메뉴 건너뛰기




Volumn 28, Issue 3, 2007, Pages 304-315

Abeta(1-40)-induced secretion of matrix metalloproteinase-9 results in sAPPα release by association with cell surface APP

Author keywords

Alzheimer; Amyloid beta peptide; Amyloid precursor protein; Integrin; MMP 9; Secretase

Indexed keywords

ALPHA SECRETASE; ALPHA2BETA1 INTEGRIN RECEPTOR; ALPHA3BETA1 INTEGRIN RECEPTOR; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID PRECURSOR PROTEIN; AMYLOID PRECURSOR PROTEIN 695; AMYLOID PRECURSOR PROTEIN ALPHA; EDETIC ACID; GELATINASE B; GELATINASE INHIBITOR; INTEGRIN RECEPTOR; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN PRECURSOR; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

EID: 36249015501     PISSN: 09699961     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.nbd.2007.07.016     Document Type: Article
Times cited : (42)

References (53)
  • 2
    • 33646379384 scopus 로고    scopus 로고
    • Cleavage of amyloid-beta precursor protein (APP) by membrane-type matrix metalloproteinases
    • Ahmad M., Takino T., Miyamori H., Yoshizaki T., Furukawa M., and Sato H. Cleavage of amyloid-beta precursor protein (APP) by membrane-type matrix metalloproteinases. J. Biochem. (Tokyo) 139 (2006) 517-526
    • (2006) J. Biochem. (Tokyo) , vol.139 , pp. 517-526
    • Ahmad, M.1    Takino, T.2    Miyamori, H.3    Yoshizaki, T.4    Furukawa, M.5    Sato, H.6
  • 4
  • 5
    • 0035083370 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase-9 and urinary-type plasminogen activator in Alzheimer's disease brain
    • Asahina M., Yoshiyama Y., and Hattori T. Expression of matrix metalloproteinase-9 and urinary-type plasminogen activator in Alzheimer's disease brain. Clin. Neuropathol. 20 (2001) 60-63
    • (2001) Clin. Neuropathol. , vol.20 , pp. 60-63
    • Asahina, M.1    Yoshiyama, Y.2    Hattori, T.3
  • 6
    • 0026597204 scopus 로고
    • Characterization of neutral proteinases from Alzheimer-affected and control brain specimens: identification of calcium-dependent metalloproteinases from the hippocampus
    • Backstrom J.R., Miller C.A., and Tokes Z.A. Characterization of neutral proteinases from Alzheimer-affected and control brain specimens: identification of calcium-dependent metalloproteinases from the hippocampus. J. Neurochem. 58 (1992) 983-992
    • (1992) J. Neurochem. , vol.58 , pp. 983-992
    • Backstrom, J.R.1    Miller, C.A.2    Tokes, Z.A.3
  • 7
    • 0029852887 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-beta peptide (1-40)
    • Backstrom J.R., Lim G.P., Cullen M.J., and Tokes Z.A. Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-beta peptide (1-40). J. Neurosci. 16 (1996) 7910-7919
    • (1996) J. Neurosci. , vol.16 , pp. 7910-7919
    • Backstrom, J.R.1    Lim, G.P.2    Cullen, M.J.3    Tokes, Z.A.4
  • 8
    • 0031808063 scopus 로고    scopus 로고
    • CD44v(3,8-10) is involved in cytoskeleton-mediated tumor cell migration and matrix metalloproteinase (MMP-9) association in metastatic breast cancer cells
    • Bourguignon L.Y., Gunja-Smith Z., Iida N., Zhu H.B., Young L.J., Muller W.J., and Cardiff R.D. CD44v(3,8-10) is involved in cytoskeleton-mediated tumor cell migration and matrix metalloproteinase (MMP-9) association in metastatic breast cancer cells. J. Cell. Physiol. 176 (1998) 206-215
    • (1998) J. Cell. Physiol. , vol.176 , pp. 206-215
    • Bourguignon, L.Y.1    Gunja-Smith, Z.2    Iida, N.3    Zhu, H.B.4    Young, L.J.5    Muller, W.J.6    Cardiff, R.D.7
  • 9
    • 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. 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    Johnson, R.S.7    Castner, B.J.8    Cerretti, D.P.9    Black, R.A.10
  • 11
    • 0029988699 scopus 로고    scopus 로고
    • Increased production of matrix metalloproteinases in enriched astrocyte and mixed hippocampal cultures treated with beta-amyloid peptides
    • Deb S., and Gottschall P.E. Increased production of matrix metalloproteinases in enriched astrocyte and mixed hippocampal cultures treated with beta-amyloid peptides. J. Neurochem. 66 (1996) 1641-1647
    • (1996) J. Neurochem. , vol.66 , pp. 1641-1647
    • Deb, S.1    Gottschall, P.E.2
  • 12
    • 0037466395 scopus 로고    scopus 로고
    • Beta-amyloid induces the production of active, matrix-degrading proteases in cultured rat astrocytes
    • Deb S., Wenjun Zhang J., and Gottschall P.E. Beta-amyloid induces the production of active, matrix-degrading proteases in cultured rat astrocytes. Brain Res. 970 (2003) 205-213
    • (2003) Brain Res. , vol.970 , pp. 205-213
    • Deb, S.1    Wenjun Zhang, J.2    Gottschall, P.E.3
  • 13
    • 0033829605 scopus 로고    scopus 로고
    • Mouse keratinocytes immortalized with large T antigen acquire alpha3beta1 integrin-dependent secretion of MMP-9/gelatinase B
    • DiPersio C.M., Shao M., Di Costanzo L., Kreidberg J.A., and Hynes R.O. Mouse keratinocytes immortalized with large T antigen acquire alpha3beta1 integrin-dependent secretion of MMP-9/gelatinase B. J. Cell. Sci. 113 Pt 16 (2000) 2909-2921
    • (2000) J. Cell. Sci. , vol.113 , Issue.PART 16 , pp. 2909-2921
    • DiPersio, C.M.1    Shao, M.2    Di Costanzo, L.3    Kreidberg, J.A.4    Hynes, R.O.5
  • 14
    • 0028296661 scopus 로고
    • Study of the phorbol ester effect on Alzheimer amyloid precursor processing: sequence requirements and involvement of a cholera toxin sensitive protein
    • Efthimiopoulos S., Felsenstein K.M., Sambamurti K., Robakis N.K., and Refolo L.M. Study of the phorbol ester effect on Alzheimer amyloid precursor processing: sequence requirements and involvement of a cholera toxin sensitive protein. J. Neurosci. Res. 38 (1994) 81-90
    • (1994) J. Neurosci. Res. , vol.38 , pp. 81-90
    • Efthimiopoulos, S.1    Felsenstein, K.M.2    Sambamurti, K.3    Robakis, N.K.4    Refolo, L.M.5
  • 15
    • 0028276177 scopus 로고
    • Cellular and substrate adhesion molecules (integrins) and their ligands in cerebral amyloid plaques in Alzheimer's disease
    • Eikelenboom P., Zhan S.S., Kamphorst W., van der Valk P., and Rozemuller J.M. Cellular and substrate adhesion molecules (integrins) and their ligands in cerebral amyloid plaques in Alzheimer's disease. Virchows Arch. 424 (1994) 421-427
    • (1994) Virchows Arch. , vol.424 , pp. 421-427
    • Eikelenboom, P.1    Zhan, S.S.2    Kamphorst, W.3    van der Valk, P.4    Rozemuller, J.M.5
  • 17
    • 0027076090 scopus 로고
    • Normal processing of the Alzheimer's disease amyloid beta protein precursor generates potentially amyloidogenic carboxyl-terminal derivatives
    • Estus S., Golde T.E., and Younkin S.G. Normal processing of the Alzheimer's disease amyloid beta protein precursor generates potentially amyloidogenic carboxyl-terminal derivatives. Ann. N. Y. Acad. Sci. 674 (1992) 138-148
    • (1992) Ann. N. Y. Acad. Sci. , vol.674 , pp. 138-148
    • Estus, S.1    Golde, T.E.2    Younkin, S.G.3
  • 18
    • 0037043820 scopus 로고    scopus 로고
    • Matrix metalloproteinase 9 (MMP-9/gelatinase B) proteolytically cleaves ICAM-1 and participates in tumor cell resistance to natural killer cell-mediated cytotoxicity
    • Fiore E., Fusco C., Romero P., and Stamenkovic I. Matrix metalloproteinase 9 (MMP-9/gelatinase B) proteolytically cleaves ICAM-1 and participates in tumor cell resistance to natural killer cell-mediated cytotoxicity. Oncogene 21 (2002) 5213-5223
    • (2002) Oncogene , vol.21 , pp. 5213-5223
    • Fiore, E.1    Fusco, C.2    Romero, P.3    Stamenkovic, I.4
  • 19
    • 0029034457 scopus 로고
    • Activation of progelatinase B (MMP-9) by gelatinase A (MMP-2)
    • Fridman R., Toth M., Pena D., and Mobashery S. Activation of progelatinase B (MMP-9) by gelatinase A (MMP-2). Cancer Res. 55 (1995) 2548-2555
    • (1995) Cancer Res. , vol.55 , pp. 2548-2555
    • Fridman, R.1    Toth, M.2    Pena, D.3    Mobashery, S.4
  • 20
    • 0030581638 scopus 로고    scopus 로고
    • Carbohydrate-mediated regulation of matrix metalloproteinase-2 activation in normal human fibroblasts and fibrosarcoma cells
    • Gervasi D.C., Raz A., Dehem M., Yang M., Kurkinen M., and Fridman R. Carbohydrate-mediated regulation of matrix metalloproteinase-2 activation in normal human fibroblasts and fibrosarcoma cells. Biochem. Biophys. Res. Commun. 228 (1996) 530-538
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 530-538
    • Gervasi, D.C.1    Raz, A.2    Dehem, M.3    Yang, M.4    Kurkinen, M.5    Fridman, R.6
  • 21
    • 0027082156 scopus 로고
    • A 109-amino-acid C-terminal fragment of Alzheimer's-disease amyloid precursor protein contains a sequence, - RHDS -, that promotes cell adhesion
    • Ghiso J., Rostagno A., Gardella J.E., Liem L., Gorevic P.D., and Frangione B. A 109-amino-acid C-terminal fragment of Alzheimer's-disease amyloid precursor protein contains a sequence, - RHDS -, that promotes cell adhesion. Biochem. J. 288 Pt 3 (1992) 1053-1059
    • (1992) Biochem. J. , vol.288 , Issue.PART 3 , pp. 1053-1059
    • Ghiso, J.1    Rostagno, A.2    Gardella, J.E.3    Liem, L.4    Gorevic, P.D.5    Frangione, B.6
  • 22
    • 0023506466 scopus 로고
    • Isolation, characterization, and chromosomal localization of human brain cDNA clones coding for the precursor of the amyloid of brain in Alzheimer's disease, Down's syndrome and aging
    • Goldgaber D., Lerman M.I., McBride W.O., Saffiotti U., and Gajdusek D.C. Isolation, characterization, and chromosomal localization of human brain cDNA clones coding for the precursor of the amyloid of brain in Alzheimer's disease, Down's syndrome and aging. J. Neural Transm., Suppl. 24 (1987) 23-28
    • (1987) J. Neural Transm., Suppl. , vol.24 , pp. 23-28
    • Goldgaber, D.1    Lerman, M.I.2    McBride, W.O.3    Saffiotti, U.4    Gajdusek, D.C.5
  • 23
    • 0029829594 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase expressions in astrocytes, microglia and neurons
    • Gottschall P.E., and Deb S. Regulation of matrix metalloproteinase expressions in astrocytes, microglia and neurons. Neuroimmunomodulation 3 (1996) 69-75
    • (1996) Neuroimmunomodulation , vol.3 , pp. 69-75
    • Gottschall, P.E.1    Deb, S.2
  • 24
    • 21844450866 scopus 로고    scopus 로고
    • A highly specific inhibitor of matrix metalloproteinase-9 rescues laminin from proteolysis and neurons from apoptosis in transient focal cerebral ischemia
    • Gu Z., Cui J., Brown S., Fridman R., Mobashery S., Strongin A.Y., and Lipton S.A. A highly specific inhibitor of matrix metalloproteinase-9 rescues laminin from proteolysis and neurons from apoptosis in transient focal cerebral ischemia. J. Neurosci. 25 (2005) 6401-6408
    • (2005) J. Neurosci. , vol.25 , pp. 6401-6408
    • Gu, Z.1    Cui, J.2    Brown, S.3    Fridman, R.4    Mobashery, S.5    Strongin, A.Y.6    Lipton, S.A.7
  • 27
    • 0035907387 scopus 로고    scopus 로고
    • X-ray absorption studies of human matrix metalloproteinase-2 (MMP-2) bound to a highly selective mechanism-based inhibitor. comparison with the latent and active forms of the enzyme
    • Kleifeld O., Kotra L.P., Gervasi D.C., Brown S., Bernardo M.M., Fridman R., Mobashery S., and Sagi I. X-ray absorption studies of human matrix metalloproteinase-2 (MMP-2) bound to a highly selective mechanism-based inhibitor. comparison with the latent and active forms of the enzyme. J. Biol. Chem. 276 (2001) 17125-17131
    • (2001) J. Biol. Chem. , vol.276 , pp. 17125-17131
    • Kleifeld, O.1    Kotra, L.P.2    Gervasi, D.C.3    Brown, S.4    Bernardo, M.M.5    Fridman, R.6    Mobashery, S.7    Sagi, I.8
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0029585289 scopus 로고
    • Collagen and collagenase gene expression in three-dimensional collagen lattices are differentially regulated by alpha 1 beta 1 and alpha 2 beta 1 integrins
    • Langholz O., Rockel D., Mauch C., Kozlowska E., Bank I., Krieg T., and Eckes B. Collagen and collagenase gene expression in three-dimensional collagen lattices are differentially regulated by alpha 1 beta 1 and alpha 2 beta 1 integrins. J. Cell Biol. 131 (1995) 1903-1915
    • (1995) J. Cell Biol. , vol.131 , pp. 1903-1915
    • Langholz, O.1    Rockel, D.2    Mauch, C.3    Kozlowska, E.4    Bank, I.5    Krieg, T.6    Eckes, B.7
  • 33
    • 0034703594 scopus 로고    scopus 로고
    • Brain matrix metalloproteinase 1 levels are elevated in Alzheimer's disease
    • Leake A., Morris C.M., and Whateley J. Brain matrix metalloproteinase 1 levels are elevated in Alzheimer's disease. Neurosci. Lett. 291 (2000) 201-203
    • (2000) Neurosci. Lett. , vol.291 , pp. 201-203
    • Leake, A.1    Morris, C.M.2    Whateley, J.3
  • 35
    • 0031596988 scopus 로고    scopus 로고
    • The alpha5beta1 integrin mediates elimination of amyloid-beta peptide and protects against apoptosis
    • Matter M.L., Zhang Z., Nordstedt C., and Ruoslahti E. The alpha5beta1 integrin mediates elimination of amyloid-beta peptide and protects against apoptosis. J. Cell Biol. 141 (1998) 1019-1030
    • (1998) J. Cell Biol. , vol.141 , pp. 1019-1030
    • Matter, M.L.1    Zhang, Z.2    Nordstedt, C.3    Ruoslahti, E.4
  • 36
    • 0030779677 scopus 로고    scopus 로고
    • Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives
    • Mattson M.P. Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives. Physiol. Rev. 77 (1997) 1081-1132
    • (1997) Physiol. Rev. , vol.77 , pp. 1081-1132
    • Mattson, M.P.1
  • 37
    • 0030977009 scopus 로고    scopus 로고
    • Control of type IV collagenase activity by components of the urokinase-plasmin system: a regulatory mechanism with cell-bound reactants
    • Mazzieri R., Masiero L., Zanetta L., Monea S., Onisto M., Garbisa S., and Mignatti P. Control of type IV collagenase activity by components of the urokinase-plasmin system: a regulatory mechanism with cell-bound reactants. EMBO J. 16 (1997) 2319-2332
    • (1997) EMBO J. , vol.16 , pp. 2319-2332
    • Mazzieri, R.1    Masiero, L.2    Zanetta, L.3    Monea, S.4    Onisto, M.5    Garbisa, S.6    Mignatti, P.7
  • 38
  • 39
    • 0033532205 scopus 로고    scopus 로고
    • Activation of matrix metalloproteinase-9 (MMP-9) via a converging plasmin/stromelysin-1 cascade enhances tumor cell invasion
    • Ramos-DeSimone N., Hahn-Dantona E., Sipley J., Nagase H., French D.L., and Quigley J.P. Activation of matrix metalloproteinase-9 (MMP-9) via a converging plasmin/stromelysin-1 cascade enhances tumor cell invasion. J. Biol. Chem. 274 (1999) 13066-13076
    • (1999) J. Biol. Chem. , vol.274 , pp. 13066-13076
    • Ramos-DeSimone, N.1    Hahn-Dantona, E.2    Sipley, J.3    Nagase, H.4    French, D.L.5    Quigley, J.P.6
  • 40
    • 2142777413 scopus 로고
    • Molecular cloning and characterization of a cDNA encoding the cerebrovascular and the neuritic plaque amyloid peptides
    • Robakis N.K., Ramakrishna N., Wolfe G., and Wisniewski H.M. Molecular cloning and characterization of a cDNA encoding the cerebrovascular and the neuritic plaque amyloid peptides. Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 4190-4194
    • (1987) Proc. Natl. Acad. Sci. U. S. A. , vol.84 , pp. 4190-4194
    • Robakis, N.K.1    Ramakrishna, N.2    Wolfe, G.3    Wisniewski, H.M.4
  • 41
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: genes, proteins, and therapy
    • Selkoe D.J. Alzheimer's disease: genes, proteins, and therapy. Physiol. Rev. 81 (2001) 741-766
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 42
    • 0001067847 scopus 로고
    • Beta-amyloid precursor protein of Alzheimer disease occurs as 110- to 135-kilodalton membrane-associated proteins in neural and nonneural tissues
    • Selkoe D.J., Podlisny M.B., Joachim C.L., Vickers E.A., Lee G., Fritz L.C., and Oltersdorf T. Beta-amyloid precursor protein of Alzheimer disease occurs as 110- to 135-kilodalton membrane-associated proteins in neural and nonneural tissues. Proc. Natl. Acad. Sci. U. S. A. 85 (1988) 7341-7345
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 7341-7345
    • Selkoe, D.J.1    Podlisny, M.B.2    Joachim, C.L.3    Vickers, E.A.4    Lee, G.5    Fritz, L.C.6    Oltersdorf, T.7
  • 45
    • 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., Matsuura N., and Higashiyama S. 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    Matsuura, N.7    Higashiyama, S.8
  • 46
    • 0030755456 scopus 로고    scopus 로고
    • Phorbol ester-induced cell surface association of matrix metalloproteinase-9 in human MCF10A breast epithelial cells
    • Toth M., Gervasi D.C., and Fridman R. Phorbol ester-induced cell surface association of matrix metalloproteinase-9 in human MCF10A breast epithelial cells. Cancer Res. 57 (1997) 3159-3167
    • (1997) Cancer Res. , vol.57 , pp. 3159-3167
    • Toth, M.1    Gervasi, D.C.2    Fridman, R.3
  • 47
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., and Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 4350-4354
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 49
    • 0030715322 scopus 로고    scopus 로고
    • ECM and cell surface proteolysis: regulating cellular ecology
    • Werb Z. ECM and cell surface proteolysis: regulating cellular ecology. Cell 91 (1997) 439-442
    • (1997) Cell , vol.91 , pp. 439-442
    • Werb, Z.1
  • 52
    • 0032926177 scopus 로고    scopus 로고
    • Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion
    • Yu Q., and Stamenkovic I. Localization of matrix metalloproteinase 9 to the cell surface provides a mechanism for CD44-mediated tumor invasion. Genes Dev. 13 (1999) 35-48
    • (1999) Genes Dev. , vol.13 , pp. 35-48
    • Yu, Q.1    Stamenkovic, I.2
  • 53
    • 0034650486 scopus 로고    scopus 로고
    • Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis
    • Yu Q., and Stamenkovic I. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes Dev. 14 (2000) 163-176
    • (2000) Genes Dev. , vol.14 , pp. 163-176
    • Yu, Q.1    Stamenkovic, I.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.