메뉴 건너뛰기




Volumn 30, Issue 7, 2005, Pages 413-422

Shedding light on ADAM metalloproteinases

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; BATIMASTAT; GROWTH FACTOR; MARIMASTAT; METALLOPROTEINASE; NOTCH RECEPTOR; PROTEIN INHIBITOR; TUMOR NECROSIS FACTOR ALPHA CONVERTING ENZYME;

EID: 21744443240     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2005.05.006     Document Type: Review
Times cited : (393)

References (83)
  • 1
    • 0141533033 scopus 로고    scopus 로고
    • ADAMs: Modulators of cell-cell and cell-matrix interactions
    • J.M. White 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
  • 2
    • 11244261160 scopus 로고    scopus 로고
    • ADAMs: Key components in EGFR signalling and development
    • C.P. Blobel 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
    • 0037224740 scopus 로고    scopus 로고
    • The ADAMs family of metalloproteases: Multidomain proteins with multiple functions
    • D.F. Seals, and S.A. Courtneidge 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
  • 4
    • 0036007414 scopus 로고    scopus 로고
    • Shedding light on sheddases: Role in growth and development
    • F. Kheradmand, and Z. Werb Shedding light on sheddases: role in growth and development Bioessays 24 2002 8 12
    • (2002) Bioessays , vol.24 , pp. 8-12
    • Kheradmand, F.1    Werb, Z.2
  • 5
    • 10744233182 scopus 로고    scopus 로고
    • Substrate specificity and inducibility of TACE (tumour necrosis factor α-converting enzyme) revisited: The Ala-Val preference, and induced intrinsic activity
    • R.A. Black Substrate specificity and inducibility of TACE (tumour necrosis factor α-converting enzyme) revisited: the Ala-Val preference, and induced intrinsic activity Biochem. Soc. Symp. 70 2003 39 52
    • (2003) Biochem. Soc. Symp. , vol.70 , pp. 39-52
    • Black, R.A.1
  • 6
    • 0043272529 scopus 로고    scopus 로고
    • Biochemical properties and functions of membrane-anchored metalloprotease-disintegrin proteins (ADAMs)
    • J.D. Becherer, and C.P. Blobel Biochemical properties and functions of membrane-anchored metalloprotease-disintegrin proteins (ADAMs) Curr. Top. Dev. Biol. 54 2003 101 123
    • (2003) Curr. Top. Dev. Biol. , vol.54 , pp. 101-123
    • Becherer, J.D.1    Blobel, C.P.2
  • 7
    • 2942567828 scopus 로고    scopus 로고
    • Therapeutic benefits from targeting of ADAM family members
    • M.L. Moss, and J.W. Bartsch 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
  • 8
    • 0032515018 scopus 로고    scopus 로고
    • An essential role for ectodomain shedding in mammalian development
    • J.J. Peschon An essential role for ectodomain shedding in mammalian development Science 282 1998 1281 1284
    • (1998) Science , vol.282 , pp. 1281-1284
    • Peschon, J.J.1
  • 9
    • 0035313164 scopus 로고    scopus 로고
    • Pulmonary hypoplasia in mice lacking tumor necrosis factor-α converting enzyme indicates an indispensable role for cell surface protein shedding during embryonic lung branching morphogenesis
    • J. Zhao Pulmonary hypoplasia in mice lacking tumor necrosis factor-α 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
  • 10
    • 0037507267 scopus 로고    scopus 로고
    • Defective valvulogenesis in HB-EGF and TACE-null mice is associated with aberrant BMP signaling
    • L.F. Jackson 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
  • 11
    • 0042887604 scopus 로고    scopus 로고
    • TACE is required for fetal murine cardiac development and modeling
    • W. Shi 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
  • 12
    • 4444229437 scopus 로고    scopus 로고
    • -/- mice leads to chronic hepatic inflammation and failure of liver regeneration
    • -/- mice leads to chronic hepatic inflammation and failure of liver regeneration Nat. Genet. 36 2004 969 977
    • (2004) Nat. Genet. , vol.36 , pp. 969-977
    • Mohammed, F.F.1
  • 13
    • 1442358746 scopus 로고    scopus 로고
    • Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands
    • U. Sahin 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
  • 14
    • 2642541715 scopus 로고    scopus 로고
    • Selective roles for tumor necrosis factor α-converting enzyme/ADAM17 in the shedding of the epidermal growth factor receptor ligand family: The juxtamembrane stalk determines cleavage efficiency
    • C.L. Hinkle Selective roles for tumor necrosis factor α-converting enzyme/ADAM17 in the shedding of the epidermal growth factor receptor ligand family: the juxtamembrane stalk determines cleavage efficiency J. Biol. Chem. 279 2004 24179 24188
    • (2004) J. Biol. Chem. , vol.279 , pp. 24179-24188
    • Hinkle, C.L.1
  • 15
    • 9144252129 scopus 로고    scopus 로고
    • Distinct ADAM metalloproteinases regulate G protein-coupled receptor-induced cell proliferation and survival
    • B. Schäfer Distinct ADAM metalloproteinases regulate G protein-coupled receptor-induced cell proliferation and survival J. Biol. Chem. 279 2004 47929 47938
    • (2004) J. Biol. Chem. , vol.279 , pp. 47929-47938
    • Schäfer, B.1
  • 16
    • 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
    • Y. Zhang 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
  • 17
    • 0242330374 scopus 로고    scopus 로고
    • ADAMs family members as amyloid precursor protein alpha-secretases
    • T.M. Allinson ADAMs family members as amyloid precursor protein alpha-secretases J. Neurosci. Res. 74 2003 342 352
    • (2003) J. Neurosci. Res. , vol.74 , pp. 342-352
    • Allinson, T.M.1
  • 18
    • 0036796421 scopus 로고    scopus 로고
    • The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for α-secretase activity in fibroblasts
    • D. Hartmann The disintegrin/metalloprotease ADAM 10 is essential for Notch signalling but not for α-secretase activity in fibroblasts Hum. Mol. Genet. 11 2002 2615 2624
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2615-2624
    • Hartmann, D.1
  • 19
    • 0034714357 scopus 로고    scopus 로고
    • Regulated cleavage of a contact-mediated axon repellent
    • M. Hattori Regulated cleavage of a contact-mediated axon repellent Science 289 2000 1360 1365
    • (2000) Science , vol.289 , pp. 1360-1365
    • Hattori, M.1
  • 20
    • 0034914811 scopus 로고    scopus 로고
    • The function of leak and kuzbanian during growth cone and cell migration
    • K. Schimmelpfeng The function of leak and kuzbanian during growth cone and cell migration Mech. Dev. 106 2001 25 36
    • (2001) Mech. Dev. , vol.106 , pp. 25-36
    • Schimmelpfeng, K.1
  • 21
    • 85047690140 scopus 로고    scopus 로고
    • A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model
    • R. Postina 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
  • 22
    • 0036890486 scopus 로고    scopus 로고
    • Alzheimer's and prion diseases: Distinct pathologies, common proteolytic denominators
    • F. Checler, and B. Vincent Alzheimer's and prion diseases: distinct pathologies, common proteolytic denominators Trends Neurosci. 25 2002 616 620
    • (2002) Trends Neurosci. , vol.25 , pp. 616-620
    • Checler, F.1    Vincent, B.2
  • 23
    • 1642524321 scopus 로고    scopus 로고
    • Dual mechanisms for shedding of the cellular prion protein
    • E.T. Parkin Dual mechanisms for shedding of the cellular prion protein J. Biol. Chem. 279 2004 11170 11178
    • (2004) J. Biol. Chem. , vol.279 , pp. 11170-11178
    • Parkin, E.T.1
  • 24
    • 0036170534 scopus 로고    scopus 로고
    • Mice lacking the metalloprotease-disintegrin MDC9 (ADAM9) have no evident major abnormalities during development or adult life
    • G. Weskamp 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
  • 25
    • 0037214312 scopus 로고    scopus 로고
    • Phenotypic analysis of Meltrin α (ADAM12)-deficient mice: Involvement of Meltrin α in adipogenesis and myogenesis
    • T. Kurisaki Phenotypic analysis of Meltrin α (ADAM12)-deficient mice: involvement of Meltrin α in adipogenesis and myogenesis Mol. Cell. Biol. 23 2003 55 61
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 55-61
    • Kurisaki, T.1
  • 26
    • 0041631044 scopus 로고    scopus 로고
    • Potential role for ADAM15 in pathological neovascularization in mice
    • K. Horiuchi Potential role for ADAM15 in pathological neovascularization in mice Mol. Cell. Biol. 23 2003 5614 5624
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5614-5624
    • Horiuchi, K.1
  • 27
    • 19944428083 scopus 로고    scopus 로고
    • Metalloprotease-disintegrin ADAM8: Expression analysis and targeted deletion in mice
    • K. Kelly Metalloprotease-disintegrin ADAM8: expression analysis and targeted deletion in mice Dev. Dyn. 232 2005 221 231
    • (2005) Dev. Dyn. , vol.232 , pp. 221-231
    • Kelly, K.1
  • 28
    • 10744227218 scopus 로고    scopus 로고
    • Compensation for dystrophin-deficiency: ADAM12 overexpression in skeletal muscle results in increased α7 integrin, utrophin and associated glycoproteins
    • B. Moghadaszadeh Compensation for dystrophin-deficiency: ADAM12 overexpression in skeletal muscle results in increased α7 integrin, utrophin and associated glycoproteins Hum. Mol. Genet. 12 2003 2467 2479
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2467-2479
    • Moghadaszadeh, B.1
  • 29
    • 10744227726 scopus 로고    scopus 로고
    • Essential roles of Meltrin β (ADAM19) in heart development
    • K. Kurohara Essential roles of Meltrin β (ADAM19) in heart development Dev. Biol. 267 2004 14 28
    • (2004) Dev. Biol. , vol.267 , pp. 14-28
    • Kurohara, K.1
  • 30
    • 10744223754 scopus 로고    scopus 로고
    • Essential role for ADAM19 in cardiovascular morphogenesis
    • H.M. Zhou Essential role for ADAM19 in cardiovascular morphogenesis Mol. Cell. Biol. 24 2004 96 104
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 96-104
    • Zhou, H.M.1
  • 31
    • 12144290186 scopus 로고    scopus 로고
    • Catalytic activity of human ADAM33
    • J. Zou Catalytic activity of human ADAM33 J. Biol. Chem. 279 2004 9818 9830
    • (2004) J. Biol. Chem. , vol.279 , pp. 9818-9830
    • Zou, J.1
  • 32
    • 5644290647 scopus 로고    scopus 로고
    • Evaluation of the contribution of different ADAMs to tumor necrosis factor α (TNFα) shedding and of the function of the TNFα ectodomain in ensuring selective stimulated shedding by the TNFα convertase (TACE/ADAM17)
    • Y. Zheng Evaluation of the contribution of different ADAMs to tumor necrosis factor α (TNFα) shedding and of the function of the TNFα ectodomain in ensuring selective stimulated shedding by the TNFα convertase (TACE/ADAM17) J. Biol. Chem. 279 2004 42898 42906
    • (2004) J. Biol. Chem. , vol.279 , pp. 42898-42906
    • Zheng, Y.1
  • 33
    • 0036250006 scopus 로고    scopus 로고
    • TACE/ADAM17-TNF-α pathway in rat cortical cultures after exposure to oxygen-glucose deprivation or glutamate
    • O. Hurtado TACE/ADAM17-TNF-α pathway in rat cortical cultures after exposure to oxygen-glucose deprivation or glutamate J. Cereb. Blood Flow Metab. 22 2002 576 585
    • (2002) J. Cereb. Blood Flow Metab. , vol.22 , pp. 576-585
    • Hurtado, O.1
  • 34
    • 8444253005 scopus 로고    scopus 로고
    • Aberrant alternative exon use and increased copy number of human metalloprotease-disintegrin ADAM15 gene in breast cancer cells
    • R.M. Ortiz 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
  • 35
    • 18444388856 scopus 로고    scopus 로고
    • The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs
    • A. Amour The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs FEBS Lett. 524 2002 154 158
    • (2002) FEBS Lett. , vol.524 , pp. 154-158
    • Amour, A.1
  • 36
    • 0037157854 scopus 로고    scopus 로고
    • The metalloprotease Kuzbanian (ADAM10) mediates the transactivation of EGF receptor by G protein-coupled receptors
    • Y. Yan The metalloprotease Kuzbanian (ADAM10) mediates the transactivation of EGF receptor by G protein-coupled receptors J. Cell Biol. 158 2002 221 226
    • (2002) J. Cell Biol. , vol.158 , pp. 221-226
    • Yan, Y.1
  • 37
    • 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
    • E. Shimizu 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
  • 38
    • 1842562408 scopus 로고    scopus 로고
    • Lipid rafts identified as locations of ectodomain shedding mediated by Meltrin β/ADAM19
    • S. Wakatsuki Lipid rafts identified as locations of ectodomain shedding mediated by Meltrin β/ADAM19 J. Neurochem. 89 2004 119 123
    • (2004) J. Neurochem. , vol.89 , pp. 119-123
    • Wakatsuki, S.1
  • 39
    • 1642357584 scopus 로고    scopus 로고
    • Depletion of cellular cholesterol and lipid rafts increases shedding of CD30
    • B. von Tresckow Depletion of cellular cholesterol and lipid rafts increases shedding of CD30 J. Immunol. 172 2004 4324 4331
    • (2004) J. Immunol. , vol.172 , pp. 4324-4331
    • Von Tresckow, B.1
  • 40
    • 0141866756 scopus 로고    scopus 로고
    • Cellular cholesterol depletion triggers shedding of the human interleukin-6 receptor by ADAM10 and ADAM17 (TACE)
    • V. Matthews 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
  • 41
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts
    • R. Ehehalt Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts J. Cell Biol. 160 2003 113 123
    • (2003) J. Cell Biol. , vol.160 , pp. 113-123
    • Ehehalt, R.1
  • 42
    • 0141482022 scopus 로고    scopus 로고
    • Exclusively targeting β-secretase to lipid rafts by GPI-anchor addition up-regulates β-site processing of the amyloid precursor protein
    • J.M. Cordy Exclusively targeting β-secretase to lipid rafts by GPI-anchor addition up-regulates β-site processing of the amyloid precursor protein Proc. Natl. Acad. Sci. U. S. A. 100 2003 11735 11740
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 11735-11740
    • Cordy, J.M.1
  • 43
    • 0035903233 scopus 로고    scopus 로고
    • Regulation of membrane metalloproteolytic cleavage of L-selectin (CD62l) by the epidermal growth factor domain
    • L. Zhao Regulation of membrane metalloproteolytic cleavage of L-selectin (CD62l) by the epidermal growth factor domain J. Biol. Chem. 276 2001 30631 30640
    • (2001) J. Biol. Chem. , vol.276 , pp. 30631-30640
    • Zhao, L.1
  • 44
    • 0035881463 scopus 로고    scopus 로고
    • Roles of the juxtamembrane and extracellular domains of angiotensin-converting enzyme in ectodomain shedding
    • S. Pang Roles of the juxtamembrane and extracellular domains of angiotensin-converting enzyme in ectodomain shedding Biochem. J. 358 2001 185 192
    • (2001) Biochem. J. , vol.358 , pp. 185-192
    • Pang, S.1
  • 45
    • 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
    • K. Endres 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
  • 46
    • 0035985185 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase phosphorylates tumor necrosis factor α-converting enzyme at threonine 735: A potential role in regulated shedding
    • E. Diaz-Rodriguez Extracellular signal-regulated kinase phosphorylates tumor necrosis factor α-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
  • 47
    • 0038719741 scopus 로고    scopus 로고
    • Characterization of growth factor-induced serine phosphorylation of tumor necrosis factor-α converting enzyme and of an alternatively translated polypeptide
    • H. Fan Characterization of growth factor-induced serine phosphorylation of tumor necrosis factor-α converting enzyme and of an alternatively translated polypeptide J. Biol. Chem. 278 2003 18617 18627
    • (2003) J. Biol. Chem. , vol.278 , pp. 18617-18627
    • Fan, H.1
  • 48
    • 1042278167 scopus 로고    scopus 로고
    • Evidence for a critical role of the tumor necrosis factor α convertase (TACE) in ectodomain shedding of the p75 neurotrophin receptor (p75NTR)
    • G. Weskamp Evidence for a critical role of the tumor necrosis factor α convertase (TACE) in ectodomain shedding of the p75 neurotrophin receptor (p75NTR) J. Biol. Chem. 279 2004 4241 4249
    • (2004) J. Biol. Chem. , vol.279 , pp. 4241-4249
    • Weskamp, G.1
  • 49
    • 0037097492 scopus 로고    scopus 로고
    • Muscarine enhances soluble amyloid precursor protein secretion in human neuroblastoma SH-SY5Y by a pathway dependent on protein kinase Cα, src-tyrosine kinase and extracellular signal-regulated kinase but not phospholipase C
    • R.M. Canet-Aviles Muscarine enhances soluble amyloid precursor protein secretion in human neuroblastoma SH-SY5Y by a pathway dependent on protein kinase Cα, src-tyrosine kinase and extracellular signal-regulated kinase but not phospholipase C Brain Res. Mol. Brain Res. 102 2002 62 72
    • (2002) Brain Res. Mol. Brain Res. , vol.102 , pp. 62-72
    • Canet-Aviles, R.M.1
  • 50
    • 0343628678 scopus 로고    scopus 로고
    • Metalloprotease-disintegrin (ADAM) genes are widely and differentially expressed in the adult CNS
    • I. Kärkkäinen 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
    • Kärkkäinen, I.1
  • 51
    • 0037474447 scopus 로고    scopus 로고
    • Putative function of ADAM9, ADAM10, and ADAM17 as APP α-secretase
    • M. Asai Putative function of ADAM9, ADAM10, and ADAM17 as APP α-secretase Biochem. Biophys. Res. Commun. 301 2003 231 235
    • (2003) Biochem. Biophys. Res. Commun. , vol.301 , pp. 231-235
    • Asai, M.1
  • 52
    • 3042643033 scopus 로고    scopus 로고
    • The role of ADAM10 and ADAM17 in the ectodomain shedding of angiotensin converting enzyme and the amyloid precursor protein
    • T.M. Allinson The role of ADAM10 and ADAM17 in the ectodomain shedding of angiotensin converting enzyme and the amyloid precursor protein Eur. J. Biochem. 271 2004 2539 2547
    • (2004) Eur. J. Biochem. , vol.271 , pp. 2539-2547
    • Allinson, T.M.1
  • 53
    • 0041355557 scopus 로고    scopus 로고
    • Notch and Presenilin: Regulated intramembrane proteolysis links development and degeneration
    • D. Selkoe, and R. Kopan 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
  • 54
    • 0037416187 scopus 로고    scopus 로고
    • TACE is required for the activation of the EGFR by TGF-α in tumors
    • M. Borrell-Pages TACE is required for the activation of the EGFR by TGF-α in tumors EMBO J. 22 2003 1114 1124
    • (2003) EMBO J. , vol.22 , pp. 1114-1124
    • Borrell-Pages, M.1
  • 55
    • 0036152858 scopus 로고    scopus 로고
    • Cardiac hypertrophy is inhibited by antagonism of ADAM12 processing of HB-EGF: Metalloproteinase inhibitors as a new therapy
    • M. Asakura 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
  • 56
    • 0037173639 scopus 로고    scopus 로고
    • Association of the ADAM33 gene with asthma and bronchial hyperresponsiveness
    • P. Van Eerdewegh Association of the ADAM33 gene with asthma and bronchial hyperresponsiveness Nature 418 2002 426 430
    • (2002) Nature , vol.418 , pp. 426-430
    • Van Eerdewegh, P.1
  • 57
    • 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
    • C. Hundhausen 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
  • 58
    • 0035851124 scopus 로고    scopus 로고
    • Tumor necrosis factor-α-converting enzyme (ADAM17) mediates the cleavage and shedding of fractalkine (CX3CL1)
    • K.J. Garton Tumor necrosis factor-α-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
  • 59
    • 2442527640 scopus 로고    scopus 로고
    • The transmembrane CXC-chemokine ligand 16 is induced by IFN-γ and TNF-α and shed by the activity of the disintegrin-like metalloproteinase ADAM10
    • S. Abel The transmembrane CXC-chemokine ligand 16 is induced by IFN-γ and TNF-α 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
  • 60
    • 1542724429 scopus 로고    scopus 로고
    • A disintegrin and metalloproteinase 10-mediated cleavage and shedding regulates the cell surface expression of CXC chemokine ligand 16
    • P.J. Gough A disintegrin and metalloproteinase 10-mediated cleavage and shedding regulates the cell surface expression of CXC chemokine ligand 16 J. Immunol. 172 2004 3678 3685
    • (2004) J. Immunol. , vol.172 , pp. 3678-3685
    • Gough, P.J.1
  • 61
    • 0034533443 scopus 로고    scopus 로고
    • Differential shedding of transmembrane neuregulin isoforms by the tumor necrosis factor-α-converting enzyme
    • J.C. Montero Differential shedding of transmembrane neuregulin isoforms by the tumor necrosis factor-α-converting enzyme Mol. Cell. Neurosci. 16 2000 631 648
    • (2000) Mol. Cell. Neurosci. , vol.16 , pp. 631-648
    • Montero, J.C.1
  • 62
    • 0042232590 scopus 로고    scopus 로고
    • Catalytic activity of ADAM8, ADAM15, and MDC-L (ADAM28) on synthetic peptide substrates and in ectodomain cleavage of CD23
    • A.M. Fourie 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
  • 63
    • 0042858460 scopus 로고    scopus 로고
    • Membrane-anchored CD40 is processed by the tumor necrosis factor-α-converting enzyme. Implications for CD40 signaling
    • C. Contin Membrane-anchored CD40 is processed by the tumor necrosis factor-α-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
  • 64
    • 1242317010 scopus 로고    scopus 로고
    • Tumor necrosis factor-α-converting enzyme controls surface expression of c-Kit and survival of embryonic stem cell-derived mast cells
    • A.C. Cruz Tumor necrosis factor-α-converting enzyme controls surface expression of c-Kit and survival of embryonic stem cell-derived mast cells J. Biol. Chem. 279 2004 5612 5620
    • (2004) J. Biol. Chem. , vol.279 , pp. 5612-5620
    • Cruz, A.C.1
  • 65
    • 0034616385 scopus 로고    scopus 로고
    • Tumor necrosis factor-α-converting enzyme is required for cleavage of erbB4/HER4
    • C. Rio Tumor necrosis factor-α-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
  • 66
    • 0036772859 scopus 로고    scopus 로고
    • Chemotactic agents induce IL-6Rα shedding from polymorphonuclear cells: Involvement of a metalloproteinase of the TNF-α-converting enzyme (TACE) type
    • V. Marin Chemotactic agents induce IL-6Rα shedding from polymorphonuclear cells: involvement of a metalloproteinase of the TNF-α-converting enzyme (TACE) type Eur. J. Immunol. 32 2002 2965 2970
    • (2002) Eur. J. Immunol. , vol.32 , pp. 2965-2970
    • Marin, V.1
  • 67
    • 4644367922 scopus 로고    scopus 로고
    • Natural soluble IL-15Rα is generated by cleavage that involves the tumor necrosis factor-α-converting enzyme (TACE/ADAM17)
    • V. Budagian Natural soluble IL-15Rα is generated by cleavage that involves the tumor necrosis factor-α-converting enzyme (TACE/ADAM17) J. Biol. Chem. 279 2004 40368 40375
    • (2004) J. Biol. Chem. , vol.279 , pp. 40368-40375
    • Budagian, V.1
  • 68
    • 0035253355 scopus 로고    scopus 로고
    • TNF-α-converting enzyme cleaves the macrophage colony-stimulating factor receptor in macrophages undergoing activation
    • E. Rovida TNF-α-converting enzyme cleaves the macrophage colony-stimulating factor receptor in macrophages undergoing activation J. Immunol. 166 2001 1583 1589
    • (2001) J. Immunol. , vol.166 , pp. 1583-1589
    • Rovida, E.1
  • 69
    • 1042278148 scopus 로고    scopus 로고
    • Engagement of CD44 promotes Rac activation and CD44 cleavage during tumor cell migration
    • T. Murai Engagement of CD44 promotes Rac activation and CD44 cleavage during tumor cell migration J. Biol. Chem. 279 2004 4541 4550
    • (2004) J. Biol. Chem. , vol.279 , pp. 4541-4550
    • Murai, T.1
  • 70
    • 3042554386 scopus 로고    scopus 로고
    • 2+ influx and PKC activation
    • 2+ influx and PKC activation J. Cell Biol. 165 2004 893 902
    • (2004) J. Cell Biol. , vol.165 , pp. 893-902
    • Nagano, O.1
  • 71
    • 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
    • S. Naus 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
  • 72
    • 0037318306 scopus 로고    scopus 로고
    • ADAM10-mediated cleavage of L1 adhesion molecule at the cell surface and in released membrane vesicles
    • P. Gutwein 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
  • 73
    • 0037064135 scopus 로고    scopus 로고
    • Structure-function relationship and role of tumor necrosis factor-α-converting enzyme in the down-regulation of L-selectin by non-steroidal anti-inflammatory drugs
    • M.V. Gomez-Gaviro Structure-function relationship and role of tumor necrosis factor-α-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
  • 74
    • 0141509970 scopus 로고    scopus 로고
    • Stimulated shedding of vascular cell adhesion molecule 1 (VCAM-1) is mediated by tumor necrosis factor-α-converting enzyme (ADAM 17)
    • K.J. Garton Stimulated shedding of vascular cell adhesion molecule 1 (VCAM-1) is mediated by tumor necrosis factor-α-converting enzyme (ADAM 17) J. Biol. Chem. 278 2003 37459 37464
    • (2003) J. Biol. Chem. , vol.278 , pp. 37459-37464
    • Garton, K.J.1
  • 75
    • 0141704284 scopus 로고    scopus 로고
    • Characterization of the ectodomain shedding of the β-site amyloid precursor protein-cleaving enzyme 1 (BACE1)
    • I. Hussain Characterization of the ectodomain shedding of the β-site amyloid precursor protein-cleaving enzyme 1 (BACE1) J. Biol. Chem. 278 2003 36264 36268
    • (2003) J. Biol. Chem. , vol.278 , pp. 36264-36268
    • Hussain, I.1
  • 76
    • 0242384939 scopus 로고    scopus 로고
    • Phorbol 12-myristate 13-acetate-induced ectodomain shedding and phosphorylation of the human meprinbeta metalloprotease
    • D. Hahn Phorbol 12-myristate 13-acetate-induced ectodomain shedding and phosphorylation of the human meprinbeta metalloprotease J. Biol. Chem. 278 2003 42829 42839
    • (2003) J. Biol. Chem. , vol.278 , pp. 42829-42839
    • Hahn, D.1
  • 77
    • 0942300665 scopus 로고    scopus 로고
    • ADAMs, a disintegrin and metalloproteinases, mediate shedding of oxytocinase
    • N. Ito ADAMs, a disintegrin and metalloproteinases, mediate shedding of oxytocinase Biochem. Biophys. Res. Commun. 314 2004 1008 1013
    • (2004) Biochem. Biophys. Res. Commun. , vol.314 , pp. 1008-1013
    • Ito, N.1
  • 78
    • 18644384411 scopus 로고    scopus 로고
    • Transmembrane collagen XVII, an epithelial adhesion protein, is shed from the cell surface by ADAMs
    • C.W. Franzke 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
  • 79
    • 0037648484 scopus 로고    scopus 로고
    • Notch-induced proteolysis and nuclear localization of the Delta ligand
    • C.E. Bland Notch-induced proteolysis and nuclear localization of the Delta ligand J. Biol. Chem. 278 2003 13607 13610
    • (2003) J. Biol. Chem. , vol.278 , pp. 13607-13610
    • Bland, C.E.1
  • 80
    • 0038610845 scopus 로고    scopus 로고
    • The Notch ligand Delta1 is sequentially cleaved by an ADAM protease and γ-secretase
    • E. Six The Notch ligand Delta1 is sequentially cleaved by an ADAM protease and γ-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
  • 81
    • 0141817915 scopus 로고    scopus 로고
    • The Notch ligands, Jagged and Delta, are sequentially processed by α-secretase and presenilin/γ-secretase and release signaling fragments
    • M.J. LaVoie, and D.J. Selkoe The Notch ligands, Jagged and Delta, are sequentially processed by α-secretase and presenilin/γ-secretase and release signaling fragments J. Biol. Chem. 278 2003 34427 34437
    • (2003) J. Biol. Chem. , vol.278 , pp. 34427-34437
    • Lavoie, M.J.1    Selkoe, D.J.2
  • 82
    • 0037474312 scopus 로고    scopus 로고
    • Tumor necrosis factor-α converting enzyme/ADAM 17 mediates MUC1 shedding
    • A. Thathiah Tumor necrosis factor-α 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
  • 83
    • 17244371476 scopus 로고    scopus 로고
    • Homeostatic effects of the metalloproteinase disintegrin ADAM15 in degenerative cartilage remodeling
    • B.B. Böhm 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
    • Böhm, B.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.