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Volumn 288, Issue 29, 2013, Pages 21367-21375

ADAMDEC1 is a metzincin metalloprotease with dampened proteolytic activity

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; DOMAIN STRUCTURE; GLYCOSYLATED; MACROGLOBULIN; METALLO-PROTEASE; PROTEOLYTIC ACTIVITIES; ZINC-BINDING SITES;

EID: 84880558281     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.474536     Document Type: Article
Times cited : (23)

References (47)
  • 2
    • 0036326359 scopus 로고    scopus 로고
    • The ADAMDEC1 (decysin) gene structure: Evolution by duplication in a metalloprotease gene cluster on chromosome 8p12
    • Bates, E. E., Fridman, W. H., and Mueller, C. G. (2002) The ADAMDEC1 (decysin) gene structure: evolution by duplication in a metalloprotease gene cluster on chromosome 8p12. Immunogenetics 54, 96-105
    • (2002) Immunogenetics , vol.54 , pp. 96-105
    • Bates, E.E.1    Fridman, W.H.2    Mueller, C.G.3
  • 3
    • 84864977995 scopus 로고    scopus 로고
    • Phylogenetic and molecular evolution of the ADAM (A Disintegrin and Metalloprotease) gene family from Xenopus tropicalis, to Mus musculus, Rattus norvegicus, and Homo sapiens
    • Long, J., Li, M., Ren, Q., Zhang, C., Fan, J., Duan, Y., Chen, J., Li, B., and Deng, L. (2012) Phylogenetic and molecular evolution of the ADAM (A Disintegrin And Metalloprotease) gene family from Xenopus tropicalis, to Mus musculus, Rattus norvegicus, and Homo sapiens. Gene 507, 36-43
    • (2012) Gene , vol.507 , pp. 36-43
    • Long, J.1    Li, M.2    Ren, Q.3    Zhang, C.4    Fan, J.5    Duan, Y.6    Chen, J.7    Li, B.8    Deng, L.9
  • 4
    • 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-Rüth, F. X., and Stöckler, W. (1993) 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, 134-140
    • (1993) FEBS Lett. , vol.331 , pp. 134-140
    • Bode, W.1    Gomis-Rüth, F.X.2    Stöckler, W.3
  • 5
    • 0038019916 scopus 로고    scopus 로고
    • Structural aspects of the metzincin clan of metalloendopeptidases
    • Gomis-Rüth, F. X. (2003) Structural aspects of the metzincin clan of metalloendopeptidases. Mol. Biotechnol. 24, 157-202
    • (2003) Mol. Biotechnol. , vol.24 , pp. 157-202
    • Gomis-Rüth, F.X.1
  • 6
    • 0034141195 scopus 로고    scopus 로고
    • The ADAM gene family: Surface proteins with adhesion and protease activity
    • Primakoff, P., and Myles, D. G. (2000) The ADAM gene family: surface proteins with adhesion and protease activity. Trends Genet. 16, 83-87
    • (2000) Trends Genet. , vol.16 , pp. 83-87
    • Primakoff, P.1    Myles, D.G.2
  • 8
    • 67650065404 scopus 로고    scopus 로고
    • Catalytic domain architecture of metzincin metalloproteases
    • Gomis-Rüth, F. X. (2009) Catalytic domain architecture of metzincin metalloproteases. J. Biol. Chem. 284, 15353-15357
    • (2009) J. Biol. Chem. , vol.284 , pp. 15353-15357
    • Gomis-Rüth, F.X.1
  • 9
    • 0017395121 scopus 로고
    • Crystallographic study of the binding of dipeptide inhibitors to thermolysin: Implications for the mechanism of catalysis
    • Kester, W. R., and Matthews, B. W. (1977) Crystallographic study of the binding of dipeptide inhibitors to thermolysin: implications for the mechanism of catalysis. Biochemistry 16, 2506-2516
    • (1977) Biochemistry , vol.16 , pp. 2506-2516
    • Kester, W.R.1    Matthews, B.W.2
  • 10
    • 79951519159 scopus 로고    scopus 로고
    • Active metalloproteases of the A Disintegrin and Metalloprotease (ADAM) family: Biological function and structure
    • Klein, T., and Bischoff, R. (2011) Active metalloproteases of the A Disintegrin and Metalloprotease (ADAM) family: biological function and structure. J. Proteome Res. 10, 17-33
    • (2011) J. Proteome Res. , vol.10 , pp. 17-33
    • Klein, T.1    Bischoff, R.2
  • 12
    • 0346851877 scopus 로고    scopus 로고
    • Inverse regulation of the ADAM-family members, decysin and MADDAM/ADAM19 during monocyte differentiation
    • Fritsche, J., Müller, A., Hausmann, M., Rogler, G., Andreesen, R., and Kreutz, M. (2003) Inverse regulation of the ADAM-family members, decysin and MADDAM/ADAM19 during monocyte differentiation. Immunology 110, 450-457
    • (2003) Immunology , vol.110 , pp. 450-457
    • Fritsche, J.1    Müller, A.2    Hausmann, M.3    Rogler, G.4    Andreesen, R.5    Kreutz, M.6
  • 15
    • 38149071725 scopus 로고    scopus 로고
    • Characterization of intestinal inflammation and identification of related gene expression changes in mdr1a-/- mice
    • Dommels, Y. E., Butts, C. A., Zhu, S., Davy, M., Martell, S., Hedderley, D., Barnett, M. P., McNabb, W. C., and Roy, N. C. (2007) Characterization of intestinal inflammation and identification of related gene expression changes in mdr1a-/- mice. Genes Nutr. 2, 209-223
    • (2007) Genes Nutr. , vol.2 , pp. 209-223
    • Dommels, Y.E.1    Butts, C.A.2    Zhu, S.3    Davy, M.4    Martell, S.5    Hedderley, D.6    Barnett, M.P.7    McNabb, W.C.8    Roy, N.C.9
  • 16
    • 84865126347 scopus 로고    scopus 로고
    • Expression and inhibition ofADAMDEC1in craniopharyngioma cells
    • Xu, J., Liu, L., Zheng, X., You, C., and Li, Q. (2012) Expression and inhibition ofADAMDEC1in craniopharyngioma cells. Neurol. Res. 34, 701-706
    • (2012) Neurol. Res. , vol.34 , pp. 701-706
    • Xu, J.1    Liu, L.2    Zheng, X.3    You, C.4    Li, Q.5
  • 18
    • 48549099613 scopus 로고    scopus 로고
    • Metastatic susceptibility locus, an 8p hot-spot for tumour progression disrupted in colorectal liver metastases: 13 candidate genes examined at the DNA, mRNA, and protein level
    • Macartney-Coxson, D. P., Hood, K. A., Shi, H. J., Ward, T., Wiles, A., O'Connor, R., Hall, D. A., Lea, R. A., Royds, J. A., Stubbs, R. S., and Rooker, S. (2008) Metastatic susceptibility locus, an 8p hot-spot for tumour progression disrupted in colorectal liver metastases: 13 candidate genes examined at the DNA, mRNA, and protein level. BMC Cancer 8, 187
    • (2008) BMC Cancer , vol.8 , pp. 187
    • Macartney-Coxson, D.P.1    Hood, K.A.2    Shi, H.J.3    Ward, T.4    Wiles, A.5    O'Connor, R.6    Hall, D.A.7    Lea, R.A.8    Royds, J.A.9    Stubbs, R.S.10    Rooker, S.11
  • 19
    • 0037406622 scopus 로고    scopus 로고
    • Decysin, a new member of the metalloproteinase family, is regulated by prolactin and steroids during mouse pregnancy
    • Baran, N., Kelly, P. A., and Binart, N. (2003) Decysin, a new member of the metalloproteinase family, is regulated by prolactin and steroids during mouse pregnancy. Biol. Reprod. 68, 1787-1792
    • (2003) Biol. Reprod. , vol.68 , pp. 1787-1792
    • Baran, N.1    Kelly, P.A.2    Binart, N.3
  • 22
    • 0025195721 scopus 로고
    • Localization of ε-lysyl-γ-glutamyl cross-links in five human α2-macroglobulin-proteinase complexes: Nature of the high molecular weight cross-linked products
    • Sottrup-Jensen, L., Hansen, H. F., Pedersen, H. S., and Kristensen, L. (1990) Localization of ε-lysyl-γ-glutamyl cross-links in five human α2-macroglobulin-proteinase complexes: nature of the high molecular weight cross-linked products. J. Biol. Chem. 265, 17727-17737
    • (1990) J. Biol. Chem. , vol.265 , pp. 17727-17737
    • Sottrup-Jensen, L.1    Hansen, H.F.2    Pedersen, H.S.3    Kristensen, L.4
  • 25
    • 0033603356 scopus 로고    scopus 로고
    • ADAMTS-1 is an active metalloproteinase associated with the extracellular matrix
    • Kuno, K., Terashima, Y., and Matsushima, K. (1999) ADAMTS-1 is an active metalloproteinase associated with the extracellular matrix. J. Biol. Chem. 274, 18821-18826
    • (1999) J. Biol. Chem. , vol.274 , pp. 18821-18826
    • Kuno, K.1    Terashima, Y.2    Matsushima, K.3
  • 27
    • 0035430436 scopus 로고    scopus 로고
    • Regulation of the α-secretase ADAM10 by its prodomain and proprotein convertases
    • Anders, A., Gilbert, S., Garten, W., Postina, R., and Fahrenholz, F. (2001) Regulation of the α-secretase ADAM10 by its prodomain and proprotein convertases. FASEB J. 15, 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
  • 28
    • 0033532144 scopus 로고    scopus 로고
    • Regulation of human ADAM 12 protease by the prodomain: Evidence for a functional cysteine switch
    • Loechel, F., Overgaard, M. T., Oxvig, C., Albrechtsen, R., and Wewer, U. M. (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    Overgaard, M.T.2    Oxvig, C.3    Albrechtsen, R.4    Wewer, U.M.5
  • 29
    • 0032475960 scopus 로고    scopus 로고
    • Intracellular maturation of the mouse metalloprotease disintegrin MDC15
    • Lum, L., Reid, M. S., and Blobel, C. P. (1998) Intracellular maturation of the mouse metalloprotease disintegrin MDC15. J. Biol. Chem. 273, 26236 -26247
    • (1998) J. Biol. Chem. , vol.273 , pp. 26236-26247
    • Lum, L.1    Reid, M.S.2    Blobel, C.P.3
  • 30
    • 0037716445 scopus 로고    scopus 로고
    • Tumor necrosis factor-α 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. (2003) Tumor necrosis factor-α converting enzyme is processed by proprotein-convertases to its mature form which is degraded upon phorbol ester stimulation. Eur. J. Biochem. 270, 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
  • 31
    • 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. (2002) 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, 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
  • 33
    • 0034657228 scopus 로고    scopus 로고
    • Cloning and characterization of ADAM28: Evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28
    • Howard, L., Maciewicz, R. A., and Blobel, C. P. (2000) Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28. Biochem. J. 348, 21-27
    • (2000) Biochem. J. , vol.348 , pp. 21-27
    • Howard, L.1    Maciewicz, R.A.2    Blobel, C.P.3
  • 34
    • 0024333351 scopus 로고
    • α-Macroglobulins: Structure, shape, and mechanism of proteinase complex formation
    • Sottrup-Jensen, L. (1989) α-Macroglobulins: structure, shape, and mechanism of proteinase complex formation. J. Biol. Chem. 264, 11539-11542
    • (1989) J. Biol. Chem. , vol.264 , pp. 11539-11542
    • Sottrup-Jensen, L.1
  • 35
    • 59649103248 scopus 로고    scopus 로고
    • N-Glycans of ADAMTS13 modulate its secretion and von Willebrand factor cleaving activity
    • Zhou, W., and Tsai, H. (2009) N-Glycans of ADAMTS13 modulate its secretion and von Willebrand factor cleaving activity. Blood 113, 929-935
    • (2009) Blood , vol.113 , pp. 929-935
    • Zhou, W.1    Tsai, H.2
  • 36
    • 0027383275 scopus 로고
    • Efficiency of N-linked core glycosylation at asparagine-319 of rabies virus glycoprotein is altered by deletions C-terminal to the glycosylation sequon
    • Shakin-Eshleman, S. H., Wunner, W. H., and Spitalnik, S. L. (1993) Efficiency of N-linked core glycosylation at asparagine-319 of rabies virus glycoprotein is altered by deletions C-terminal to the glycosylation sequon. Biochemistry 32, 9465-9472
    • (1993) Biochemistry , vol.32 , pp. 9465-9472
    • Shakin-Eshleman, S.H.1    Wunner, W.H.2    Spitalnik, S.L.3
  • 37
    • 0034625413 scopus 로고    scopus 로고
    • Glycosylation efficiency of Asn-Xaa-Thr sequons depends both on the distance from theCterminus and on the presence of a downstream transmembrane segment
    • Nilsson, I., and von Heijne, G. (2000) Glycosylation efficiency of Asn-Xaa-Thr sequons depends both on the distance from theCterminus and on the presence of a downstream transmembrane segment. J. Biol. Chem. 275, 17338-17343
    • (2000) J. Biol. Chem. , vol.275 , pp. 17338-17343
    • Nilsson, I.1    Von Heijne, G.2
  • 38
    • 0033452452 scopus 로고    scopus 로고
    • Proprotein and prohormone convertases: A family of subtilases generating diverse bioactive polypeptides
    • Seidah, N. G., and Chrétien, M. (1999) Proprotein and prohormone convertases: a family of subtilases generating diverse bioactive polypeptides. Brain Res. 848, 45-62
    • (1999) Brain Res. , vol.848 , pp. 45-62
    • Seidah, N.G.1    Chrétien, M.2
  • 39
    • 84859426282 scopus 로고    scopus 로고
    • MEROPS: The database of proteolytic enzymes, their substrates and inhibitors
    • Rawlings, N. D., Barrett, A. J., and Bateman, A. (2012) MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res. 40, D343-D350
    • (2012) Nucleic Acids Res. , vol.40
    • Rawlings, N.D.1    Barrett, A.J.2    Bateman, A.3
  • 40
    • 0034055985 scopus 로고    scopus 로고
    • Function and mechanism of zinc metalloenzymes
    • McCall, K. A., Huang, C., and Fierke, C. A. (2000) Function and mechanism of zinc metalloenzymes. J. Nutr. 130, 1437S-1446S
    • (2000) J. Nutr. , vol.130
    • McCall, K.A.1    Huang, C.2    Fierke, C.A.3
  • 41
    • 0028589527 scopus 로고
    • Structural consequences of redesigning a protein-zinc binding site
    • Ippolito, J. A., and Christianson, D. W. (1994) Structural consequences of redesigning a protein-zinc binding site. Biochemistry 33, 15241-15249
    • (1994) Biochemistry , vol.33 , pp. 15241-15249
    • Ippolito, J.A.1    Christianson, D.W.2
  • 42
    • 0027818618 scopus 로고
    • Redesigning the zinc binding site of human carbonic anhydrase II: Structure of a His2Asp-Zn2+ metal coordination polyhedron
    • Kiefer, L. L., Ippolito, J. A., Fierke, C. A., and Christianson, D. W. (1993) Redesigning the zinc binding site of human carbonic anhydrase II: structure of a His2Asp-Zn2+ metal coordination polyhedron. J. Am. Chem. Soc. 115, 12581-12582
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 12581-12582
    • Kiefer, L.L.1    Ippolito, J.A.2    Fierke, C.A.3    Christianson, D.W.4
  • 44
    • 0026716149 scopus 로고
    • Cloning and sequencing of a gene encoding a novel extracellular neutral proteinase from Streptomyces sp. strain C5 and expression of the gene in Streptomyces lividans 1326
    • Lampel, J. S., Aphale, J. S., Lampel, K. A., and Strohl, W. R. (1992) Cloning and sequencing of a gene encoding a novel extracellular neutral proteinase from Streptomyces sp. strain C5 and expression of the gene in Streptomyces lividans 1326. J. Bacteriol. 174, 2797-2808
    • (1992) J. Bacteriol. , vol.174 , pp. 2797-2808
    • Lampel, J.S.1    Aphale, J.S.2    Lampel, K.A.3    Strohl, W.R.4
  • 45
    • 0030794567 scopus 로고    scopus 로고
    • Characterization of a small metalloprotease from Streptomyces caespitosus with high specificity to aromatic residues
    • Kurisu, G., Sugimoto, A., Harada, S., Takagi, M., Imanaka, T., and Kai, Y. (1997) Characterization of a small metalloprotease from Streptomyces caespitosus with high specificity to aromatic residues. J. Ferment. Bioeng. 83, 590-592
    • (1997) J. Ferment. Bioeng. , vol.83 , pp. 590-592
    • Kurisu, G.1    Sugimoto, A.2    Harada, S.3    Takagi, M.4    Imanaka, T.5    Kai, Y.6
  • 46
    • 0033741863 scopus 로고    scopus 로고
    • Structure of the zinc-binding site in the crystal structure of a zinc endoprotease from Streptomyces caespitosus at 1 Ä resolution
    • Kurisu, G., Kai, Y., and Harada, S. (2000) Structure of the zinc-binding site in the crystal structure of a zinc endoprotease from Streptomyces caespitosus at 1 Ä resolution. J Inorg Biochem. 82, 225-228
    • (2000) J Inorg Biochem. , vol.82 , pp. 225-228
    • Kurisu, G.1    Kai, Y.2    Harada, S.3
  • 47
    • 0018690723 scopus 로고
    • Heat-induced fragmentation of human α2-macroglobulin
    • Harpel, P. C., Hayes, M. B., and Hugli, T. E. (1979) Heat-induced fragmentation of human α2-macroglobulin. J. Biol. Chem. 254, 8669-8678
    • (1979) J. Biol. Chem. , vol.254 , pp. 8669-8678
    • Harpel, P.C.1    Hayes, M.B.2    Hugli, T.E.3


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