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Volumn 89, Issue 12, 2009, Pages 1340-1347

Timp-3 deficiency impairs cognitive function in mice

Author keywords

Cognitive function; Extracellular matrix; Hippocampus; Matrix metalloproteinase; Timp 3

Indexed keywords

TISSUE INHIBITOR OF METALLOPROTEINASE 3;

EID: 70549102493     PISSN: 00236837     EISSN: 15300307     Source Type: Journal    
DOI: 10.1038/labinvest.2009.101     Document Type: Article
Times cited : (19)

References (38)
  • 1
    • 0037704306 scopus 로고    scopus 로고
    • Extracellular matrix molecules and synaptic plasticity
    • Dityatev A, Schachner M. Extracellular matrix molecules and synaptic plasticity. Nat Rev Neurosci 2003;4:456-468.
    • (2003) Nat Rev Neurosci , vol.4 , pp. 456-468
    • Dityatev, A.1    Schachner, M.2
  • 2
    • 33748932378 scopus 로고    scopus 로고
    • The extracellular matrix and synapses
    • Dityatev A, Schachner M. The extracellular matrix and synapses. Cell Tissue Res 2006;326:647-654.
    • (2006) Cell Tissue Res , vol.326 , pp. 647-654
    • Dityatev, A.1    Schachner, M.2
  • 3
    • 2342655011 scopus 로고    scopus 로고
    • The brain angiotensin system and extracellular matrix molecules in neural plasticity, learning, and memory
    • Wright JW, Harding JW. The brain angiotensin system and extracellular matrix molecules in neural plasticity, learning, and memory. Prog Neurobiol 2004;72:263-293.
    • (2004) Prog Neurobiol , vol.72 , pp. 263-293
    • Wright, J.W.1    Harding, J.W.2
  • 4
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase H, Woessner Jr JF. Matrix metalloproteinases. J Biol Chem 1999;274:21491-21494.
    • (1999) J Biol Chem , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner Jr, J.F.2
  • 5
    • 34347256340 scopus 로고    scopus 로고
    • The matrix metalloproteinases and CNS plasticity: An overview
    • Milward EA, Fitzsimmons C, Szklarczyk A, et al. The matrix metalloproteinases and CNS plasticity: an overview. J Neuroimmunol 2007;187:9-19.
    • (2007) J Neuroimmunol , vol.187 , pp. 9-19
    • Milward, E.A.1    Fitzsimmons, C.2    Szklarczyk, A.3
  • 6
    • 0038011833 scopus 로고    scopus 로고
    • Evolving concepts of rheumatoid arthritis
    • Firestein GS. Evolving concepts of rheumatoid arthritis. Nature 2003;423:356-361.
    • (2003) Nature , vol.423 , pp. 356-361
    • Firestein, G.S.1
  • 7
    • 0036867198 scopus 로고    scopus 로고
    • Possible roles of angiotensin II-forming enzymes, angiotensin converting enzyme and chymase-like enzyme, in the human aneurysmal aorta
    • Tsunemi K, Takai S, Nishimoto M, et al. Possible roles of angiotensin II-forming enzymes, angiotensin converting enzyme and chymase-like enzyme, in the human aneurysmal aorta. Hypertens Res 2002;25: 817-822.
    • (2002) Hypertens Res , vol.25 , pp. 817-822
    • Tsunemi, K.1    Takai, S.2    Nishimoto, M.3
  • 8
    • 0036188891 scopus 로고    scopus 로고
    • Influence of plasma aldosterone on left ventricular geometry and diastolic function in treated essential hypertension
    • Iwashima Y, Horio T, Kuroda S, et al. Influence of plasma aldosterone on left ventricular geometry and diastolic function in treated essential hypertension. Hypertens Res 2002;25:49-56.
    • (2002) Hypertens Res , vol.25 , pp. 49-56
    • Iwashima, Y.1    Horio, T.2    Kuroda, S.3
  • 9
    • 34447534193 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-3 deficiency inhibits blood pressure elevation and myocardial microvascular remodeling induced by chronic administration of Nomega-nitro-L-arginine methyl ester in mice
    • Higuchi M, Yasuda O, Kawamoto H, et al. Tissue inhibitor of metalloproteinase-3 deficiency inhibits blood pressure elevation and myocardial microvascular remodeling induced by chronic administration of Nomega-nitro-L-arginine methyl ester in mice. Hypertens Res 2007;30:563-571.
    • (2007) Hypertens Res , vol.30 , pp. 563-571
    • Higuchi, M.1    Yasuda, O.2    Kawamoto, H.3
  • 10
    • 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 2000;1477:267-283.
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 267-283
    • Brew, K.1    Dinakarpandian, D.2    Nagase, H.3
  • 11
    • 0028244447 scopus 로고
    • Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues
    • Leco KJ, Khokha R, Pavloff N, et al. Tissue inhibitor of metalloproteinases-3 (TIMP-3) is an extracellular matrix-associated protein with a distinctive pattern of expression in mouse cells and tissues. J Biol Chem 1994;269:9352-9360.
    • (1994) J Biol Chem , vol.269 , pp. 9352-9360
    • Leco, K.J.1    Khokha, R.2    Pavloff, N.3
  • 12
    • 15044351753 scopus 로고    scopus 로고
    • Cardiac remodeling and failure: From molecules to man (Part II)
    • DOI 10.1016/j.carpath.2005.01.005
    • Fedak PW, Verma S, Weisel RD, et al. Cardiac remodeling and failure: from molecules to man (Part II). Cardiovasc Pathol 2005;14:49-60. (Pubitemid 40381300)
    • (2005) Cardiovascular Pathology , vol.14 , Issue.2 , pp. 49-60
    • Fedak, P.W.M.1    Verma, S.2    Weisel, R.D.3    Li, R.-K.4
  • 14
    • 31344458952 scopus 로고    scopus 로고
    • Structure and function of matrix metalloproteinases and TIMPs
    • Nagase H, Visse R, Murphy G. Structure and function of matrix metalloproteinases and TIMPs. Cardiovasc Res 2006;69:562-573.
    • (2006) Cardiovasc Res , vol.69 , pp. 562-573
    • Nagase, H.1    Visse, R.2    Murphy, G.3
  • 15
    • 2542436756 scopus 로고    scopus 로고
    • Matrix metalloproteinases and their endogenous inhibitors in neuronal physiology of the adult brain
    • Dzwonek J, Rylski M, Kaczmarek L. Matrix metalloproteinases and their endogenous inhibitors in neuronal physiology of the adult brain. FEBS Lett 2004;567:129-135.
    • (2004) FEBS Lett , vol.567 , pp. 129-135
    • Dzwonek, J.1    Rylski, M.2    Kaczmarek, L.3
  • 16
    • 36849030749 scopus 로고    scopus 로고
    • MMPs in the central nervous system: Where the good guys go bad
    • Agrawal SM, Lau L, Yong VW. MMPs in the central nervous system: where the good guys go bad. Semin Cell Dev Biol 2008; 19:42-51.
    • (2008) Semin Cell Dev Biol , vol.19 , pp. 42-51
    • Agrawal, S.M.1    Lau, L.2    Yong, V.W.3
  • 17
    • 0035405886 scopus 로고    scopus 로고
    • Metalloproteinases in biology and pathology of the nervous system
    • Yong VW, Power C, Forsyth P, et al. Metalloproteinases in biology and pathology of the nervous system. Nat Rev Neurosci 2001;2: 502-511.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 502-511
    • Yong, V.W.1    Power, C.2    Forsyth, P.3
  • 18
    • 0032006878 scopus 로고    scopus 로고
    • Matrix metalloproteinases and diseases of the CNS
    • Yong VW, Krekoski CA, Forsyth PA, et al. Matrix metalloproteinases and diseases of the CNS. Trends Neurosci 1998;21:75-80.
    • (1998) Trends Neurosci , vol.21 , pp. 75-80
    • Yong, V.W.1    Krekoski, C.A.2    Forsyth, P.A.3
  • 19
    • 65349118139 scopus 로고    scopus 로고
    • Role of hyaluronan in glioma invasion
    • Park JB, Kwak HJ, Lee SH. Role of hyaluronan in glioma invasion. Cell Adh Migr 2008;2:202-207.
    • (2008) Cell Adh Migr , vol.2 , pp. 202-207
    • Park, J.B.1    Kwak, H.J.2    Lee, S.H.3
  • 20
    • 33746925663 scopus 로고    scopus 로고
    • MMP-12, MMP-3, and TIMP-1 are markedly upregulated in chronic demyelinating theiler murine encephalomyelitis
    • Ulrich R, Baumgartner W, Gerhauser I, et al. MMP-12, MMP-3, and TIMP-1 are markedly upregulated in chronic demyelinating theiler murine encephalomyelitis. J Neuropathol Exp Neurol 2006;65: 783-793.
    • (2006) J Neuropathol Exp Neurol , vol.65 , pp. 783-793
    • Ulrich, R.1    Baumgartner, W.2    Gerhauser, I.3
  • 21
    • 28644435880 scopus 로고    scopus 로고
    • Metalloproteinases: Mediators of pathology and regeneration in the CNS
    • Yong VW. Metalloproteinases: mediators of pathology and regeneration in the CNS. Nat Rev Neurosci 2005;6:931-944.
    • (2005) Nat Rev Neurosci , vol.6 , pp. 931-944
    • Yong, V.W.1
  • 22
    • 34547957954 scopus 로고    scopus 로고
    • Matrix metalloproteinases in brain development and remodeling: Synaptic functions and targets
    • Ethell IM, Ethell DW. Matrix metalloproteinases in brain development and remodeling: synaptic functions and targets. J Neurosci Res 2007;85:2813-2823.
    • (2007) J Neurosci Res , vol.85 , pp. 2813-2823
    • Ethell, I.M.1    Ethell, D.W.2
  • 23
    • 28744435937 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-1 (TIMP-1) modulates neuronal death, axonal plasticity, and learning and memory
    • Jourquin J, Tremblay E, Bernard A, et al. Tissue inhibitor of metalloproteinases-1 (TIMP-1) modulates neuronal death, axonal plasticity, and learning and memory. Eur J Neurosci 2005;22: 2569-2578.
    • (2005) Eur J Neurosci , vol.22 , pp. 2569-2578
    • Jourquin, J.1    Tremblay, E.2    Bernard, A.3
  • 24
    • 33748150993 scopus 로고    scopus 로고
    • Involvement of tissue inhibition of metalloproteinases-1 in learning and memory in mice
    • Chaillan FA, Rivera S, Marchetti E, et al. Involvement of tissue inhibition of metalloproteinases-1 in learning and memory in mice. Behav Brain Res 2006;173:191-198.
    • (2006) Behav Brain Res , vol.173 , pp. 191-198
    • Chaillan, F.A.1    Rivera, S.2    Marchetti, E.3
  • 25
    • 22144470855 scopus 로고    scopus 로고
    • Prepulse inhibition and fear-potentiated startle are altered in tissue inhibitor of metalloproteinase-2 (TIMP-2) knockout mice
    • Jaworski DM, Boone J, Caterina J, et al. Prepulse inhibition and fear-potentiated startle are altered in tissue inhibitor of metalloproteinase-2 (TIMP-2) knockout mice. Brain Res 2005;1051:81-89.
    • (2005) Brain Res , vol.1051 , pp. 81-89
    • Jaworski, D.M.1    Boone, J.2    Caterina, J.3
  • 26
    • 33744949958 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase-3 plays important roles in the kidney following unilateral ureteral obstruction
    • Kawamoto H, Yasuda O, Suzuki T, et al. Tissue inhibitor of metalloproteinase-3 plays important roles in the kidney following unilateral ureteral obstruction. Hypertens Res 2006;29:285-294.
    • (2006) Hypertens Res , vol.29 , pp. 285-294
    • Kawamoto, H.1    Yasuda, O.2    Suzuki, T.3
  • 27
    • 39749162072 scopus 로고    scopus 로고
    • Brain regional and cellular localization of gelatinase activity in rat that have undergone transient middle cerebral artery occlusion
    • Amantea D, Corasaniti MT, Mercuri NB, et al. Brain regional and cellular localization of gelatinase activity in rat that have undergone transient middle cerebral artery occlusion. Neuroscience 2008; 152:8-17.
    • (2008) Neuroscience , vol.152 , pp. 8-17
    • Amantea, D.1    Corasaniti, M.T.2    Mercuri, N.B.3
  • 28
    • 0037675000 scopus 로고    scopus 로고
    • In situ localization of gelatinolytic activity in the extracellular matrix of metastases of colon cancer in rat liver using quenched fluorogenic DQ-gelatin
    • Mook OR, Van Overbeek C, Ackema EG, et al. In situ localization of gelatinolytic activity in the extracellular matrix of metastases of colon cancer in rat liver using quenched fluorogenic DQ-gelatin. J Histochem Cytochem 2003;51:821-829.
    • (2003) J Histochem Cytochem , vol.51 , pp. 821-829
    • Mook, O.R.1    Van Overbeek, C.2    Ackema, E.G.3
  • 29
    • 0023866498 scopus 로고
    • Differences between inbred strains of mice in Morris water maze performance
    • Upchurch M, Wehner JM. Differences between inbred strains of mice in Morris water maze performance. Behav Genet 1988;18: 55-68.
    • (1988) Behav Genet , vol.18 , pp. 55-68
    • Upchurch, M.1    Wehner, J.M.2
  • 30
    • 0035813328 scopus 로고    scopus 로고
    • Immunoelectron microscopic localization of the neural recognition molecules L1, NCAM, and its isoform NCAM180, the NCAM-associated polysialic acid, beta1 integrin and the extracellular matrix molecule tenascin-R in synapses of the adult rat hippocampus
    • Schuster T, Krug M, Stalder M, et al. Immunoelectron microscopic localization of the neural recognition molecules L1, NCAM, and its isoform NCAM180, the NCAM-associated polysialic acid, beta1 integrin and the extracellular matrix molecule tenascin-R in synapses of the adult rat hippocampus. J Neurobiol 2001;49:142-158.
    • (2001) J Neurobiol , vol.49 , pp. 142-158
    • Schuster, T.1    Krug, M.2    Stalder, M.3
  • 31
    • 0242487406 scopus 로고    scopus 로고
    • Time-dependent reversal of long-term potentiation by an integrin antagonist
    • Staubli U, Chun D, Lynch G. Time-dependent reversal of long-term potentiation by an integrin antagonist. J Neurosci 1998;18: 3460-3469.
    • (1998) J Neurosci , vol.18 , pp. 3460-3469
    • Staubli, U.1    Chun, D.2    Lynch, G.3
  • 32
    • 0031889386 scopus 로고    scopus 로고
    • Differential expression of matrix metalloproteinase and tissue inhibitor of matrix metalloproteinase genes in the mouse central nervous system in normal and inflammatory states
    • Pagenstecher A, Stalder AK, Kincaid CL, et al. Differential expression of matrix metalloproteinase and tissue inhibitor of matrix metalloproteinase genes in the mouse central nervous system in normal and inflammatory states. Am J Pathol 1998;152:729-741.
    • (1998) Am J Pathol , vol.152 , pp. 729-741
    • Pagenstecher, A.1    Stalder, A.K.2    Kincaid, C.L.3
  • 33
    • 0034663489 scopus 로고    scopus 로고
    • Regulation of tissue inhibitor of metalloproteinase-3 (Timp-3) mRNA expression during rat CNS development
    • Jaworski DM, Fager N. Regulation of tissue inhibitor of metalloproteinase-3 (Timp-3) mRNA expression during rat CNS development. J Neurosci Res 2000;61:396-408.
    • (2000) J Neurosci Res , vol.61 , pp. 396-408
    • Jaworski, D.M.1    Fager, N.2
  • 34
    • 31044440813 scopus 로고    scopus 로고
    • TIMP3 mutation in Sorsby's fundus dystrophy: Molecular insights
    • Li Z, Clarke MP, Barker MD, et al. TIMP3 mutation in Sorsby's fundus dystrophy: molecular insights. Expert Rev Mol Med 2005;7:1-15.
    • (2005) Expert Rev Mol Med , vol.7 , pp. 1-15
    • Li, Z.1    Clarke, M.P.2    Barker, M.D.3
  • 35
    • 0034282898 scopus 로고    scopus 로고
    • A novel tissue inhibitor of metalloproteinases-3 mutation reveals a common molecular phenotype in Sorsby's fundus dystrophy
    • Langton KP, McKie N, Curtis A, et al. A novel tissue inhibitor of metalloproteinases-3 mutation reveals a common molecular phenotype in Sorsby's fundus dystrophy. J Biol Chem 2000;275:27027-27031.
    • (2000) J Biol Chem , vol.275 , pp. 27027-27031
    • Langton, K.P.1    McKie, N.2    Curtis, A.3
  • 36
    • 0031726862 scopus 로고    scopus 로고
    • Accumulation of tissue inhibitor of metalloproteinases-3 in human eyes with Sorsby's fundus dystrophy or retinitis pigmentosa
    • Fariss RN, Apte SS, Luthert PJ, et al. Accumulation of tissue inhibitor of metalloproteinases-3 in human eyes with Sorsby's fundus dystrophy or retinitis pigmentosa. Br J Ophthalmol 1998;82:1329-1334.
    • (1998) Br J Ophthalmol , vol.82 , pp. 1329-1334
    • Fariss, R.N.1    Apte, S.S.2    Luthert, P.J.3
  • 37
    • 6444240024 scopus 로고    scopus 로고
    • TIMP-3 deficiency leads to dilated cardiomyopathy
    • Fedak PW, Smookler DS, Kassiri Z, et al. TIMP-3 deficiency leads to dilated cardiomyopathy. Circulation 2004;110:2401-2409.
    • (2004) Circulation , vol.110 , pp. 2401-2409
    • Fedak, P.W.1    Smookler, D.S.2    Kassiri, Z.3
  • 38
    • 0034833362 scopus 로고    scopus 로고
    • Spontaneous air space enlargement in the lungs of mice lacking tissue inhibitor of metalloproteinases-3 (TIMP-3)
    • Leco KJ, Waterhouse P, Sanchez OH, et al. Spontaneous air space enlargement in the lungs of mice lacking tissue inhibitor of metalloproteinases-3 (TIMP-3). J Clin Invest 2001;108: 817-829.
    • (2001) J Clin Invest , vol.108 , pp. 817-829
    • Leco, K.J.1    Waterhouse, P.2    Sanchez, O.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.