메뉴 건너뛰기




Volumn 39, Issue 3, 2002, Pages 279-291

Matrix metalloproteinases in neuroinflammation

Author keywords

Matrix metalloproteinases; Neuroinflammation; TIMPs

Indexed keywords

MATRIX METALLOPROTEINASE;

EID: 0036737795     PISSN: 08941491     EISSN: None     Source Type: Journal    
DOI: 10.1002/glia.10108     Document Type: Article
Times cited : (762)

References (94)
  • 3
    • 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 JC, del Zoppo GJ, Fini ME, Lo EH. 2000. Role for matrix metalloproteinase 9 after focal cerebral ischemia: effects of gene knockout and enzyme inhibition with BB-94. J Cereb Blood Flow Metab 20:1681-1689.
    • (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
  • 4
    • 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 JC, Moskowitz MA, Fini ME, Lo EH. 2001. Effects of matrix metalloproteinase-9 gene knock-out on the proteolysis of blood-brain barrier and white matter components after cerebral ischemia. J Neurosci 21:7724-7732.
    • (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
  • 5
    • 0032521142 scopus 로고    scopus 로고
    • Divergent effects of tissue inhibitor of metalloproteinase-1, -2, or -3 overexpression on rat vascular smooth muscle cell invasion, proliferation, and death in vitro. TIMP-3 promotes apoptosis
    • Baker AH, Zaltsman AB, George SJ, Newby AC. 1998. Divergent effects of tissue inhibitor of metalloproteinase-1, -2, or -3 overexpression on rat vascular smooth muscle cell invasion, proliferation, and death in vitro. TIMP-3 promotes apoptosis. J Clin Invest 101:1478-1487.
    • (1998) J Clin Invest , vol.101 , pp. 1478-1487
    • Baker, A.H.1    Zaltsman, A.B.2    George, S.J.3    Newby, A.C.4
  • 6
    • 0028945629 scopus 로고
    • ECM degradation by cultured human mesangial cells is mediated by a PA/plasmin/MMP-2 cascade
    • Baricos WH, Cortez SL, el-Dahr SS, Schnaper HW. 1995. ECM degradation by cultured human mesangial cells is mediated by a PA/plasmin/MMP-2 cascade. Kidney Int 47:1039-1047.
    • (1995) Kidney Int , vol.47 , pp. 1039-1047
    • Baricos, W.H.1    Cortez, S.L.2    El-Dahr, S.S.3    Schnaper, H.W.4
  • 7
    • 0030480848 scopus 로고    scopus 로고
    • Characterization of a putative p53 binding site in the promoter of the mouse tissue inhibitor of metalloproteinases-3 (TIMP-3) gene: TIMP-3 is not a p53 target gene
    • Bian J, Jacobs C, Wang Y, Sun Y. 1996. Characterization of a putative p53 binding site in the promoter of the mouse tissue inhibitor of metalloproteinases-3 (TIMP-3) gene: TIMP-3 is not a p53 target gene. Carcinogenesis 17:2559-2562.
    • (1996) Carcinogenesis , vol.17 , pp. 2559-2562
    • Bian, J.1    Jacobs, C.2    Wang, Y.3    Sun, Y.4
  • 8
    • 0034615550 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases: Evolution, structure and function
    • Brew K, Dinakarpandian D, Nagase H. 2000. Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochim Biophys Acta 1477:267-283.
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 267-283
    • Brew, K.1    Dinakarpandian, D.2    Nagase, H.3
  • 9
    • 0002699681 scopus 로고    scopus 로고
    • Synthetic inhibitors of matrix metalloproteinases
    • Parks WC, Mecham RP, editors. San Diego, CA: Academic Press
    • Brown PD. 1998. Synthetic inhibitors of matrix metalloproteinases. In: Parks WC, Mecham RP, editors. Matrix metalloproteinases. San Diego, CA: Academic Press. p 243-262.
    • (1998) Matrix Metalloproteinases , pp. 243-262
    • Brown, P.D.1
  • 12
    • 0033152431 scopus 로고    scopus 로고
    • Electron microscopic evidence against apoptosis as the mechanism of neuronal death in global ischemia
    • Colbourne F, Sutherland GR, Auer RN. 1999. Electron microscopic evidence against apoptosis as the mechanism of neuronal death in global ischemia. J Neurosci 19:4200-4210.
    • (1999) J Neurosci , vol.19 , pp. 4200-4210
    • Colbourne, F.1    Sutherland, G.R.2    Auer, R.N.3
  • 13
    • 0027243871 scopus 로고
    • Protease production by cultured microglia: Substrate gel analysis and immobilized matrix degradation
    • Colton CA, Keri JE, Chen WT, Monsky WL. 1993. Protease production by cultured microglia: substrate gel analysis and immobilized matrix degradation. J Neurosci Res 35:297-304.
    • (1993) J Neurosci Res , vol.35 , pp. 297-304
    • Colton, C.A.1    Keri, J.E.2    Chen, W.T.3    Monsky, W.L.4
  • 14
    • 0033081796 scopus 로고    scopus 로고
    • Plasminogen activators and matrix metalloproteases, mediators of extracellular proteolysis in inflammatory demyelination of the central nervous system
    • Cuzner ML, Opdenakker G. 1999. Plasminogen activators and matrix metalloproteases, mediators of extracellular proteolysis in inflammatory demyelination of the central nervous system. J Neuroimmunol 94:1-14.
    • (1999) J Neuroimmunol , vol.94 , pp. 1-14
    • Cuzner, M.L.1    Opdenakker, G.2
  • 15
    • 0029907622 scopus 로고    scopus 로고
    • The expression of tissue-type plaminogen activator, matrix metalloproteases and endogenous inhibitor in the central nervous system in multiple sclerosis: Comparison of stages in lesion evolution
    • Cuzner ML, Gveric D, Strand C, Loughlin AJ, Paemen L, Opdenakker G, Newcombe J. 1996. The expression of tissue-type plaminogen activator, matrix metalloproteases and endogenous inhibitor in the central nervous system in multiple sclerosis: comparison of stages in lesion evolution. J Neuropathol Exp Neurol 55:1194-1209.
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 1194-1209
    • Cuzner, M.L.1    Gveric, D.2    Strand, C.3    Loughlin, A.J.4    Paemen, L.5    Opdenakker, G.6    Newcombe, J.7
  • 16
    • 0029988699 scopus 로고    scopus 로고
    • Increased production of matrix metalloproteinases in enriched astrocyte and mixed hippocampal cultures treated with beta- amyloid peptides
    • Deb S, Gottschall PE. 1996. Increased production of matrix metalloproteinases in enriched astrocyte and mixed hippocampal cultures treated with beta- amyloid peptides. J Neurochem 66:1641-1647.
    • (1996) J Neurochem , vol.66 , pp. 1641-1647
    • Deb, S.1    Gottschall, P.E.2
  • 17
    • 0030047274 scopus 로고    scopus 로고
    • Very delayed infarction after mild focal cerebral ischemia: A role for apoptosis?
    • Du C, Hu R, Csernansky CA, Hsu CY, Choi DW. 1996. Very delayed infarction after mild focal cerebral ischemia: a role for apoptosis? J Cereb Blood Flow Metab 16:195-201.
    • (1996) J Cereb Blood Flow Metab , vol.16 , pp. 195-201
    • Du, C.1    Hu, R.2    Csernansky, C.A.3    Hsu, C.Y.4    Choi, D.W.5
  • 19
    • 0034790897 scopus 로고    scopus 로고
    • Matrix metalloproteinases (MMPs) and their tissue inhibitor (TIMPs) as markers of disease subtype and response to interferon-beta therapy in relapsing and secondary progressive multiple sclerosis patients
    • Galboiz Y, Shapiro S, Lahat N, Rawashdeh H, Miller A.2001. Matrix metalloproteinases (MMPs) and their tissue inhibitor (TIMPs) as markers of disease subtype and response to interferon-beta therapy in relapsing and secondary progressive multiple sclerosis patients. Ann Neurol 50:443-451.
    • (2001) Ann Neurol , vol.50 , pp. 443-451
    • Galboiz, Y.1    Shapiro, S.2    Lahat, N.3    Rawashdeh, H.4    Miller, A.5
  • 20
    • 0033505281 scopus 로고    scopus 로고
    • Early appearance of activated matrix metalloproteinase-9 after focal cerebral ischemia in mice: A possible role in blood-brain barrier dysfunction
    • Gasche Y, Fujimura M, Morita-Fujimura Y, Copin JC, Kawase M, Massengale J, Chan PH. 1999. Early appearance of activated matrix metalloproteinase-9 after focal cerebral ischemia in mice: a possible role in blood-brain barrier dysfunction. J Cereb Blood Flow Metab 19:1020-1028.
    • (1999) J Cereb Blood Flow Metab , vol.19 , pp. 1020-1028
    • Gasche, Y.1    Fujimura, M.2    Morita-Fujimura, Y.3    Copin, J.C.4    Kawase, M.5    Massengale, J.6    Chan, P.H.7
  • 21
    • 0035194622 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibition prevents oxidative stress-associated blood-brain barrier disruption after transient focal cerebral ischemia
    • Gasche Y, Copin JC, Sugawara T, Fujimura M, Chan PH. 2001a. Matrix metalloproteinase inhibition prevents oxidative stress-associated blood-brain barrier disruption after transient focal cerebral ischemia. J Cereb Blood Flow Metab 21:1393-1400.
    • (2001) J Cereb Blood Flow Metab , vol.21 , pp. 1393-1400
    • Gasche, Y.1    Copin, J.C.2    Sugawara, T.3    Fujimura, M.4    Chan, P.H.5
  • 22
    • 0035194622 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibition prevents oxidative stress-associated blood-brain barrier disruption after transient focal cerebral ischemia
    • Gasche Y, Copin JC, Sugawara T, Fujimura M, Chan PH. 2001b. Matrix metalloproteinase inhibition prevents oxidative stress-associated blood-brain barrier disruption after transient focal cerebral ischemia. J Cereb Blood Flow Metab 21:1393-1400.
    • (2001) J Cereb Blood Flow Metab , vol.21 , pp. 1393-1400
    • Gasche, Y.1    Copin, J.C.2    Sugawara, T.3    Fujimura, M.4    Chan, P.H.5
  • 24
    • 0026442957 scopus 로고
    • Gelatinase in the cerebrospinal fluid of patients with multiple sclerosis and other inflammatory neurological disorders
    • Gijbels K, Masure S, Carton H, Opdenakker G. 1992. Gelatinase in the cerebrospinal fluid of patients with multiple sclerosis and other inflammatory neurological disorders. J Neuroimmunol 41:29-34.
    • (1992) J Neuroimmunol , vol.41 , pp. 29-34
    • Gijbels, K.1    Masure, S.2    Carton, H.3    Opdenakker, G.4
  • 25
    • 0027944171 scopus 로고
    • Reversal of experimental autoimmune encephalomyelitis with a hydroxamate inhibitor of matrix metalloproteases
    • Gijbels K, Galardy RE, Steinman L. 1994. Reversal of experimental autoimmune encephalomyelitis with a hydroxamate inhibitor of matrix metalloproteases. J Clin Invest 94:2177-2182.
    • (1994) J Clin Invest , vol.94 , pp. 2177-2182
    • Gijbels, K.1    Galardy, R.E.2    Steinman, L.3
  • 26
    • 0028934085 scopus 로고
    • Cytokines regulate gelatinase A and B (matrix metalloproteinase 2 and 9) activity in cultured rat astrocytes
    • Gottschall PE, Yu X. 1995. Cytokines regulate gelatinase A and B (matrix metalloproteinase 2 and 9) activity in cultured rat astrocytes. J Neurochem 64:1513-1520.
    • (1995) J Neurochem , vol.64 , pp. 1513-1520
    • Gottschall, P.E.1    Yu, X.2
  • 27
    • 0035122040 scopus 로고    scopus 로고
    • Programmed cell death in cerebral ischemia
    • Graham SH, Chen J. 2001. Programmed cell death in cerebral ischemia. J Cereb Blood Flow Metab 21:99-109.
    • (2001) J Cereb Blood Flow Metab , vol.21 , pp. 99-109
    • Graham, S.H.1    Chen, J.2
  • 28
    • 0032529290 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinase (TIMP)-1 induces differentiation and an antiapoptotic phenotype in germinal center B cells
    • Guedez L, Courtemanch L, Stetler-Stevenson M. 1998. Tissue inhibitor of metalloproteinase (TIMP)-1 induces differentiation and an antiapoptotic phenotype in germinal center B cells. Blood 92:1342-1349.
    • (1998) Blood , vol.92 , pp. 1342-1349
    • Guedez, L.1    Courtemanch, L.2    Stetler-Stevenson, M.3
  • 29
    • 0028792449 scopus 로고
    • Microvascular basal lamina antigens disappear during cerebral ischemia and reperfusion
    • Hamann GF, Okada Y, Fitridge R, del Zoppo GJ. 1995. Microvascular basal lamina antigens disappear during cerebral ischemia and reperfusion. Stroke 26:2120-2126.
    • (1995) Stroke , vol.26 , pp. 2120-2126
    • Hamann, G.F.1    Okada, Y.2    Fitridge, R.3    Del Zoppo, G.J.4
  • 32
    • 0022979424 scopus 로고
    • Secretion of metalloproteinases by stimulated capillary endothelial cells. II. Expression of collagenase and stromelysin activities is regulated by endogenous inhibitors
    • Herron GS, Banda MJ, Clark EJ, Gavrilovic J, Werb Z. 1986a. Secretion of metalloproteinases by stimulated capillary endothelial cells. II. Expression of collagenase and stromelysin activities is regulated by endogenous inhibitors. J Biol Chem 261:2814-2818.
    • (1986) J Biol Chem , vol.261 , pp. 2814-2818
    • Herron, G.S.1    Banda, M.J.2    Clark, E.J.3    Gavrilovic, J.4    Werb, Z.5
  • 33
    • 0023035995 scopus 로고
    • Secretion of metalloproteinases by stimulated capillary endothelial cells. I. Production of procollagenase and prostromelysin exceeds expression of proteolytic activity
    • Herron GS, Werb Z, Dwyer K, Banda MJ. 1986b. Secretion of metalloproteinases by stimulated capillary endothelial cells. I. Production of procollagenase and prostromelysin exceeds expression of proteolytic activity. J Biol Chem 261:2810-2813.
    • (1986) J Biol Chem , vol.261 , pp. 2810-2813
    • Herron, G.S.1    Werb, Z.2    Dwyer, K.3    Banda, M.J.4
  • 34
    • 0029046464 scopus 로고
    • Suppression of experimental allergic encephalomyelitis in the Lewis rat by the matrix metalloproteinase inhibitor Ro31-9790
    • Hewson AK, Smith T, Leonard JP, Cuzner ML. 1995. Suppression of experimental allergic encephalomyelitis in the Lewis rat by the matrix metalloproteinase inhibitor Ro31-9790. Inflamm Res 44:345-349.
    • (1995) Inflamm Res , vol.44 , pp. 345-349
    • Hewson, A.K.1    Smith, T.2    Leonard, J.P.3    Cuzner, M.L.4
  • 36
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr JF, Wyllie AH, Currie AR. 1972. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 26:239-257.
    • (1972) Br J Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.1    Wyllie, A.H.2    Currie, A.R.3
  • 37
    • 0028345645 scopus 로고
    • Quantitative zymography: Detection of picogram quantities of gelatinases
    • Kleiner DE, Stetler-Stevenson WG. 1994. Quantitative zymography: detection of picogram quantities of gelatinases. Anal Biochem 218:325-329.
    • (1994) Anal Biochem , vol.218 , pp. 325-329
    • Kleiner, D.E.1    Stetler-Stevenson, W.G.2
  • 38
    • 0022410974 scopus 로고
    • The biphasic opening of the blood-brain barrier to proteins following temporary middle cerebral artery occlusion
    • Kuroiwa T, Ting P, Martinez H, Klatzo I. 1985. The biphasic opening of the blood-brain barrier to proteins following temporary middle cerebral artery occlusion. Acta Neuropathol (Berl) 68:122-129.
    • (1985) Acta Neuropathol (Berl) , vol.68 , pp. 122-129
    • Kuroiwa, T.1    Ting, P.2    Martinez, H.3    Klatzo, I.4
  • 39
    • 0030442578 scopus 로고    scopus 로고
    • Basement membrane and repair of injury to peripheral nerve: Defining a potential role for macrophages, matrix metalloproteinases, and tissue inhibitor of metalloproteinases-1
    • La Fleur M, Underwood JL, Rappolee DA, Werb Z. 1996. Basement membrane and repair of injury to peripheral nerve: defining a potential role for macrophages, matrix metalloproteinases, and tissue inhibitor of metalloproteinases-1. J Exp Med 184:2311-2326.
    • (1996) J Exp Med , vol.184 , pp. 2311-2326
    • La Fleur, M.1    Underwood, J.L.2    Rappolee, D.A.3    Werb, Z.4
  • 40
    • 0033666754 scopus 로고    scopus 로고
    • Metalloproteinase inhibition reduces thrombolytic (tissue plasminogen activator)-induced hemorrhage after thromboembolic stroke
    • Lapchak PA, Chapman DF, Zivin JA. 2000. Metalloproteinase inhibition reduces thrombolytic (tissue plasminogen activator)-induced hemorrhage after thromboembolic stroke. Stroke 31:3034-3040.
    • (2000) Stroke , vol.31 , pp. 3034-3040
    • Lapchak, P.A.1    Chapman, D.F.2    Zivin, J.A.3
  • 41
    • 0026073369 scopus 로고
    • Microglial cells are a component of the perivascular glia limitans
    • Lassmann H, Zimprich F, Vass K, Hickey WF. 1991. Microglial cells are a component of the perivascular glia limitans. J Neurosci Res 28:236-243.
    • (1991) J Neurosci Res , vol.28 , pp. 236-243
    • Lassmann, H.1    Zimprich, F.2    Vass, K.3    Hickey, W.F.4
  • 42
    • 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, Hawkes SP, Edwards DR. 1994. 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 269:9352-9360.
    • (1994) J Biol Chem , vol.269 , pp. 9352-9360
    • Leco, K.J.1    Khokha, R.2    Pavloff, N.3    Hawkes, S.P.4    Edwards, D.R.5
  • 43
    • 0032948343 scopus 로고    scopus 로고
    • Serum gelatinase B, TIMP-1 and TIMP-2 levels in multiple sclerosis. A longitudinal clinical and MRI study
    • Lee MA, Palace J, Stabler G, Ford J, Gearing A, Miller K. 1999. Serum gelatinase B, TIMP-1 and TIMP-2 levels in multiple sclerosis. A longitudinal clinical and MRI study. Brain 122:191-197.
    • (1999) Brain , vol.122 , pp. 191-197
    • Lee, M.A.1    Palace, J.2    Stabler, G.3    Ford, J.4    Gearing, A.5    Miller, K.6
  • 44
    • 0033984374 scopus 로고    scopus 로고
    • Matrix metalloproteinases contribute to brain damage in experimental pneumococcal meningitis
    • Leib SL, Leppert D, Clements J, Tauber MG. 2000. Matrix metalloproteinases contribute to brain damage in experimental pneumococcal meningitis. Infect Immun 68:615-620.
    • (2000) Infect Immun , vol.68 , pp. 615-620
    • Leib, S.L.1    Leppert, D.2    Clements, J.3    Tauber, M.G.4
  • 45
    • 0034845846 scopus 로고    scopus 로고
    • Inhibition of matrix metalloproteinases and tumour necrosis factor alpha converting enzyme as adjuvant therapy in pneumococcal meningitis
    • Leib SL, Clements JM, Lindberg RL, Heimgartner C, Loeffler JM, Pfister LA, Tauber MG, Leppert D. 2001. Inhibition of matrix metalloproteinases and tumour necrosis factor alpha converting enzyme as adjuvant therapy in pneumococcal meningitis. Brain 124:1734-1742.
    • (2001) Brain , vol.124 , pp. 1734-1742
    • Leib, S.L.1    Clements, J.M.2    Lindberg, R.L.3    Heimgartner, C.4    Loeffler, J.M.5    Pfister, L.A.6    Tauber, M.G.7    Leppert, D.8
  • 46
    • 0035400082 scopus 로고    scopus 로고
    • Intact aggrecan and fragments generated by both aggrecans and metalloproteinase-like activities are present in the developing and adult rat spinal cord and their relative abundance is altered by injury
    • Lemons ML, Sandy JD, Anderson DK, Howland DR. 2001. Intact aggrecan and fragments generated by both aggrecans and metalloproteinase-like activities are present in the developing and adult rat spinal cord and their relative abundance is altered by injury. J Neurosci 21:4772-4781.
    • (2001) J Neurosci , vol.21 , pp. 4772-4781
    • Lemons, M.L.1    Sandy, J.D.2    Anderson, D.K.3    Howland, D.R.4
  • 47
    • 0029041446 scopus 로고
    • T cell gelatinases mediate basement membrane transmigration in vitro
    • Leppert D, Waubant E, Galardy R, Bunnett NW, Hauser SL. 1995. T cell gelatinases mediate basement membrane transmigration in vitro. J Immunol 154:4379-4389.
    • (1995) J Immunol , vol.154 , pp. 4379-4389
    • Leppert, D.1    Waubant, E.2    Galardy, R.3    Bunnett, N.W.4    Hauser, S.L.5
  • 48
    • 0033551469 scopus 로고    scopus 로고
    • Matrix metalloproteinase upregulation in chronic inflammatory demyelinating polyneuropathy and nonsystemic vasculitic neuropathy
    • Leppert D, Hughes P, Huber S, Erne B, Grygar C, Said G, Miller KM, Steck AJ, Probst A, Fuhr P. 1999. Matrix metalloproteinase upregulation in chronic inflammatory demyelinating polyneuropathy and nonsystemic vasculitic neuropathy Neurology 53:62-70.
    • (1999) Neurology , vol.53 , pp. 62-70
    • Leppert, D.1    Hughes, P.2    Huber, S.3    Erne, B.4    Grygar, C.5    Said, G.6    Miller, K.M.7    Steck, A.J.8    Probst, A.9    Fuhr, P.10
  • 50
    • 0019195010 scopus 로고
    • Metastatic potential correlates with enzymatic degradation of basement membrane collagen
    • Liotta LA, Tryggvason K, Garbisa S, Hart I, Foltz CM, Shafie S. 1980. Metastatic potential correlates with enzymatic degradation of basement membrane collagen. Nature 284:67-68.
    • (1980) Nature , vol.284 , pp. 67-68
    • Liotta, L.A.1    Tryggvason, K.2    Garbisa, S.3    Hart, I.4    Foltz, C.M.5    Shafie, S.6
  • 51
    • 0033539947 scopus 로고    scopus 로고
    • Inhibition of the putative tumor suppressor gene TIMP-3 by tumor-derived p53 mutants and wild type p53
    • Loging WT, Reisman D. 1999. Inhibition of the putative tumor suppressor gene TIMP-3 by tumor-derived p53 mutants and wild type p53. Oncogene 18:7608-7615.
    • (1999) Oncogene , vol.18 , pp. 7608-7615
    • Loging, W.T.1    Reisman, D.2
  • 52
    • 0032821995 scopus 로고    scopus 로고
    • Extracellular matrix degradation by metalloproteinases and central nervous system diseases
    • Lukes A, Mun-Bryce S, Lukes M, Rosenberg GA. 1999. Extracellular matrix degradation by metalloproteinases and central nervous system diseases. Mol Neurobiol 19:267-284.
    • (1999) Mol Neurobiol , vol.19 , pp. 267-284
    • Lukes, A.1    Mun-Bryce, S.2    Lukes, M.3    Rosenberg, G.A.4
  • 53
    • 0029867128 scopus 로고    scopus 로고
    • Matrix metalloproteinases in the normal human central nervous system, microglial nodules, and multiple sclerosis lesions
    • Maeda A, Sobel RA. 1996. Matrix metalloproteinases in the normal human central nervous system, microglial nodules, and multiple sclerosis lesions. J Neuropathol Exp Neurol 55:300-309.
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 300-309
    • Maeda, A.1    Sobel, R.A.2
  • 54
    • 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, Mignatti P. 1997. Control of type IV collagenase activity by components of the urokinase-plasmin system: a regulatory mechanism with cell-bound reactants. EMBO J 16:2319-2332.
    • (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
  • 56
    • 0029943568 scopus 로고    scopus 로고
    • Plasminogen activators and matrix metalloproteinases in angiogenesis
    • Mignatti P, Rifkin DB. 1996. Plasminogen activators and matrix metalloproteinases in angiogenesis. Enzyme Protein 49:117-137.
    • (1996) Enzyme Protein , vol.49 , pp. 117-137
    • Mignatti, P.1    Rifkin, D.B.2
  • 57
    • 0034893137 scopus 로고    scopus 로고
    • Matrix metalloproteinase expression after human cardioembolic stroke: Temporal profile and relation to neurological impairment
    • Montaner J, Alvarez-Sabin J, Molina C, Angles A, Abilleira S, Arenillas J, Gonzalez MA, Monasterio J. 2001a. Matrix metalloproteinase expression after human cardioembolic stroke: temporal profile and relation to neurological impairment. Stroke 32:1759-1766.
    • (2001) Stroke , vol.32 , pp. 1759-1766
    • Montaner, J.1    Alvarez-Sabin, J.2    Molina, C.3    Angles, A.4    Abilleira, S.5    Arenillas, J.6    Gonzalez, M.A.7    Monasterio, J.8
  • 59
    • 0031831764 scopus 로고    scopus 로고
    • Gelatinase B modulates selective opening of the blood-brain barrier during inflammation
    • Mun-Bryce S, Rosenberg GA. 1998a. Gelatinase B modulates selective opening of the blood-brain barrier during inflammation. Am J Physiol 274:R1203-11.
    • (1998) Am J Physiol , vol.274
    • Mun-Bryce, S.1    Rosenberg, G.A.2
  • 60
    • 0031768024 scopus 로고    scopus 로고
    • Matrix metalloproteinases in cerebrovascular disease
    • Mun-Bryce S, Rosenberg GA. 1998b. Matrix metalloproteinases in cerebrovascular disease. J Cereb Blood Flow Metab 18:1163-1172.
    • (1998) J Cereb Blood Flow Metab , vol.18 , pp. 1163-1172
    • Mun-Bryce, S.1    Rosenberg, G.A.2
  • 61
    • 0037066416 scopus 로고    scopus 로고
    • Stromelysin-1 and gelatinase A are upregulated before TNF-alpha in LPS-stimulated neuroinflammation
    • Mun-Bryce S, Lukes A, Wallace J, Lukes-Marx M, Rosenberg GA. 2002. Stromelysin-1 and gelatinase A are upregulated before TNF-alpha in LPS-stimulated neuroinflammation. Brain Res 933:42-49.
    • (2002) Brain Res , vol.933 , pp. 42-49
    • Mun-Bryce, S.1    Lukes, A.2    Wallace, J.3    Lukes-Marx, M.4    Rosenberg, G.A.5
  • 62
    • 0030957218 scopus 로고    scopus 로고
    • Activation mechanisms of matrix metalloproteinases
    • Nagase H. 1997. Activation mechanisms of matrix metalloproteinases. Biol Chem 378:151-160.
    • (1997) Biol Chem , vol.378 , pp. 151-160
    • Nagase, H.1
  • 63
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase H, Woessner JF Jr. 1999. Matrix metalloproteinases. J Biol Chem 274:21491-21494.
    • (1999) J Biol Chem , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner J.F., Jr.2
  • 64
    • 0033999308 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Biologic activity and clinical implications
    • Nelson AR, Fingleton B, Rothenberg ML, Matrisian LM. 2000. Matrix metalloproteinases: biologic activity and clinical implications. J Clin Oncol 18:1135-1149.
    • (2000) J Clin Oncol , vol.18 , pp. 1135-1149
    • Nelson, A.R.1    Fingleton, B.2    Rothenberg, M.L.3    Matrisian, L.M.4
  • 65
  • 66
    • 0026794057 scopus 로고
    • A new inhibitor of metalloproteinases from chicken: ChIMP-3. A third member of the TIMP family
    • Pavloff N, Staskus PW, Kishnani NS, Hawkes SP. 1992. A new inhibitor of metalloproteinases from chicken: ChIMP-3. A third member of the TIMP family. J Biol Chem 267:17321-17326.
    • (1992) J Biol Chem , vol.267 , pp. 17321-17326
    • Pavloff, N.1    Staskus, P.W.2    Kishnani, N.S.3    Hawkes, S.P.4
  • 68
    • 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 DL, Quigley, JP. 1999. Activation of matrix metalloproteinase-9 (MMP-9) via a converging plasmin/stromelysin-1 cascade enhances tumor cell invasion. J Biol Chem 274:13066-13076.
    • (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
  • 69
    • 0030860443 scopus 로고    scopus 로고
    • A combined inhibitor of matrix metalloproteinase activity and tumour necrosis factor-alpha processing attenuates experimental autoimmune neuritis
    • Redford EJ, Smith KJ, Gregson NA, Davies M, Hughes P, Gearing AJ, Miller K, Hughes RA. 1997. A combined inhibitor of matrix metalloproteinase activity and tumour necrosis factor-alpha processing attenuates experimental autoimmune neuritis. Brain 120:1895-1905.
    • (1997) Brain , vol.120 , pp. 1895-1905
    • Redford, E.J.1    Smith, K.J.2    Gregson, N.A.3    Davies, M.4    Hughes, P.5    Gearing, A.J.6    Miller, K.7    Hughes, R.A.8
  • 70
    • 0028255910 scopus 로고
    • Extracellular matrix-degrading proteinases in the nervous system
    • Romanic AM, Madri JA. 1994. Extracellular matrix-degrading proteinases in the nervous system. Brain Pathol 4:145-156.
    • (1994) Brain Pathol , vol.4 , pp. 145-156
    • Romanic, A.M.1    Madri, J.A.2
  • 71
    • 0031959973 scopus 로고    scopus 로고
    • Matrix metalloproteinase expression increases after cerebral focal ischemia in rats: Inhibition of matrix metalloproteinase-9 reduces infarct size
    • Romanic AM, White RF, Arleth AJ, Ohlstein EH, Barone FC. 1998. Matrix metalloproteinase expression increases after cerebral focal ischemia in rats: inhibition of matrix metalloproteinase-9 reduces infarct size. Stroke 29:1020-1030.
    • (1998) Stroke , vol.29 , pp. 1020-1030
    • Romanic, A.M.1    White, R.F.2    Arleth, A.J.3    Ohlstein, E.H.4    Barone, F.C.5
  • 72
    • 0028825270 scopus 로고
    • Matrix metalloproteinases in brain injury
    • Rosenberg GA. 1995. Matrix metalloproteinases in brain injury. J Neurotrauma 12:833-842.
    • (1995) J Neurotrauma , vol.12 , pp. 833-842
    • Rosenberg, G.A.1
  • 73
    • 0034785552 scopus 로고    scopus 로고
    • Matrix metalloproteinases in multiple sclerosis: Is it time for a treatment trial?
    • Rosenberg GA. 2001. Matrix metalloproteinases in multiple sclerosis: Is it time for a treatment trial? Ann Neurol 50:431-433.
    • (2001) Ann Neurol , vol.50 , pp. 431-433
    • Rosenberg, G.A.1
  • 74
    • 0030899195 scopus 로고    scopus 로고
    • Metalloproteinase inhibition blocks edema in intracerebral hemorrhage in the rat
    • Rosenberg GA, Navratil M. 1997. Metalloproteinase inhibition blocks edema in intracerebral hemorrhage in the rat. Neurology 48:921-926.
    • (1997) Neurology , vol.48 , pp. 921-926
    • Rosenberg, G.A.1    Navratil, M.2
  • 76
    • 0028973084 scopus 로고
    • Tumor necrosis factor-alpha-induced gelatinase B causes delayed opening of the blood-brain barrier: An expanded therapeutic window
    • Rosenberg GA, Estrada EY, Dencoff JE, Stetler-Stevenson WG. 1995. Tumor necrosis factor-alpha-induced gelatinase B causes delayed opening of the blood-brain barrier: an expanded therapeutic window. Brain Res 703:151-155.
    • (1995) Brain Res , vol.703 , pp. 151-155
    • Rosenberg, G.A.1    Estrada, E.Y.2    Dencoff, J.E.3    Stetler-Stevenson, W.G.4
  • 77
    • 0029889674 scopus 로고    scopus 로고
    • Effect of steroids on CSF matrix metalloproteinases in multiple sclerosis: Relation to blood-brain barrier injury
    • Rosenberg GA, Dencoff JE, Correa N Jr, Reiners M, Ford CC. 1996a. Effect of steroids on CSF matrix metalloproteinases in multiple sclerosis: relation to blood-brain barrier injury. Neurology 46:1626-1632.
    • (1996) Neurology , vol.46 , pp. 1626-1632
    • Rosenberg, G.A.1    Dencoff, J.E.2    Correa N., Jr.3    Reiners, M.4    Ford, C.C.5
  • 79
    • 0031693557 scopus 로고    scopus 로고
    • Matrix metalloproteinases and TIMPs are associated with blood-brain barrier opening after reperfusion in rat brain
    • Rosenberg GA, Estrada EY, Dencoff JE. 1998. Matrix metalloproteinases and TIMPs are associated with blood-brain barrier opening after reperfusion in rat brain. Stroke 29:2189-2195.
    • (1998) Stroke , vol.29 , pp. 2189-2195
    • Rosenberg, G.A.1    Estrada, E.Y.2    Dencoff, J.E.3
  • 80
    • 0035793934 scopus 로고    scopus 로고
    • Immunohistochemistry of matrix metalloproteinases in reperfusion injury to rat brain: Activation of MMP-9 linked to stromelysin-1 and microglia in cell cultures
    • Rosenberg GA, Cunningham LA, Wallace J, Alexander S, Estrada EY, Grossetete M, Razhagi A, Miller K, Gearing A. 2001a. Immunohistochemistry of matrix metalloproteinases in reperfusion injury to rat brain: activation of MMP-9 linked to stromelysin-1 and microglia in cell cultures. Brain Res 893:104-112.
    • (2001) Brain Res , vol.893 , pp. 104-112
    • Rosenberg, G.A.1    Cunningham, L.A.2    Wallace, J.3    Alexander, S.4    Estrada, E.Y.5    Grossetete, M.6    Razhagi, A.7    Miller, K.8    Gearing, A.9
  • 81
    • 0034846419 scopus 로고    scopus 로고
    • White matter damage is associated with matrix metalloproteinases in vascular dementia
    • Rosenberg GA, Sullivan N, Esiri MM. 2001b. White matter damage is associated with matrix metalloproteinases in vascular dementia. Stroke 32:1162-1168.
    • (2001) Stroke , vol.32 , pp. 1162-1168
    • Rosenberg, G.A.1    Sullivan, N.2    Esiri, M.M.3
  • 82
    • 0030785485 scopus 로고    scopus 로고
    • Coordinate expression of matrix metalloproteinase family members in the uterus of normal, matrilysin-deficient, and stromelysin-1-deficient mice
    • Rudolph-Owen LA, Hulboy DL, Wilson CL, Mudgett J, Matrisian LM. 1997. Coordinate expression of matrix metalloproteinase family members in the uterus of normal, matrilysin-deficient, and stromelysin-1-deficient mice. Endocrinology 138:4902-4911.
    • (1997) Endocrinology , vol.138 , pp. 4902-4911
    • Rudolph-Owen, L.A.1    Hulboy, D.L.2    Wilson, C.L.3    Mudgett, J.4    Matrisian, L.M.5
  • 83
  • 84
    • 0032741143 scopus 로고    scopus 로고
    • Metalloprotease-disintegrins: Modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding
    • Schlondorff J, Blobel CP. 1999. Metalloprotease-disintegrins: modular proteins capable of promoting cell-cell interactions and triggering signals by protein-ectodomain shedding. J Cell Sci 112:3603-3617.
    • (1999) J Cell Sci , vol.112 , pp. 3603-3617
    • Schlondorff, J.1    Blobel, C.P.2
  • 85
    • 0031259566 scopus 로고    scopus 로고
    • TIMP-3 induces cell death by stabilizing TNF-alpha receptors on the surface of human colon carcinoma cells
    • Smith MR, Kung H, Durum SK, Colburn NH, Sun Y. 1997. TIMP-3 induces cell death by stabilizing TNF-alpha receptors on the surface of human colon carcinoma cells. Cytokine 9:770-780.
    • (1997) Cytokine , vol.9 , pp. 770-780
    • Smith, M.R.1    Kung, H.2    Durum, S.K.3    Colburn, N.H.4    Sun, Y.5
  • 86
    • 0028907318 scopus 로고
    • Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease
    • Strongin AY, Collier I, Bannikov G, Marmer BL, Grant GA, Goldberg GI. 1995. Mechanism of cell surface activation of 72-kDa type IV collagenase. Isolation of the activated form of the membrane metalloprotease. J Biol Chem 270:5331-5338.
    • (1995) J Biol Chem , vol.270 , pp. 5331-5338
    • Strongin, A.Y.1    Collier, I.2    Bannikov, G.3    Marmer, B.L.4    Grant, G.A.5    Goldberg, G.I.6
  • 88
    • 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 HE, 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 U S A 87:5578-5582.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5578-5582
    • Van Wart, H.E.1    Birkedal Hansen, H.2
  • 89
    • 0034046651 scopus 로고    scopus 로고
    • Cytotoxicity by matrix metalloprotease-1 in organotypic spinal cord and dissociated neuronal cultures
    • Vos CM, Sjulson L, Nath A, McArthur JC, Pardo CA, Rothstein J, Conant K. 2000. Cytotoxicity by matrix metalloprotease-1 in organotypic spinal cord and dissociated neuronal cultures. Exp Neurol 163:324-330.
    • (2000) Exp Neurol , vol.163 , pp. 324-330
    • Vos, C.M.1    Sjulson, L.2    Nath, A.3    McArthur, J.C.4    Pardo, C.A.5    Rothstein, J.6    Conant, K.7
  • 90
    • 0031886454 scopus 로고    scopus 로고
    • Subtractive cloning identifies tissue inhibitor of matrix metalloproteinase-1 (TIMP-1) increased gene expression following focal stroke
    • Wang X, Barone FC, White RF, Feuersteln GZ. 1998. Subtractive cloning identifies tissue inhibitor of matrix metalloproteinase-1 (TIMP-1) increased gene expression following focal stroke. Stroke 29:516-520.
    • (1998) Stroke , vol.29 , pp. 516-520
    • Wang, X.1    Barone, F.C.2    White, R.F.3    Feuersteln, G.Z.4
  • 92
    • 0030472401 scopus 로고    scopus 로고
    • Quantitation of matrix metalloproteinases in cultured rat astrocytes using the polymerase chain reaction with a multi-competitor cDNA standard
    • Wells GM, Catlin G, Cossins JA, Mangan M, Ward GA, Miller KM, Clements JM. 1996. Quantitation of matrix metalloproteinases in cultured rat astrocytes using the polymerase chain reaction with a multi-competitor cDNA standard. Glia 18:332-340.
    • (1996) Glia , vol.18 , pp. 332-340
    • Wells, G.M.1    Catlin, G.2    Cossins, J.A.3    Mangan, M.4    Ward, G.A.5    Miller, K.M.6    Clements, J.M.7
  • 94
    • 0035405886 scopus 로고    scopus 로고
    • Metalloproteinases in biology and pathology of the nervous system
    • Yong VW, Power C, Forsyth P, Edwards DR. 2001. Metalloproteinases in biology and pathology of the nervous system. Nat Rev Neurosci 2:502-511.
    • (2001) Nat Rev Neurosci , vol.2 , pp. 502-511
    • Yong, V.W.1    Power, C.2    Forsyth, P.3    Edwards, D.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.