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Volumn 18, Issue 20, 2009, Pages 3987-3996

Potential late-onset Alzheimer's disease-associated mutations in the ADAM10 gene attenuate α-secretase activity

Author keywords

[No Author keywords available]

Indexed keywords

ADAM PROTEIN; ADAM10 PROTEIN; ALPHA SECRETASE; AMYLOID BETA PROTEIN; PROTEIN KINASE C; UNCLASSIFIED DRUG;

EID: 70349569016     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddp323     Document Type: Article
Times cited : (192)

References (48)
  • 1
    • 0024395366 scopus 로고
    • Secreted form of amyloid beta protein precursor is involved in the growth regulation of fibroblasts
    • Saitoh, T., Sundsmo, M., Roch, J.M., Kimura, N., Cole, G., Schubert, D., Oltersdorf, T. and Schenk, D.B. (1989) Secreted form of amyloid beta protein precursor is involved in the growth regulation of fibroblasts. Cell, 58, 615-622.
    • (1989) Cell , vol.58 , pp. 615-622
    • Saitoh, T.1    Sundsmo, M.2    Roch, J.M.3    Kimura, N.4    Cole, G.5    Schubert, D.6    Oltersdorf, T.7    Schenk, D.B.8
  • 2
    • 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., Fox, M. and Mattson, M.P. (1996) 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, 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    Fox, M.7    Mattson, M.P.8
  • 3
    • 0032514633 scopus 로고    scopus 로고
    • Memory-enhancing effects of secreted forms of the beta-amyloid precursor protein in normal and amnestic mice
    • Meziane, H., Dodart, J.C., Mathis, C., Little, S., Clemens, J., Paul, S.M. and Ungerer, A. (1998) Memory-enhancing effects of secreted forms of the beta-amyloid precursor protein in normal and amnestic mice. Proc. Natl Acad. Sci. USA, 95, 12683-12688.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12683-12688
    • Meziane, H.1    Dodart, J.C.2    Mathis, C.3    Little, S.4    Clemens, J.5    Paul, S.M.6    Ungerer, A.7
  • 4
    • 0344483869 scopus 로고    scopus 로고
    • Secreted form of amyloid precursor protein enhances basal glucose and glutamate transport and protects against oxidative impairment of glucose and glutamate transport in synaptosomes by a cyclic GMP-mediated mechanism
    • Mattson, M.P., Guo, Z.H. and Geiger, J.D. (1999) Secreted form of amyloid precursor protein enhances basal glucose and glutamate transport and protects against oxidative impairment of glucose and glutamate transport in synaptosomes by a cyclic GMP-mediated mechanism. J. Neurochem., 73, 532-537.
    • (1999) J. Neurochem , vol.73 , pp. 532-537
    • Mattson, M.P.1    Guo, Z.H.2    Geiger, J.D.3
  • 5
    • 0026448114 scopus 로고
    • Cholinergic agonists and interleukin 1 regulate processing and secretion of the Alzheimer beta/A4 amyloid protein precursor
    • Buxbaum, J.D., Oishi, M., Chen, H.I., Pinkas-Kramarski, R., Jaffe, E.A., Gandy, S.E. and Greengard, P. (1992) Cholinergic agonists and interleukin 1 regulate processing and secretion of the Alzheimer beta/A4 amyloid protein precursor. Proc. Natl Acad. Sci. USA, 89, 10075-10078.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10075-10078
    • Buxbaum, J.D.1    Oishi, M.2    Chen, H.I.3    Pinkas-Kramarski, R.4    Jaffe, E.A.5    Gandy, S.E.6    Greengard, P.7
  • 6
    • 0029379605 scopus 로고
    • Processing of the beta-amyloid precursor protein and its regulation in Alzheimer's disease
    • Checler, F. (1995) Processing of the beta-amyloid precursor protein and its regulation in Alzheimer's disease. J. Neurochem., 65, 1431-1444.
    • (1995) J. Neurochem , vol.65 , pp. 1431-1444
    • Checler, F.1
  • 7
    • 0032710361 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase is involved in N-methyl-D-aspartate receptor regulation of amyloid precursor protein cleavage
    • Mills, J. and Reiner, P.B. (1999) Mitogen-activated protein kinase is involved in N-methyl-D-aspartate receptor regulation of amyloid precursor protein cleavage. Neuroscience, 94, 1333-1338.
    • (1999) Neuroscience , vol.94 , pp. 1333-1338
    • Mills, J.1    Reiner, P.B.2
  • 9
    • 0027435535 scopus 로고
    • Protein phosphorylation inhibits production of Alzheimer amyloid beta/A4 peptide
    • Buxbaum, J.D., Koo, E.H. and Greengard, P. (1993) Protein phosphorylation inhibits production of Alzheimer amyloid beta/A4 peptide. Proc. Natl Acad. Sci. USA, 90, 9195-9198.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9195-9198
    • Buxbaum, J.D.1    Koo, E.H.2    Greengard, P.3
  • 10
    • 0027332657 scopus 로고
    • Inhibition of beta-amyloid production by activation of protein kinase C
    • Gabuzda, D., Busciglio, J. and Yankner, B.A. (1993) Inhibition of beta-amyloid production by activation of protein kinase C. J. Neurochem., 61, 2326-2329.
    • (1993) J. Neurochem , vol.61 , pp. 2326-2329
    • Gabuzda, D.1    Busciglio, J.2    Yankner, B.A.3
  • 13
    • 0028030517 scopus 로고
    • Regulated cleavage of the Alzheimer amyloid precursor protein: Molecular and cellular basis
    • Gandy, S. and Greengard, P. (1994) Regulated cleavage of the Alzheimer amyloid precursor protein: Molecular and cellular basis. Biochimie 76, 300-303.
    • (1994) Biochimie , vol.76 , pp. 300-303
    • Gandy, S.1    Greengard, P.2
  • 14
    • 0242330374 scopus 로고    scopus 로고
    • ADAMs family members as amyloid precursor protein alpha-secretases
    • Allinson, T.M., Parkin, E.T., Turner, A.J. and Hooper, N.M. (2003) ADAMs family members as amyloid precursor protein alpha-secretases. J. Neurosci. Res., 74, 342-352.
    • (2003) J. Neurosci. Res , vol.74 , pp. 342-352
    • Allinson, T.M.1    Parkin, E.T.2    Turner, A.J.3    Hooper, N.M.4
  • 16
    • 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., Johnson, R.S., Castner, B.J., Cerretti, D.P. and Black, R.A. (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    Liu, K.N.2    Luo, Y.3    Slack, J.L.4    Stocking, K.L.5    Peschon, J.J.6    Johnson, R.S.7    Castner, B.J.8    Cerretti, D.P.9    Black, R.A.10
  • 17
    • 0032544723 scopus 로고    scopus 로고
    • Pro-tumor necrosis factor-alpha processing activity is tightly controlled by a component that does not affect notch processing
    • Merlos-Suarez, A., Fernandez-Larrea, J., Reddy, P., Baselga, J. and Arribas, J. (1998) Pro-tumor necrosis factor-alpha processing activity is tightly controlled by a component that does not affect notch processing. J. Biol. Chem., 273, 24955-24962.
    • (1998) J. Biol. Chem , vol.273 , pp. 24955-24962
    • Merlos-Suarez, A.1    Fernandez-Larrea, J.2    Reddy, P.3    Baselga, J.4    Arribas, J.5
  • 18
    • 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. and Blobel, C.P. (2002) Mice lacking the metalloprotease-disintegrin MDC9 (ADAM9) have no evident major abnormalities during development or adult life. Mol. Cell. Biol., 22, 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    Blobel, C.P.7
  • 19
    • 0035089318 scopus 로고    scopus 로고
    • Constitutive alpha-secretase cleavage of the beta-amyloid precursor protein in the furin-deficient LoVo cell line: Involvement of the pro-hormone convertase 7 and the disintegrin metalloprotease ADAM10
    • Lopez-Perez, E., Zhang, Y., Frank, S.J., Creemers, J., Seidah, N. and Checler, F. (2001) Constitutive alpha-secretase cleavage of the beta-amyloid precursor protein in the furin-deficient LoVo cell line: involvement of the pro-hormone convertase 7 and the disintegrin metalloprotease ADAM10. J. Neurochem., 76, 1532-1539.
    • (2001) J. Neurochem , vol.76 , pp. 1532-1539
    • Lopez-Perez, E.1    Zhang, Y.2    Frank, S.J.3    Creemers, J.4    Seidah, N.5    Checler, F.6
  • 21
    • 18744364692 scopus 로고    scopus 로고
    • Effect of tumor necrosis factor-alpha converting enzyme (TACE) and metalloprotease inhibitor on amyloid precursor protein metabolism in human neurons
    • Blacker, M., Noe, M.C., Carty, T.J., Goodyer, C.G. and LeBlanc, A.C. (2002) Effect of tumor necrosis factor-alpha converting enzyme (TACE) and metalloprotease inhibitor on amyloid precursor protein metabolism in human neurons. J. Neurochem., 83, 1349-1357.
    • (2002) J. Neurochem , vol.83 , pp. 1349-1357
    • Blacker, M.1    Noe, M.C.2    Carty, T.J.3    Goodyer, C.G.4    LeBlanc, A.C.5
  • 22
    • 0035930617 scopus 로고    scopus 로고
    • Metalloprotease-dependent protransforming growth factor-alpha ectodomain shedding in the absence of tumor necrosis factor-alpha-converting enzyme
    • Merlos-Suarez, A., Ruiz-Paz, S., Baselga, J. and Arribas, J. (2001) Metalloprotease-dependent protransforming growth factor-alpha ectodomain shedding in the absence of tumor necrosis factor-alpha-converting enzyme. J. Biol. Chem., 276, 48510-48517.
    • (2001) J. Biol. Chem , vol.276 , pp. 48510-48517
    • Merlos-Suarez, A.1    Ruiz-Paz, S.2    Baselga, J.3    Arribas, J.4
  • 23
    • 33750156019 scopus 로고    scopus 로고
    • Alpha-secretase activation - an approach to Alzheimer's disease therapy
    • Fahrenholz, F. and Postina, R. (2006) Alpha-secretase activation - an approach to Alzheimer's disease therapy. Neurodegener. Dis., 3 255-261.
    • (2006) Neurodegener. Dis , vol.3 , pp. 255-261
    • Fahrenholz, F.1    Postina, R.2
  • 24
    • 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. (2000) 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, 2133-2143.
    • (2000) J. Neurochem , vol.75 , pp. 2133-2143
    • Marcinkiewicz, M.1    Seidah, N.G.2
  • 27
    • 0037224740 scopus 로고    scopus 로고
    • The ADAMs family of metalloproteases: Multidomain proteins with multiple functions
    • Seals, D.F. and Courtneidge, S.A. (2003) The ADAMs family of metalloproteases: Multidomain proteins with multiple functions. Genes Dev., 17, 7-30.
    • (2003) Genes Dev , vol.17 , pp. 7-30
    • Seals, D.F.1    Courtneidge, S.A.2
  • 28
    • 0025025442 scopus 로고
    • The cysteine switch: A principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family
    • Van Wart, H.E. and Birkedal-Hansen, H. (1990) The cysteine switch: A principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family. Proc. Natl Acad. Sci. USA, 87, 5578-5582.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal-Hansen, H.2
  • 29
    • 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. (2001) Regulation of the alpha-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
  • 30
    • 33845892752 scopus 로고    scopus 로고
    • Systematic meta-analyses of Alzheimer disease genetic association studies: The AlzGene database
    • Bertram, L., McQueen, M.B., Mullin, K., Blacker, D. and Tanzi, R.E. (2007) Systematic meta-analyses of Alzheimer disease genetic association studies: The AlzGene database. Nat. Genet., 39, 17-23.
    • (2007) Nat. Genet , vol.39 , pp. 17-23
    • Bertram, L.1    McQueen, M.B.2    Mullin, K.3    Blacker, D.4    Tanzi, R.E.5
  • 35
    • 34249949113 scopus 로고    scopus 로고
    • Kauwe, J.S., Jacquart, S., Chakraverty, S., Wang, J., Mayo, K., Fagan, A.M., Holtzman, D.M., Morris, J.C. and Goate, A.M. (2007) Extreme cerebrospinal fluid amyloid beta levels identify family with late-onset Alzheimer's disease presenilin 1 mutation. Ann. Neurol., 61, 446-453.
    • Kauwe, J.S., Jacquart, S., Chakraverty, S., Wang, J., Mayo, K., Fagan, A.M., Holtzman, D.M., Morris, J.C. and Goate, A.M. (2007) Extreme cerebrospinal fluid amyloid beta levels identify family with late-onset Alzheimer's disease presenilin 1 mutation. Ann. Neurol., 61, 446-453.
  • 36
    • 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. (2008) Part-time alpha-secretases: the functional biology of ADAM 9, 10 and 17. Curr. Alzheimer Res., 5, 187-201.
    • (2008) Curr. Alzheimer Res , vol.5 , pp. 187-201
    • Deuss, M.1    Reiss, K.2    Hartmann, D.3
  • 37
    • 40849130843 scopus 로고    scopus 로고
    • Effects of neuron-specific ADAM10 modulation in an in vivo model of acute excitotoxic stress
    • Clement, A.B., Hanstein, R., Schroder, A., Nagel, H., Endres, K., Fahrenholz, F. and Behl, C. (2008) Effects of neuron-specific ADAM10 modulation in an in vivo model of acute excitotoxic stress. Neuroscience, 152, 459-468.
    • (2008) Neuroscience , vol.152 , pp. 459-468
    • Clement, A.B.1    Hanstein, R.2    Schroder, A.3    Nagel, H.4    Endres, K.5    Fahrenholz, F.6    Behl, C.7
  • 38
    • 0034723418 scopus 로고    scopus 로고
    • Protein kinase C-dependent alpha-secretase competes with beta-secretase for cleavage of amyloid-beta precursor protein in the trans-golgi network
    • Skovronsky, D.M., Moore, D.B., Milla, M.E., Doms, R.W. and Lee, V.M. (2000) Protein kinase C-dependent alpha-secretase competes with beta-secretase for cleavage of amyloid-beta precursor protein in the trans-golgi network. J. Biol. Chem., 275, 2568-2575.
    • (2000) J. Biol. Chem , vol.275 , pp. 2568-2575
    • Skovronsky, D.M.1    Moore, D.B.2    Milla, M.E.3    Doms, R.W.4    Lee, V.M.5
  • 39
    • 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
  • 41
    • 18844374886 scopus 로고    scopus 로고
    • Chaperone-like properties of the prodomain of TNFalpha-converting enzyme (TACE) and the functional role of its cysteine switch
    • Leonard, J.D., Lin, F. and Milla, M.E. (2005) Chaperone-like properties of the prodomain of TNFalpha-converting enzyme (TACE) and the functional role of its cysteine switch. Biochem. J., 387, 797-805.
    • (2005) Biochem. J , vol.387 , pp. 797-805
    • Leonard, J.D.1    Lin, F.2    Milla, M.E.3
  • 42
    • 0021271971 scopus 로고
    • Clinical diagnosis of Alzheimer's disease: Report of the NINCDS-ADRDA Work Group under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease
    • McKhann, G., Drachman, D., Folstein, M., Katzman, R., Price, D. and Stadlan, E.M. (1984) Clinical diagnosis of Alzheimer's disease: Report of the NINCDS-ADRDA Work Group under the auspices of Department of Health and Human Services Task Force on Alzheimer's Disease. Neurology, 34, 939-944.
    • (1984) Neurology , vol.34 , pp. 939-944
    • McKhann, G.1    Drachman, D.2    Folstein, M.3    Katzman, R.4    Price, D.5    Stadlan, E.M.6
  • 43
    • 0027961102 scopus 로고
    • Reliability and validity of NINCDS-ADRDA criteria for Alzheimer's disease. The National Institute of Mental Health Genetics Initiative
    • Blacker, D., Albert, M.S., Bassett, S.S., Go, R.C., Harrell, L.E. and Folstein, M.F. (1994) Reliability and validity of NINCDS-ADRDA criteria for Alzheimer's disease. The National Institute of Mental Health Genetics Initiative. Arch. Neurol., 51, 1198-1204.
    • (1994) Arch. Neurol , vol.51 , pp. 1198-1204
    • Blacker, D.1    Albert, M.S.2    Bassett, S.S.3    Go, R.C.4    Harrell, L.E.5    Folstein, M.F.6
  • 46
    • 25144437529 scopus 로고    scopus 로고
    • Dynamite extended: Two new services to simplify protein dynamic analysis
    • Barrett, C.P. and Noble, M.E. (2005) Dynamite extended: Two new services to simplify protein dynamic analysis. Bioinformatics, 21, 3174-3175.
    • (2005) Bioinformatics , vol.21 , pp. 3174-3175
    • Barrett, C.P.1    Noble, M.E.2


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