin-like growth factor binding protein-5 protease produced and secreted by human osteoblasts
    • Mohan S., Thompson G.R., Amaar Y.G., Hathaway G., Tschesche H., and Baylink D.J. ADAM-9 is an insulin-like growth factor binding protein-5 protease produced and secreted by human osteoblasts. Biochemistry 41 (2002) 15394-15403
    • (2002) Biochemistry , vol.41 , pp. 15394-15403
    • Mohan, S.1    Thompson, G.R.2    Amaar, Y.G.3    Hathaway, G.4    Tschesche, H.5    Baylink, D.J.6
  • 123
    • 19644367756 scopus 로고    scopus 로고
    • A secreted form of ADAM9 promotes carcinoma invasion through tumor-stromal interactions
    • Mazzocca A., Coppari R., De Franco R., Cho J.Y., Libermann T.A., Pinzani M., et al. A secreted form of ADAM9 promotes carcinoma invasion through tumor-stromal interactions. Cancer Res 65 (2005) 4728-4738
    • (2005) Cancer Res , vol.65 , pp. 4728-4738
    • Mazzocca, A.1    Coppari, R.2    De Franco, R.3    Cho, J.Y.4    Libermann, T.A.5    Pinzani, M.6
  • 124
    • 4644367922 scopus 로고    scopus 로고
    • Natural soluble interleukin-15Ralpha is generated by cleavage that involves the tumor necrosis factor-alpha-converting enzyme (TACE/ADAM17)
    • Budagian V., Bulanova E., Orinska Z., Ludwig A., Rose-John S., Saftig P., et al. Natural soluble interleukin-15Ralpha is generated by cleavage that involves the tumor necrosis factor-alpha-converting enzyme (TACE/ADAM17). J Biol Chem 279 (2004) 40368-40375
    • (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    Saftig, P.6
  • 125
    • 33846285347 scopus 로고    scopus 로고
    • ADAM10 is a principal 'sheddase' of the low-affinity immunoglobulin E receptor CD23
    • Weskamp G., Ford J.W., Sturgill J., Martin S., Docherty A.J., Swendeman S., et al. ADAM10 is a principal 'sheddase' of the low-affinity immunoglobulin E receptor CD23. Nat Immunol 7 (2006) 1293-1298
    • (2006) Nat Immunol , vol.7 , pp. 1293-1298
    • Weskamp, G.1    Ford, J.W.2    Sturgill, J.3    Martin, S.4    Docherty, A.J.5    Swendeman, S.6
  • 127
    • 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
    • Nagano O., Murakami D., Hartmann D., de Strooper B., Saftig P., Iwatsubo T., et al. 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 (2004) 893-902
    • (2004) J Cell Biol , vol.165 , pp. 893-902
    • Nagano, O.1    Murakami, D.2    Hartmann, D.3    de Strooper, B.4    Saftig, P.5    Iwatsubo, T.6
  • 128
    • 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 (2001) 37743-37746
    • (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
  • 129
    • 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 O.R., Ister D., Pennington C.J., Hauser S., et al. Tissue inhibitor of metalloproteinases-1 promotes liver metastasis by induction of hepatocyte growth factor signaling. Cancer Res 67 (2007) 8615-8623
    • (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
  • 130
    • 0032540170 scopus 로고    scopus 로고
    • The metallo-disintegrin ADAM10 (MADM) from bovine kidney has type IV collagenase activity in vitro
    • Millichip M.I., Dallas D.J., Wu E., Dale S., and McKie N. The metallo-disintegrin ADAM10 (MADM) from bovine kidney has type IV collagenase activity in vitro. Biochem Biophys Res Commun 245 (1998) 594-598
    • (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
  • 131
    • 0042237924 scopus 로고    scopus 로고
    • The disintegrin-like metalloproteinase ADAM10 is involved in constitutive cleavage of CX3CL1 (fractalkine) and regulates CX3CL1-mediated cell-cell adhesion
    • Hundhausen C., Misztela D., Berkhout T.A., Broadway N., Saftig P., Reiss K., et al. The disintegrin-like metalloproteinase ADAM10 is involved in constitutive cleavage of CX3CL1 (fractalkine) and regulates CX3CL1-mediated cell-cell adhesion. Blood 102 (2003) 1186-1195
    • (2003) Blood , vol.102 , pp. 1186-1195
    • Hundhausen, C.1    Misztela, D.2    Berkhout, T.A.3    Broadway, N.4    Saftig, P.5    Reiss, K.6
  • 132
    • 33745477470 scopus 로고    scopus 로고
    • Proteomic identification of desmoglein 2 and activated leukocyte cell adhesion molecule as substrates of ADAM17 and ADAM10 by difference gel electrophoresis
    • Bech-Serra J.J., Santiago-Josefat B., Esselens C., Saftig P., Baselga J., Arribas J., et al. Proteomic identification of desmoglein 2 and activated leukocyte cell adhesion molecule as substrates of ADAM17 and ADAM10 by difference gel electrophoresis. Mol Cell Biol 26 (2006) 5086-5095
    • (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
  • 133
    • 33745765680 scopus 로고    scopus 로고
    • Identification of ADAM10 as a major source of HER2 ectodomain sheddase activity in HER2 overexpressing breast cancer cells
    • Liu P.C., 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 (2006) 657-664
    • (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
  • 134
    • 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 (2007) 1040-1049
    • (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
  • 135
    • 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., Schutze 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 (2003) 38829-38839
    • (2003) J Biol Chem , vol.278 , pp. 38829-38839
    • Matthews, V.1    Schuster, B.2    Schutze, S.3    Bussmeyer, I.4    Ludwig, A.5    Hundhausen, C.6
  • 136
    • 38049144010 scopus 로고    scopus 로고
    • Insulin stimulates the cleavage and release of the extracellular domain of Klotho by ADAM10 and ADAM17
    • Chen C.D., Podvin S., Gillespie E., Leeman S.E., and Abraham C.R. Insulin stimulates the cleavage and release of the extracellular domain of Klotho by ADAM10 and ADAM17. Proc Natl Acad Sci U S A 104 (2007) 19796-19801
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 19796-19801
    • Chen, C.D.1    Podvin, S.2    Gillespie, E.3    Leeman, S.E.4    Abraham, C.R.5
  • 137
    • 33846551969 scopus 로고    scopus 로고
    • Metalloproteases regulate T-cell proliferation and effector function via LAG-3
    • Li N., Wang Y., Forbes K., Vignali K.M., Heale B.S., Saftig P., et al. Metalloproteases regulate T-cell proliferation and effector function via LAG-3. EMBO J 26 (2007) 494-504
    • (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
  • 138
    • 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
    • Maretzky T., Schulte M., Ludwig A., Rose-John S., Blobel C., Hartmann D., et al. 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 (2005) 9040-9053
    • (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    Hartmann, D.6
  • 140
    • 37549003693 scopus 로고    scopus 로고
    • Cleavage of the human thyrotropin receptor by ADAM10 is regulated by thyrotropin
    • Kaczur V., Puskas L.G., Nagy Z.U., Miled N., Rebai A., Juhasz F., et al. Cleavage of the human thyrotropin receptor by ADAM10 is regulated by thyrotropin. J Mol Recognit 20 (2007) 392-404
    • (2007) J Mol Recognit , vol.20 , pp. 392-404
    • Kaczur, V.1    Puskas, L.G.2    Nagy, Z.U.3    Miled, N.4    Rebai, A.5    Juhasz, F.6
  • 141
    • 33845994375 scopus 로고    scopus 로고
    • Negative regulation of osteoclastogenesis by ectodomain shedding of receptor activator of NF-kappaB 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-kappaB ligand. J Biol Chem 281 (2006) 36846-36855
    • (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
  • 142
    • 10944263573 scopus 로고    scopus 로고
    • ADAM 12 cleaves extracellular matrix proteins and correlates with cancer status and stage
    • Roy R., Wewer U.M., Zurakowski D., Pories S.E., and Moses M.A. ADAM 12 cleaves extracellular matrix proteins and correlates with cancer status and stage. J Biol Chem 279 (2004) 51323-51330
    • (2004) J Biol Chem , vol.279 , pp. 51323-51330
    • Roy, R.1    Wewer, U.M.2    Zurakowski, D.3    Pories, S.E.4    Moses, M.A.5
  • 143
    • 0036152858 scopus 로고    scopus 로고
    • Cardiac hypertrophy is inhibited by antagonism of ADAM12 processing of HB-EGF: metalloproteinase inhibitors as a new therapy
    • Asakura M., Kitakaze M., Takashima S., Liao Y., Ishikura F., Yoshinaka T., et al. Cardiac hypertrophy is inhibited by antagonism of ADAM12 processing of HB-EGF: metalloproteinase inhibitors as a new therapy. Nat Med 8 (2002) 35-40
    • (2002) Nat Med , vol.8 , pp. 35-40
    • Asakura, M.1    Kitakaze, M.2    Takashima, S.3    Liao, Y.4    Ishikura, F.5    Yoshinaka, T.6
  • 146
    • 0037214312 scopus 로고    scopus 로고
    • Phenotypic analysis of Meltrin alpha (ADAM12)-deficient mice: involvement of Meltrin alpha in adipogenesis and myogenesis
    • Kurisaki T., Masuda A., Sudo K., Sakagami J., Higashiyama S., Matsuda Y., et al. Phenotypic analysis of Meltrin alpha (ADAM12)-deficient mice: involvement of Meltrin alpha in adipogenesis and myogenesis. Mol Cell Biol 23 (2003) 55-61
    • (2003) Mol Cell Biol , vol.23 , pp. 55-61
    • Kurisaki, T.1    Masuda, A.2    Sudo, K.3    Sakagami, J.4    Higashiyama, S.5    Matsuda, Y.6
  • 147
    • 1342322686 scopus 로고    scopus 로고
    • Multiple G-protein-coupled receptor signals converge on the epidermal growth factor receptor to promote migration and invasion
    • Schafer B., Gschwind A., and Ullrich A. Multiple G-protein-coupled receptor signals converge on the epidermal growth factor receptor to promote migration and invasion. Oncogene 23 (2004) 991-999
    • (2004) Oncogene , vol.23 , pp. 991-999
    • Schafer, B.1    Gschwind, A.2    Ullrich, A.3
  • 148
    • 49649103585 scopus 로고    scopus 로고
    • The ectodomain shedding of E-cadherin by ADAM15 supports ErbB receptor activation
    • Najy A.J., Day K.C., and Day M.L. The ectodomain shedding of E-cadherin by ADAM15 supports ErbB receptor activation. J Biol Chem 283 (2008) 18393-18401
    • (2008) J Biol Chem , vol.283 , pp. 18393-18401
    • Najy, A.J.1    Day, K.C.2    Day, M.L.3
  • 149
    • 26844556553 scopus 로고    scopus 로고
    • GPCR-induced migration of breast carcinoma cells depends on both EGFR signal transactivation and EGFR-independent pathways
    • Hart S., Fischer O.M., Prenzel N., Zwick-Wallasch E., Schneider M., Hennighausen L., et al. GPCR-induced migration of breast carcinoma cells depends on both EGFR signal transactivation and EGFR-independent pathways. Biol Chem 386 (2005) 845-855
    • (2005) Biol Chem , vol.386 , pp. 845-855
    • Hart, S.1    Fischer, O.M.2    Prenzel, N.3    Zwick-Wallasch, E.4    Schneider, M.5    Hennighausen, L.6
  • 150
    • 24044444558 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha convertase (ADAM17) mediates regulated ectodomain shedding of the severe-acute respiratory syndrome-coronavirus (SARS-CoV) receptor, angiotensin-converting enzyme-2 (ACE2)
    • Lambert D.W., Yarski M., Warner F.J., Thornhill P., Parkin E.T., Smith A.I., et al. Tumor necrosis factor-alpha 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 (2005) 30113-30119
    • (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
  • 151
    • 14444272986 scopus 로고    scopus 로고
    • Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor
    • Buxbaum J.D., Liu K.N., Luo Y., Slack J.L., Stocking K.L., Peschon J.J., et al. Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor. J Biol Chem 273 (1998) 27765-27767
    • (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
  • 152
    • 0034671566 scopus 로고    scopus 로고
    • CD30 shedding from Karpas 299 lymphoma cells is mediated by TNF-alpha-converting enzyme
    • Hansen H.P., Dietrich S., Kisseleva T., Mokros T., Mentlein R., Lange H.H., et al. CD30 shedding from Karpas 299 lymphoma cells is mediated by TNF-alpha-converting enzyme. J Immunol 165 (2000) 6703-6709
    • (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
  • 153
    • 0042858460 scopus 로고    scopus 로고
    • Membrane-anchored CD40 is processed by the tumor necrosis factor-alpha-converting enzyme. Implications for CD40 signaling
    • Contin C., Pitard V., Itai T., Nagata S., Moreau J.F., and Dechanet-Merville J. Membrane-anchored CD40 is processed by the tumor necrosis factor-alpha-converting enzyme. Implications for CD40 signaling. J Biol Chem 278 (2003) 32801-32809
    • (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    Dechanet-Merville, J.6
  • 154
    • 38449111957 scopus 로고    scopus 로고
    • Cell surface colony-stimulating factor 1 can be cleaved by TNF-alpha converting enzyme or endocytosed in a clathrin-dependent 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-alpha converting enzyme or endocytosed in a clathrin-dependent manner. J Immunol 179 (2007) 6715-6724
    • (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
  • 155
    • 0035851124 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha-converting enzyme (ADAM17) mediates the cleavage and shedding of fractalkine (CX3CL1)
    • Garton K.J., Gough P.J., Blobel C.P., Murphy G., Greaves D.R., Dempsey P.J., et al. Tumor necrosis factor-alpha-converting enzyme (ADAM17) mediates the cleavage and shedding of fractalkine (CX3CL1). J Biol Chem 276 (2001) 37993-38001
    • (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
  • 156
    • 0034616385 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha-converting enzyme is required for cleavage of erbB4/HER4
    • Rio C., Buxbaum J.D., Peschon J.J., and Corfas G. Tumor necrosis factor-alpha-converting enzyme is required for cleavage of erbB4/HER4. J Biol Chem 275 (2000) 10379-10387
    • (2000) J Biol Chem , vol.275 , pp. 10379-10387
    • Rio, C.1    Buxbaum, J.D.2    Peschon, J.J.3    Corfas, G.4
  • 157
    • 0034520154 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha converting enzyme (TACE) is a growth hormone binding protein (GHBP) sheddase: the metalloprotease TACE/ADAM-17 is critical for (PMA-induced) GH receptor proteolysis and GHBP generation
    • Zhang Y., Jiang J., Black R.A., Baumann G., and Frank S.J. Tumor necrosis factor-alpha converting enzyme (TACE) is a growth hormone binding protein (GHBP) sheddase: the metalloprotease TACE/ADAM-17 is critical for (PMA-induced) GH receptor proteolysis and GHBP generation. Endocrinology 141 (2000) 4342-4348
    • (2000) Endocrinology , vol.141 , pp. 4342-4348
    • Zhang, Y.1    Jiang, J.2    Black, R.A.3    Baumann, G.4    Frank, S.J.5
  • 158
    • 34548856204 scopus 로고    scopus 로고
    • Apoptosis is a natural stimulus of IL6R shedding and contributes to the proinflammatory trans-signaling function of neutrophils
    • Chalaris A., Rabe B., Paliga K., Lange H., Laskay T., Fielding C.A., et al. Apoptosis is a natural stimulus of IL6R shedding and contributes to the proinflammatory trans-signaling function of neutrophils. Blood 110 (2007) 1748-1755
    • (2007) Blood , vol.110 , pp. 1748-1755
    • Chalaris, A.1    Rabe, B.2    Paliga, K.3    Lange, H.4    Laskay, T.5    Fielding, C.A.6
  • 159
    • 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 J.D., Toyama Y., Besmer P., and Blobel C.P. 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 (2007) 943-952
    • (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
  • 160
    • 0037474312 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha converting enzyme/ADAM 17 mediates MUC1 shedding
    • Thathiah A., Blobel C.P., and Carson D.D. Tumor necrosis factor-alpha converting enzyme/ADAM 17 mediates MUC1 shedding. J Biol Chem 278 (2003) 3386-3394
    • (2003) J Biol Chem , vol.278 , pp. 3386-3394
    • Thathiah, A.1    Blobel, C.P.2    Carson, D.D.3
  • 161
    • 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., and Kleene R. Proteolytic cleavage of the neural cell adhesion molecule by ADAM17/TACE is involved in neurite outgrowth. J Neurochem 98 (2006) 78-88
    • (2006) J Neurochem , vol.98 , pp. 78-88
    • Kalus, I.1    Bormann, U.2    Mzoughi, M.3    Schachner, M.4    Kleene, R.5
  • 162
    • 21244497783 scopus 로고    scopus 로고
    • Nectin-4, a new serological breast cancer marker, is a substrate for tumor necrosis factor-alpha-converting enzyme (TACE)/ADAM-17
    • Fabre-Lafay S., Garrido-Urbani S., Reymond N., Goncalves A., Dubreuil P., and Lopez M. Nectin-4, a new serological breast cancer marker, is a substrate for tumor necrosis factor-alpha-converting enzyme (TACE)/ADAM-17. J Biol Chem 280 (2005) 19543-19550
    • (2005) J Biol Chem , vol.280 , pp. 19543-19550
    • Fabre-Lafay, S.1    Garrido-Urbani, S.2    Reymond, N.3    Goncalves, A.4    Dubreuil, P.5    Lopez, M.6
  • 163
    • 40849119744 scopus 로고    scopus 로고
    • mGluR1/5-dependent long-term depression requires the regulated ectodomain cleavage of neuronal pentraxin NPR by TACE
    • Cho R.W., Park J.M., Wolff S.B., Xu D., Hopf C., Kim J.A., et al. mGluR1/5-dependent long-term depression requires the regulated ectodomain cleavage of neuronal pentraxin NPR by TACE. Neuron 57 (2008) 858-871
    • (2008) Neuron , vol.57 , pp. 858-871
    • Cho, R.W.1    Park, J.M.2    Wolff, S.B.3    Xu, D.4    Hopf, C.5    Kim, J.A.6
  • 165
    • 33846850498 scopus 로고    scopus 로고
    • Regulated surface expression and shedding support a dual role for semaphorin 4D in platelet responses to vascular injury
    • Zhu L., Bergmeier W., Wu J., Jiang H., Stalker T.J., Cieslak M., et al. Regulated surface expression and shedding support a dual role for semaphorin 4D in platelet responses to vascular injury. Proc Natl Acad Sci U S A 104 (2007) 1621-1626
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 1621-1626
    • Zhu, L.1    Bergmeier, W.2    Wu, J.3    Jiang, H.4    Stalker, T.J.5    Cieslak, M.6
  • 166
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells
    • Black R.A., Rauch C.T., Kozlosky C.J., Peschon J.J., Slack J.L., Wolfson M.F., et al. A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. Nature 385 (1997) 729-733
    • (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    Wolfson, M.F.6
  • 167
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha
    • Moss M.L., Jin S.L., Milla M.E., Bickett D.M., Burkhart W., Carter H.L., et al. Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha. Nature 385 (1997) 733-736
    • (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    Carter, H.L.6
  • 168
    • 0033532191 scopus 로고    scopus 로고
    • Evidence for a role of a tumor necrosis factor-alpha (TNF-alpha)-converting enzyme-like protease in shedding of TRANCE, a TNF family member involved in osteoclastogenesis and dendritic cell survival
    • Lum L., Wong B.R., Josien R., Becherer J.D., Erdjument-Bromage H., Schlondorff J., et al. Evidence for a role of a tumor necrosis factor-alpha (TNF-alpha)-converting enzyme-like protease in shedding of TRANCE, a TNF family member involved in osteoclastogenesis and dendritic cell survival. J Biol Chem 274 (1999) 13613-13618
    • (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    Schlondorff, J.6
  • 169
    • 0035985185 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding
    • Diaz-Rodriguez E., Montero J.C., Esparis-Ogando A., Yuste L., and Pandiella A. Extracellular signal-regulated kinase phosphorylates tumor necrosis factor alpha-converting enzyme at threonine 735: a potential role in regulated shedding. Mol Biol Cell 13 (2002) 2031-2044
    • (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
  • 170
    • 1042278167 scopus 로고    scopus 로고
    • Evidence for a critical role of the tumor necrosis factor alpha convertase (TACE) in ectodomain shedding of the p75 neurotrophin receptor (p75NTR)
    • Weskamp G., Schlondorff J., Lum L., Becherer J.D., Kim T.W., Saftig P., et al. Evidence for a critical role of the tumor necrosis factor alpha convertase (TACE) in ectodomain shedding of the p75 neurotrophin receptor (p75NTR). J Biol Chem 279 (2004) 4241-4249
    • (2004) J Biol Chem , vol.279 , pp. 4241-4249
    • Weskamp, G.1    Schlondorff, J.2    Lum, L.3    Becherer, J.D.4    Kim, T.W.5    Saftig, P.6
  • 171
    • 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., and Sul H.S. 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 (2006) 5421-5435
    • (2006) Mol Cell Biol , vol.26 , pp. 5421-5435
    • Wang, Y.1    Sul, H.S.2
  • 172
    • 33744813041 scopus 로고    scopus 로고
    • EGFR signaling leads to downregulation of PTP-LAR via TACE-mediated proteolytic processing
    • Ruhe J.E., Streit S., Hart S., and Ullrich A. EGFR signaling leads to downregulation of PTP-LAR via TACE-mediated proteolytic processing. Cell Signal 18 (2006) 1515-1527
    • (2006) Cell Signal , vol.18 , pp. 1515-1527
    • Ruhe, J.E.1    Streit, S.2    Hart, S.3    Ullrich, A.4
  • 173
    • 33645763676 scopus 로고    scopus 로고
    • Tumour necrosis factor alpha-converting enzyme mediates ectodomain shedding of Vps10p-domain receptor family members
    • Hermey G., Sjogaard S.S., Petersen C.M., Nykjaer A., and Gliemann J. Tumour necrosis factor alpha-converting enzyme mediates ectodomain shedding of Vps10p-domain receptor family members. Biochem J 395 (2006) 285-293
    • (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
  • 174
    • 0042887604 scopus 로고    scopus 로고
    • TACE is required for fetal murine cardiac development and modeling
    • Shi W., Chen H., Sun J., Buckley S., Zhao J., Anderson K.D., et al. TACE is required for fetal murine cardiac development and modeling. Dev Biol 261 (2003) 371-380
    • (2003) Dev Biol , vol.261 , pp. 371-380
    • Shi, W.1    Chen, H.2    Sun, J.3    Buckley, S.4    Zhao, J.5    Anderson, K.D.6
  • 175
    • 0035313164 scopus 로고    scopus 로고
    • Pulmonary hypoplasia in mice lacking tumor necrosis factor-alpha converting enzyme indicates an indispensable role for cell surface protein shedding during embryonic lung branching morphogenesis
    • Zhao J., Chen H., Peschon J.J., Shi W., Zhang Y., Frank S.J., et al. Pulmonary hypoplasia in mice lacking tumor necrosis factor-alpha converting enzyme indicates an indispensable role for cell surface protein shedding during embryonic lung branching morphogenesis. Dev Biol 232 (2001) 204-218
    • (2001) Dev Biol , vol.232 , pp. 204-218
    • Zhao, J.1    Chen, H.2    Peschon, J.J.3    Shi, W.4    Zhang, Y.5    Frank, S.J.6
  • 178
    • 5644290647 scopus 로고    scopus 로고
    • Evaluation of the contribution of different ADAMs to TNFa shedding and of the function of the TNFa ectodomain in ensuring selective stimulated shedding by the TNFa convertase (TACE/ADAM17)
    • Zheng Y., Saftig P., Hartmann D., and Blobel C. Evaluation of the contribution of different ADAMs to TNFa shedding and of the function of the TNFa ectodomain in ensuring selective stimulated shedding by the TNFa convertase (TACE/ADAM17). J Biol Chem (2004)
    • (2004) J Biol Chem
    • Zheng, Y.1    Saftig, P.2    Hartmann, D.3    Blobel, C.4
  • 179
    • 0037067764 scopus 로고    scopus 로고
    • Intracellular activation of human adamalysin 19/disintegrin and metalloproteinase 19 by furin occurs via one of the two consecutive recognition sites
    • Kang T., Zhao Y.G., Pei D., Sucic J.F., and Sang Q.X. Intracellular activation of human adamalysin 19/disintegrin and metalloproteinase 19 by furin occurs via one of the two consecutive recognition sites. J Biol Chem 277 (2002) 25583-25591
    • (2002) J Biol Chem , vol.277 , pp. 25583-25591
    • Kang, T.1    Zhao, Y.G.2    Pei, D.3    Sucic, J.F.4    Sang, Q.X.5
  • 181
    • 0842308119 scopus 로고    scopus 로고
    • ADAM28 is activated by MMP-7 (matrilysin-1) and cleaves insulin-like growth factor binding protein-3
    • Mochizuki S., Shimoda M., Shiomi T., Fujii Y., and Okada Y. ADAM28 is activated by MMP-7 (matrilysin-1) and cleaves insulin-like growth factor binding protein-3. Biochem Biophys Res Commun 315 (2004) 79-84
    • (2004) Biochem Biophys Res Commun , vol.315 , pp. 79-84
    • Mochizuki, S.1    Shimoda, M.2    Shiomi, T.3    Fujii, Y.4    Okada, Y.5
  • 182
    • 34247616080 scopus 로고    scopus 로고
    • Polymorphism R62W results in resistance of CD23 to enzymatic cleavage in cultured cells
    • Meng J.F., McFall C., and Rosenwasser L.J. Polymorphism R62W results in resistance of CD23 to enzymatic cleavage in cultured cells. Genes Immun 8 (2007) 215-223
    • (2007) Genes Immun , vol.8 , pp. 215-223
    • Meng, J.F.1    McFall, C.2    Rosenwasser, L.J.3
  • 184
    • 33748676135 scopus 로고    scopus 로고
    • ADAM33 is not essential for growth and development and does not modulate allergic asthma in mice
    • Chen C., Huang X., and Sheppard D. ADAM33 is not essential for growth and development and does not modulate allergic asthma in mice. Mol Cell Biol 26 (2006) 6950-6956
    • (2006) Mol Cell Biol , vol.26 , pp. 6950-6956
    • Chen, C.1    Huang, X.2    Sheppard, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.