메뉴 건너뛰기




Volumn 43, Issue 3, 2003, Pages 191-196

Increased plasma levels of matrix metalloproteinase-9 in patients with Alzheimer's disease

Author keywords

Alzheimer's disease; Amyotrophic lateral sclerosis; Matrix metalloproteinases; Parkinson's disease; Tissue inhibitors of metalloproteinases

Indexed keywords

APOLIPOPROTEIN E; GELATINASE A; GELATINASE B; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TISSUE INHIBITOR OF METALLOPROTEINASE 2;

EID: 0037411793     PISSN: 01970186     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0197-0186(03)00004-4     Document Type: Article
Times cited : (197)

References (34)
  • 1
    • 0033624419 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in aging and neurodegenerative
    • Albers D.S., Beal M.F. Mitochondrial dysfunction and oxidative stress in aging and neurodegenerative. J. Neural Trans. Suppl. 59:2000;133-154.
    • (2000) J. Neural Trans. Suppl. , vol.59 , pp. 133-154
    • Albers, D.S.1    Beal, M.F.2
  • 2
    • 0033638508 scopus 로고    scopus 로고
    • Role for matrix metalloproteinase-9 after focal cerebral ischemia: Effects of gene knockout and enzyme inhibition with BB-94
    • Asahi M., Asahi K., Jung J.C., del Zoppo G.J., Fini M.E., Lo E.H. Role for matrix metalloproteinase-9 after focal cerebral ischemia: effects of gene knockout and enzyme inhibition with BB-94. J. Cereb. Blood Flow Metab. 20:2000;1681-1689.
    • (2000) J. Cereb. Blood Flow Metab. , vol.20 , pp. 1681-1689
    • Asahi, M.1    Asahi, K.2    Jung, J.C.3    Del Zoppo, G.J.4    Fini, M.E.5    Lo, E.H.6
  • 3
    • 0035478029 scopus 로고    scopus 로고
    • Effects of matrix metalloproteinase-9 gene knock-out on the proteolysis of blood-brain barrier and white matter components after cerebral ischemia
    • Asahi M., Wang X., Mori T., Sumii T., Jung J.C., Moskowitz M.A., Fini M.E., Lo E.H. Effects of matrix metalloproteinase-9 gene knock-out on the proteolysis of blood-brain barrier and white matter components after cerebral ischemia. J. Neurosci. 21:2001;7724-7732.
    • (2001) J. Neurosci. , vol.21 , pp. 7724-7732
    • Asahi, M.1    Wang, X.2    Mori, T.3    Sumii, T.4    Jung, J.C.5    Moskowitz, M.A.6    Fini, M.E.7    Lo, E.H.8
  • 4
    • 0035083370 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinase-9 and urinary-type plasminogen activator in Alzheimer's disease brain
    • Asahina M., Yoshiyama Y., 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
  • 5
    • 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., 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
  • 6
    • 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., 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
  • 7
    • 0034626855 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 is elevated in serum of patients with amyotrophic lateral sclerosis
    • Beuche W., Yushchenko M., Mader M., Maliszewska M., Felgenhauer K., Weber F. Matrix metalloproteinase-9 is elevated in serum of patients with amyotrophic lateral sclerosis. Neuroreport. 11:2000;3419-3422.
    • (2000) Neuroreport , vol.11 , pp. 3419-3422
    • Beuche, W.1    Yushchenko, M.2    Mader, M.3    Maliszewska, M.4    Felgenhauer, K.5    Weber, F.6
  • 9
    • 0034615550 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases: Evolution, structure and function
    • Brew K., Dinakarpandian D., Nagase H. Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochim. Biophys. Acta. 1477:2000;267-283.
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 267-283
    • Brew, K.1    Dinakarpandian, D.2    Nagase, H.3
  • 10
    • 0028142392 scopus 로고
    • El Escorial World Federation of Neurology criteria for the diagnosis of amyotrophic lateral sclerosis. Subcommittee on Motor Neuron Diseases/Amyotrophic Lateral Sclerosis of the World Federation of Neurology Research Group on Neuromuscular Diseases and the El Escorial "Clinical limits of amyotrophic lateral sclerosis" workshop contributors
    • Brooks B.R. El Escorial World Federation of Neurology criteria for the diagnosis of amyotrophic lateral sclerosis. Subcommittee on Motor Neuron Diseases/Amyotrophic Lateral Sclerosis of the World Federation of Neurology Research Group on Neuromuscular Diseases and the El Escorial "Clinical limits of amyotrophic lateral sclerosis" workshop contributors. J. Neurol. Sci. 124(Suppl.):1994;96-107.
    • (1994) J. Neurol. Sci. , vol.124 , Issue.SUPPL. , pp. 96-107
    • Brooks, B.R.1
  • 11
    • 0035968225 scopus 로고    scopus 로고
    • Effects of the beta-amyloid and carboxyl-terminal fragment of Alzheimer's amyloid precursor protein on the production of the tumor necrosis factor-alpha and matrix metalloproteinase-9 by human monocytic THP-1
    • Chong Y.H., Sung J.H., Shin S.A., Chung J.H., Suh Y.H. Effects of the beta-amyloid and carboxyl-terminal fragment of Alzheimer's amyloid precursor protein on the production of the tumor necrosis factor-alpha and matrix metalloproteinase-9 by human monocytic THP-1. J. Biol. Chem. 276:2001;23511-23517.
    • (2001) J. Biol. Chem. , vol.276 , pp. 23511-23517
    • Chong, Y.H.1    Sung, J.H.2    Shin, S.A.3    Chung, J.H.4    Suh, Y.H.5
  • 12
    • 0031459856 scopus 로고    scopus 로고
    • Increased gelatinase A (MMP-2) and gelatinase B (MMP-9) activities in human brain after focal ischemia
    • Clark A.W., Krekoski C.A., Bou S.S., Chapman K.R., Edwards D.R. Increased gelatinase A (MMP-2) and gelatinase B (MMP-9) activities in human brain after focal ischemia. Neurosci. Lett. 238:1997;53-56.
    • (1997) Neurosci. Lett. , vol.238 , pp. 53-56
    • Clark, A.W.1    Krekoski, C.A.2    Bou, S.S.3    Chapman, K.R.4    Edwards, D.R.5
  • 13
    • 0029829594 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinase expressions in astrocytes, microglia and neurons
    • Gottschall P.E., 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
  • 14
    • 0014082977 scopus 로고
    • Parkinsonism: Onset, progression and mortality
    • Hoehn M.M., Yahr M.D. Parkinsonism: onset, progression and mortality. Neurology. 17:1967;427-442.
    • (1967) Neurology , vol.17 , pp. 427-442
    • Hoehn, M.M.1    Yahr, M.D.2
  • 17
    • 0032522261 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases in viral meningitis: Upregulation of MMP-9 and TIMP-1 in cerebrospinal fluid
    • Kolb S.A., Lahrtz F., Paul R., Leppert D., Nadal D., Pfister H.W., Fontana A. Matrix metalloproteinases and tissue inhibitors of metalloproteinases in viral meningitis: upregulation of MMP-9 and TIMP-1 in cerebrospinal fluid. J. Neuroimmunol. 84:1998;143-150.
    • (1998) J. Neuroimmunol. , vol.84 , pp. 143-150
    • Kolb, S.A.1    Lahrtz, F.2    Paul, R.3    Leppert, D.4    Nadal, D.5    Pfister, H.W.6    Fontana, A.7
  • 18
    • 0029417131 scopus 로고
    • Gelatinase A possesses a beta-secretase-like activity in cleaving the amyloid protein precursor of Alzheimer's disease
    • LePage R.N., Fosang A.J., Fuller S.J., Murphy G., Evin G., Beyreuther K., Masters C.L., Small D.H. Gelatinase A possesses a beta-secretase-like activity in cleaving the amyloid protein precursor of Alzheimer's disease. FEBS Lett. 377:1995;267-270.
    • (1995) FEBS Lett. , vol.377 , pp. 267-270
    • LePage, R.N.1    Fosang, A.J.2    Fuller, S.J.3    Murphy, G.4    Evin, G.5    Beyreuther, K.6    Masters, C.L.7    Small, D.H.8
  • 19
    • 0031798063 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 (gelatinase B) is selectively elevated in CSF during relapses and stable phases of multiple sclerosis
    • Leppert D., Ford J., Stabler G., Grygar C., Lienert C., Huber S., Miller K.M., Hauser S.L., Kappos L. Matrix metalloproteinase-9 (gelatinase B) is selectively elevated in CSF during relapses and stable phases of multiple sclerosis. Brain. 121:1998;2327-2334.
    • (1998) Brain , vol.121 , pp. 2327-2334
    • Leppert, D.1    Ford, J.2    Stabler, G.3    Grygar, C.4    Lienert, C.5    Huber, S.6    Miller, K.M.7    Hauser, S.L.8    Kappos, L.9
  • 20
    • 0031593604 scopus 로고    scopus 로고
    • Mechanisms of cell death in Alzheimer's disease - Immunopathology
    • McGeer P.L., McGeer E.G. Mechanisms of cell death in Alzheimer's disease - immunopathology. J. Neural Trans. Suppl. 54:1998;159-166.
    • (1998) J. Neural Trans. Suppl. , vol.54 , pp. 159-166
    • McGeer, P.L.1    McGeer, E.G.2
  • 21
    • 0027254060 scopus 로고
    • A metalloproteinase inhibitor domain in Alzheimer amyloid protein precursor
    • Miyazaki K., Hasegawa M., Funahashi K., Umeda M. A metalloproteinase inhibitor domain in Alzheimer amyloid protein precursor. Nature. 362:1993;839-841.
    • (1993) Nature , vol.362 , pp. 839-841
    • Miyazaki, K.1    Hasegawa, M.2    Funahashi, K.3    Umeda, M.4
  • 22
    • 0027014484 scopus 로고
    • Characterization of metalloproteinases and tissue inhibitors of metalloproteinases in human plasma
    • Moutsiakis D., Mancuso P., Krutzsch H., Stetler-Stevenson W., Zucker S. Characterization of metalloproteinases and tissue inhibitors of metalloproteinases in human plasma. Connect Tissue Res. 28:1992;213-230.
    • (1992) Connect Tissue Res. , vol.28 , pp. 213-230
    • Moutsiakis, D.1    Mancuso, P.2    Krutzsch, H.3    Stetler-Stevenson, W.4    Zucker, S.5
  • 23
    • 0034910719 scopus 로고    scopus 로고
    • Induction of oxidative stress by homocyst(e)ine impairs endothelial function
    • Mujumdar V.S., Aru G.M., Tyagi S.C. Induction of oxidative stress by homocyst(e)ine impairs endothelial function. J. Cell. Biochem. 82:2001;491-500.
    • (2001) J. Cell. Biochem. , vol.82 , pp. 491-500
    • Mujumdar, V.S.1    Aru, G.M.2    Tyagi, S.C.3
  • 24
    • 0035800858 scopus 로고    scopus 로고
    • Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation
    • Okamoto T., Akaike T., Sawa T., Miyamoto Y., van der Vliet A., Maeda H. Activation of matrix metalloproteinases by peroxynitrite-induced protein S-glutathiolation via disulfide S-oxide formation. J. Biol. Chem. 276:2001;29596-29602.
    • (2001) J. Biol. Chem. , vol.276 , pp. 29596-29602
    • Okamoto, T.1    Akaike, T.2    Sawa, T.3    Miyamoto, Y.4    Van der Vliet, A.5    Maeda, H.6
  • 25
    • 0031723106 scopus 로고    scopus 로고
    • Matrix metalloproteinases contribute to the blood-brain barrier disruption during bacterial meningitis
    • Paul R., Lorenzl S., Koedel U., Sporer B., Vogel U., Frosch M., Pfister H.W. Matrix metalloproteinases contribute to the blood-brain barrier disruption during bacterial meningitis. Ann. Neurol. 44:1998;592-600.
    • (1998) Ann. Neurol. , vol.44 , pp. 592-600
    • Paul, R.1    Lorenzl, S.2    Koedel, U.3    Sporer, B.4    Vogel, U.5    Frosch, M.6    Pfister, H.W.7
  • 26
    • 0028895806 scopus 로고
    • Localization of tissue inhibitor of matrix metalloproteinases in Alzheimer's disease and normal brain
    • Peress N., Perillo E., Zucker S. Localization of tissue inhibitor of matrix metalloproteinases in Alzheimer's disease and normal brain. J. Neuropathol. Exp. Neurol. 54:1995;16-22.
    • (1995) J. Neuropathol. Exp. Neurol. , vol.54 , pp. 16-22
    • Peress, N.1    Perillo, E.2    Zucker, S.3
  • 27
    • 0033762711 scopus 로고    scopus 로고
    • Increased 8,12-iso-iPF2alpha-VI in Alzheimer's disease: Correlation of a noninvasive index of lipid peroxidation with disease severity
    • Pratico D., Clark C.M., Lee V.M., Trojanowski J.Q., Rokach J., FitzGerald G.A. Increased 8,12-iso-iPF2alpha-VI in Alzheimer's disease: correlation of a noninvasive index of lipid peroxidation with disease severity. Ann. Neurol. 48:2000;809-812.
    • (2000) Ann. Neurol. , vol.48 , pp. 809-812
    • Pratico, D.1    Clark, C.M.2    Lee, V.M.3    Trojanowski, J.Q.4    Rokach, J.5    FitzGerald, G.A.6
  • 28
    • 0025770134 scopus 로고
    • The distribution of tangles, plaques and related immunohistochemical markers in healthy aging and Alzheimer's disease
    • Price J.L., Davis P.B., Morris J.C., White D.L. The distribution of tangles, plaques and related immunohistochemical markers in healthy aging and Alzheimer's disease. Neurobiol. Aging. 12:1991;295-312.
    • (1991) Neurobiol. Aging , vol.12 , pp. 295-312
    • Price, J.L.1    Davis, P.B.2    Morris, J.C.3    White, D.L.4
  • 29
    • 0033088484 scopus 로고    scopus 로고
    • Human neutrophils secrete gelatinase B in vitro and in vivo in response to endotoxin and proinflammatory mediators
    • Pugin J., Widmer M.C., Kossodo S., Liang C.M., Preas H.L.n., Suffredini A.F. Human neutrophils secrete gelatinase B in vitro and in vivo in response to endotoxin and proinflammatory mediators. Am. J. Respir. Cell. Mol. 20:1999;458-464.
    • (1999) Am. J. Respir. Cell. Mol. , vol.20 , pp. 458-464
    • Pugin, J.1    Widmer, M.C.2    Kossodo, S.3    Liang, C.M.4    Preas, H.L.n.5    Suffredini, A.F.6
  • 30
    • 0035003439 scopus 로고    scopus 로고
    • Chemistry and biochemistry of oxidative stress in neurodegenerative disease
    • Sayre L.M., Smith M.A., Perry G. Chemistry and biochemistry of oxidative stress in neurodegenerative disease. Curr. Med. Chem. 8:2001;721-738.
    • (2001) Curr. Med. Chem. , vol.8 , pp. 721-738
    • Sayre, L.M.1    Smith, M.A.2    Perry, G.3
  • 32
    • 0035405886 scopus 로고    scopus 로고
    • Metalloproteinases in biology and pathology of the nervous system
    • Yong V.W., Power C., Forsyth P., Edwards D.R. Metalloproteinases in biology and pathology of the nervous system. Nat. Rev. Neurosci. 2:2001;502-511.
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 502-511
    • Yong, V.W.1    Power, C.2    Forsyth, P.3    Edwards, D.R.4
  • 33
    • 0034597152 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 (MMP-9) in human cerebrospinal fluid (CSF): Elevated levels are primarily related to CSF cell count
    • Yushchenko M., Weber F., Mader M., Scholl U., Maliszewska M., Tumani H., Felgenhauer K., Beuche W. Matrix metalloproteinase-9 (MMP-9) in human cerebrospinal fluid (CSF): elevated levels are primarily related to CSF cell count. J. Neuroimmunol. 110:2000;244-251.
    • (2000) J. Neuroimmunol. , vol.110 , pp. 244-251
    • Yushchenko, M.1    Weber, F.2    Mader, M.3    Scholl, U.4    Maliszewska, M.5    Tumani, H.6    Felgenhauer, K.7    Beuche, W.8
  • 34
    • 0032836427 scopus 로고    scopus 로고
    • Measurement of matrix metalloproteinases and tissue inhibitors of metalloproteinases in blood and tissues. Clinical and experimental applications
    • Zucker S., Hymowitz M., Conner C., Zarrabi H.M., Hurewitz A.N., Matrisian L., Boyd D., Nicolson G., Montana S. Measurement of matrix metalloproteinases and tissue inhibitors of metalloproteinases in blood and tissues. Clinical and experimental applications. Ann. N. Y. Acad. Sci. 878:1999;212-227.
    • (1999) Ann. N. Y. Acad. Sci. , vol.878 , pp. 212-227
    • Zucker, S.1    Hymowitz, M.2    Conner, C.3    Zarrabi, H.M.4    Hurewitz, A.N.5    Matrisian, L.6    Boyd, D.7    Nicolson, G.8    Montana, S.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.