메뉴 건너뛰기




Volumn 16, Issue 2, 2000, Pages 83-87

The ADAM gene family: Surface proteins with adhesion and protease activity

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; METALLOPROTEINASE; PROTEINASE;

EID: 0034141195     PISSN: 01689525     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9525(99)01926-5     Document Type: Review
Times cited : (520)

References (47)
  • 1
    • 0033525037 scopus 로고    scopus 로고
    • Metalloprotease-disintegrin MDC9: Intracellular maturation and catalytic activity
    • Roghani, M. et al. (1999) Metalloprotease-disintegrin MDC9: Intracellular maturation and catalytic activity. J. Biol. Chem. 274, 3531-3540
    • (1999) J. Biol. Chem. , vol.274 , pp. 3531-3540
    • Roghani, M.1
  • 2
    • 0032479157 scopus 로고    scopus 로고
    • Human ADAM 12 (meltrin alpha) is an active metalloprotease
    • Loechel, F. et al. (1998) Human ADAM 12 (meltrin alpha) is an active metalloprotease. J. Biol. Chem. 273, 16993-16997
    • (1998) J. Biol. Chem. , vol.273 , pp. 16993-16997
    • Loechel, F.1
  • 3
    • 0026510747 scopus 로고
    • A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion
    • Blobel, C.P. et al. (1992) A potential fusion peptide and an integrin ligand domain in a protein active in sperm-egg fusion. Nature 356, 248-252
    • (1992) Nature , vol.356 , pp. 248-252
    • Blobel, C.P.1
  • 4
    • 8044250278 scopus 로고    scopus 로고
    • Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha
    • Moss, M.L. et al. (1997) Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-alpha. Nature 385, 733-736
    • (1997) Nature , vol.385 , pp. 733-736
    • Moss, M.L.1
  • 5
    • 0032544623 scopus 로고    scopus 로고
    • Fertilization defects in sperm from mice lacking fertilin beta
    • Cho, C. et al. (1998) Fertilization defects in sperm from mice lacking fertilin beta. Science 281, 1857-1859
    • (1998) Science , vol.281 , pp. 1857-1859
    • Cho, C.1
  • 6
    • 0030951614 scopus 로고    scopus 로고
    • A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm-egg plasma membrane adhesion and fusion
    • Yuan, R. et al. (1997) A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm-egg plasma membrane adhesion and fusion. J. Cell. Biol. 137, 105-112
    • (1997) J. Cell. Biol. , vol.137 , pp. 105-112
    • Yuan, R.1
  • 7
    • 0030981901 scopus 로고    scopus 로고
    • Decreased in vitro fertilization efficiencies in the presence of specific cyritestin peptides
    • Linder, B. and Heinlein, U.A. (1997) Decreased in vitro fertilization efficiencies in the presence of specific cyritestin peptides. Dev. Growth Differ. 39, 243-247
    • (1997) Dev. Growth Differ. , vol.39 , pp. 243-247
    • Linder, B.1    Heinlein, U.A.2
  • 8
    • 0032571315 scopus 로고    scopus 로고
    • Specific interaction of the recombinant disintegrin-like domain of MDC-15 (metargidin, ADAM-15) with integrin alpha v beta 3
    • Zhang, X.P. et al. (1998) Specific interaction of the recombinant disintegrin-like domain of MDC-15 (metargidin, ADAM-15) with integrin alpha v beta 3. J. Biol. Chem. 273, 7345-7350
    • (1998) J. Biol. Chem. , vol.273 , pp. 7345-7350
    • Zhang, X.P.1
  • 9
    • 0032969233 scopus 로고    scopus 로고
    • 1 integrins on different haemopoietic cells
    • 1 integrins on different haemopoietic cells. J. Cell Sci. 112, 579-587
    • (1999) J. Cell Sci. , vol.112 , pp. 579-587
    • Nath, D.1
  • 10
    • 0032908446 scopus 로고    scopus 로고
    • Cysteine-rich domain of human ADAM 12 (Meltrin alpha) supports tumor cell adhesion
    • Iba, K. et al. (1999) Cysteine-rich domain of human ADAM 12 (Meltrin alpha) supports tumor cell adhesion. Am. J. Pathol. 154, 1489-1501
    • (1999) Am. J. Pathol. , vol.154 , pp. 1489-1501
    • Iba, K.1
  • 11
    • 0032422065 scopus 로고    scopus 로고
    • Peptides corresponding to the epidermal growth factor-like domain of mouse fertilin: Synthesis and biological activity
    • Chen, H. et al. (1998) Peptides corresponding to the epidermal growth factor-like domain of mouse fertilin: Synthesis and biological activity. Biopolymers 47, 299-307
    • (1998) Biopolymers , vol.47 , pp. 299-307
    • Chen, H.1
  • 12
    • 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. et al. (1998) A metalloprotease-disintegrin, MDC9/meltrin-gamma/ADAM9 and PKCdelta are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor. EMBO J. 17, 7260-7272
    • (1998) EMBO J. , vol.17 , pp. 7260-7272
    • Izumi, Y.1
  • 13
    • 0029770079 scopus 로고    scopus 로고
    • Virus-cell and cell-cell fusion
    • Hernandez, L.D. et al. (1996) Virus-cell and cell-cell fusion. Annu. Rev. Cell Dev. Biol. 12, 627-661
    • (1996) Annu. Rev. Cell Dev. Biol. , vol.12 , pp. 627-661
    • Hernandez, L.D.1
  • 14
    • 0030986652 scopus 로고    scopus 로고
    • A model for sperm-egg binding and fusion based on ADAMs and integrins
    • Bigler, D. et al. (1997) A model for sperm-egg binding and fusion based on ADAMs and integrins. Trends Cell Biol. 7, 220-225
    • (1997) Trends Cell Biol. , vol.7 , pp. 220-225
    • Bigler, D.1
  • 15
    • 0030834283 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: Links to cell adhesion and cleavage of TNFα and Notch
    • Blobel, C.P. (1997) Metalloprotease-disintegrins: Links to cell adhesion and cleavage of TNFα and Notch. Cell 90, 589-592
    • (1997) Cell , vol.90 , pp. 589-592
    • Blobel, C.P.1
  • 16
    • 0000117001 scopus 로고    scopus 로고
    • Roles of metalloprotease-disintegrins in cell-cell interactions, in neurogenesis, and in the cleavage of TNF α
    • Blobel, C.P. (1999) Roles of metalloprotease-disintegrins in cell-cell interactions, in neurogenesis, and in the cleavage of TNF α. Adv. Dev. Biochem. 5, 165-198
    • (1999) Adv. Dev. Biochem. , vol.5 , pp. 165-198
    • Blobel, C.P.1
  • 17
    • 0031698581 scopus 로고    scopus 로고
    • ADAMs: Focus on the protease domain
    • Black, R.A. and White, J.M. (1998) ADAMs: Focus on the protease domain. Curr. Opin. Cell Biol. 10, 654-659
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 654-659
    • Black, R.A.1    White, J.M.2
  • 18
    • 0031032891 scopus 로고    scopus 로고
    • Membrane protein secretases
    • Hooper, N.M. et al. (1997) Membrane protein secretases. Biochem. J. 321, 265-279
    • (1997) Biochem. J. , vol.321 , pp. 265-279
    • Hooper, N.M.1
  • 19
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells
    • Black, R.A. et al. (1997) A metalloproteinase disintegrin that releases tumour-necrosis factor-alpha from cells. Nature 385, 729-733
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.A.1
  • 20
    • 0032515018 scopus 로고    scopus 로고
    • An essential role for ectodomain shedding in mammalian development
    • Peschon, J.J. et al. (1998) An essential role for ectodomain shedding in mammalian development. Science 282, 1281-1284
    • (1998) Science , vol.282 , pp. 1281-1284
    • Peschon, J.J.1
  • 21
    • 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. et al. (1998) 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, 27765-27767
    • (1998) J. Biol. Chem. , vol.273 , pp. 27765-27767
    • Buxbaum, J.D.1
  • 22
    • 0344019404 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzyme
    • Maskos, K. et al. (1998) Crystal structure of the catalytic domain of human tumor necrosis factor-alpha-converting enzyme. Proc. Natl. Acad. Sci. U. S. A. 95, 3408-3412
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 3408-3412
    • Maskos, K.1
  • 23
    • 0032923759 scopus 로고    scopus 로고
    • Processing of the notch ligand delta by the metalloprotease Kuzbanian
    • Qi, H. et al. (1999) Processing of the notch ligand delta by the metalloprotease Kuzbanian. Science 283, 91-94
    • (1999) Science , vol.283 , pp. 91-94
    • Qi, H.1
  • 24
    • 0033617522 scopus 로고    scopus 로고
    • Notch signaling: Cell fate control and signal integration in development
    • Artavanis-Tsakonas, S. et al. (1999) Notch signaling: Cell fate control and signal integration in development. Science 284, 770-776
    • (1999) Science , vol.284 , pp. 770-776
    • Artavanis-Tsakonas, S.1
  • 25
    • 0029788321 scopus 로고    scopus 로고
    • KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis
    • Rooke, J. et al. (1996) KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis. Science 273, 1227-1231
    • (1996) Science , vol.273 , pp. 1227-1231
    • Rooke, J.1
  • 26
    • 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. (1997) Kuzbanian controls proteolytic processing of Notch and mediates lateral inhibition during Drosophila and vertebrate neurogenesis. Cell 90, 271-280
    • (1997) Cell , vol.90 , pp. 271-280
    • Pan, D.1    Rubin, G.M.2
  • 27
    • 0033616716 scopus 로고    scopus 로고
    • Constitutive and regulated alpha-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease
    • Lammich, S. et al. (1999) Constitutive and regulated alpha-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease. Proc. Natl. Acad. Sci. U. S. A. 96, 3922-3927
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 3922-3927
    • Lammich, S.1
  • 28
    • 0028807402 scopus 로고
    • A metalloprotease-disintegrin participating in myoblast fusion
    • Yagami-Hiromasa, T. et al. (1995) A metalloprotease-disintegrin participating in myoblast fusion. Nature 377, 652-656
    • (1995) Nature , vol.377 , pp. 652-656
    • Yagami-Hiromasa, T.1
  • 29
    • 0033532144 scopus 로고    scopus 로고
    • Regulation of human ADAM 12 protease by the prodomain. Evidence for a functional cysteine switch
    • Loechel, F. et al. (1999) Regulation of human ADAM 12 protease by the prodomain. Evidence for a functional cysteine switch. J. Biol. Chem. 274, 13427-13433
    • (1999) J. Biol. Chem. , vol.274 , pp. 13427-13433
    • Loechel, F.1
  • 30
    • 0031961873 scopus 로고    scopus 로고
    • A novel, secreted form of human ADAM 12 (meltrin alpha) provokes myogenesis in vivo
    • Gilpin, B.J. et al. (1998) A novel, secreted form of human ADAM 12 (meltrin alpha) provokes myogenesis in vivo. J. Biol. Chem. 273, 157-166
    • (1998) J. Biol. Chem. , vol.273 , pp. 157-166
    • Gilpin, B.J.1
  • 31
    • 0032978988 scopus 로고    scopus 로고
    • ADAMTS: A novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats
    • Tang, B.L. and Hong, W. (1999) ADAMTS: a novel family of proteases with an ADAM protease domain and thrombospondin 1 repeats. FEBS Lett. 445, 223-225
    • (1999) FEBS Lett. , vol.445 , pp. 223-225
    • Tang, B.L.1    Hong, W.2
  • 32
    • 0033542457 scopus 로고    scopus 로고
    • Control of organ shape by a secreted metalloprotease in the nematode Caenorhabditis elegans
    • Blelloch, R. and Kimble, J. (1999) Control of organ shape by a secreted metalloprotease in the nematode Caenorhabditis elegans. Nature 399, 586-590
    • (1999) Nature , vol.399 , pp. 586-590
    • Blelloch, R.1    Kimble, J.2
  • 33
    • 0345211445 scopus 로고    scopus 로고
    • Purification and cloning of aggrecanase-1: A member of the ADAMTS family of proteins
    • Tortorella, M.D. et al. (1999) Purification and cloning of aggrecanase-1: a member of the ADAMTS family of proteins. Science 284, 1664-1666
    • (1999) Science , vol.284 , pp. 1664-1666
    • Tortorella, M.D.1
  • 34
    • 0033551844 scopus 로고    scopus 로고
    • Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family
    • Abbaszade, I. et al. (1999) Cloning and characterization of ADAMTS11, an aggrecanase from the ADAMTS family. J. Biol. Chem. 274, 23443-23450
    • (1999) J. Biol. Chem. , vol.274 , pp. 23443-23450
    • Abbaszade, I.1
  • 35
    • 0023100910 scopus 로고
    • Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion
    • Primakoff, P. et al. (1987) Identification and purification of a sperm surface protein with a potential role in sperm-egg membrane fusion. J. Cell Biol. 104, 141-149
    • (1987) J. Cell Biol. , vol.104 , pp. 141-149
    • Primakoff, P.1
  • 36
    • 0031282021 scopus 로고    scopus 로고
    • Evidence for distinct serine protease activities with a potential role in processing the sperm protein fertilin
    • Lum, L. and Blobel, C.P. (1997) Evidence for distinct serine protease activities with a potential role in processing the sperm protein fertilin. Dev. Biol. 191, 131-145
    • (1997) Dev. Biol. , vol.191 , pp. 131-145
    • Lum, L.1    Blobel, C.P.2
  • 37
    • 0028150753 scopus 로고
    • Disintegrinsand other naturally occurring antagonists of platelet fibrinogen receptors
    • Niewiarowski, S. et al. (1994) Disintegrinsand other naturally occurring antagonists of platelet fibrinogen receptors. Semin. Hematol. 31, 289-300
    • (1994) Semin. Hematol. , vol.31 , pp. 289-300
    • Niewiarowski, S.1
  • 38
    • 0030976889 scopus 로고    scopus 로고
    • Function of disintegrin-like/cysteine-rich domains of atrolysin A. Inhibition of platelet aggregation by recombinant protein and peptide antagonists
    • Jia, L.G. et al. (1997) Function of disintegrin-like/cysteine-rich domains of atrolysin A. Inhibition of platelet aggregation by recombinant protein and peptide antagonists. J. Biol. Chem. 272, 13094-13102
    • (1997) J. Biol. Chem. , vol.272 , pp. 13094-13102
    • Jia, L.G.1
  • 39
    • 0029949611 scopus 로고    scopus 로고
    • Inhibition of collagen-induced platelet aggregation as the result of cleavage of alpha 2 beta 1-integrin by the snake venom metalloproteinase jararhagin
    • Kamiguti, A.S. et al. (1996) Inhibition of collagen-induced platelet aggregation as the result of cleavage of alpha 2 beta 1-integrin by the snake venom metalloproteinase jararhagin. Biochem. J. 320, 635-641
    • (1996) Biochem. J. , vol.320 , pp. 635-641
    • Kamiguti, A.S.1
  • 40
    • 0028909347 scopus 로고
    • Expression of the rabbit sperm protein Sp17 in COS cells and interaction of recombinant Sp17 with the rabbit zona pellucida
    • Yamasaki, N. et al. (1995) Expression of the rabbit sperm protein Sp17 in COS cells and interaction of recombinant Sp17 with the rabbit zona pellucida. Mol. Reprod. Dev. 40, 48-55
    • (1995) Mol. Reprod. Dev. , vol.40 , pp. 48-55
    • Yamasaki, N.1
  • 41
    • 0028325475 scopus 로고
    • Identification of a binding site in the disintegrin domain of fertilin required for sperm-egg fusion
    • Myles, D.G. et al. (1994) Identification of a binding site in the disintegrin domain of fertilin required for sperm-egg fusion. Proc. Natl. Acad. Sci. U. S. A. 91, 4195-4198
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 4195-4198
    • Myles, D.G.1
  • 42
    • 0033535043 scopus 로고    scopus 로고
    • Evidence that distinct states of the integrin alpha 6 beta 1 interact with laminin and an ADAM
    • Chen, M.S. et al. (1999) Evidence that distinct states of the integrin alpha 6 beta 1 interact with laminin and an ADAM. J. Cell Biol. 144, 549-561
    • (1999) J. Cell Biol. , vol.144 , pp. 549-561
    • Chen, M.S.1
  • 43
    • 0029162781 scopus 로고
    • Mouse sperm-egg plasma membrane interactions: Analysis of roles of egg integrins and the mouse sperm homologue of PH-30 (fertilin) beta
    • Evans, J.P. et al. (1995) Mouse sperm-egg plasma membrane interactions: analysis of roles of egg integrins and the mouse sperm homologue of PH-30 (fertilin) beta. J. Cell Sci. 108, 3267-3278
    • (1995) J. Cell Sci. , vol.108 , pp. 3267-3278
    • Evans, J.P.1
  • 44
    • 0029047919 scopus 로고
    • Mouse egg integrin alpha 6 beta 1 functions as a sperm receptor
    • Almeida, E.A. et al. (1995) Mouse egg integrin alpha 6 beta 1 functions as a sperm receptor. Cell 81, 1095-1104
    • (1995) Cell , vol.81 , pp. 1095-1104
    • Almeida, E.A.1
  • 45
    • 0032782655 scopus 로고    scopus 로고
    • Mediation of sperm-egg fusion: Evidence that mouse egg alpha6 beta1 integrin is the receptor for sperm fertilin beta
    • Chen, H. and Sampson, N.S. (1999) Mediation of sperm-egg fusion: Evidence that mouse egg alpha6 beta1 integrin is the receptor for sperm fertilin beta. Chem. Biol. 6, 1-10
    • (1999) Chem. Biol. , vol.6 , pp. 1-10
    • Chen, H.1    Sampson, N.S.2
  • 46
    • 0031194395 scopus 로고    scopus 로고
    • Characterization of the binding of recombinant mouse sperm fertilin alpha subunit to mouse eggs: Evidence for function as a cell adhesion molecule in sperm-egg binding
    • Evans, J.P. et al. (1997) Characterization of the binding of recombinant mouse sperm fertilin alpha subunit to mouse eggs: evidence for function as a cell adhesion molecule in sperm-egg binding. Dev. Biol. 187, 94-106
    • (1997) Dev. Biol. , vol.187 , pp. 94-106
    • Evans, J.P.1
  • 47
    • 0029995478 scopus 로고    scopus 로고
    • Molecular cloning of MADM: A catalytically active mammalian disintegrin-metalloprotease expressed in various cell types
    • Howard, L. et al. (1996) Molecular cloning of MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell types. Biochem. J. 317, 45-50
    • (1996) Biochem. J. , vol.317 , pp. 45-50
    • Howard, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.