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Volumn 6, Issue 3, 2011, Pages

A high throughput screen identifies chemical modulators of the laminin-induced clustering of dystroglycan and aquaporin-4 in primary astrocytes

Author keywords

[No Author keywords available]

Indexed keywords

ACETYLCYSTEINE; AQUAPORIN 4; BETA DYSTROGLYCAN; CHLORANIL; FLUNARIZINE; GELATINASE A; LAMININ; REACTIVE OXYGEN METABOLITE; DYSTROGLYCAN; GELATIN; ORGANIC COMPOUND; PRINOMASTAT; TISSUE INHIBITOR OF METALLOPROTEINASE;

EID: 79952355111     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0017559     Document Type: Article
Times cited : (12)

References (65)
  • 1
    • 9344226163 scopus 로고    scopus 로고
    • New insights into water transport and edema in the central nervous system from phenotype analysis of aquaporin-4 null mice
    • Manley GT, Binder DK, Papadopoulos MC, Verkman AS, (2004) New insights into water transport and edema in the central nervous system from phenotype analysis of aquaporin-4 null mice. Neuroscience 129: 983-991.
    • (2004) Neuroscience , vol.129 , pp. 983-991
    • Manley, G.T.1    Binder, D.K.2    Papadopoulos, M.C.3    Verkman, A.S.4
  • 2
    • 0031022918 scopus 로고    scopus 로고
    • Specialized membrane domains for water transport in glial cells: high-resolution immunogold cytochemistry of aquaporin-4 in rat brain
    • Nielsen S, Nagelhus EA, Amiry-Moghaddam M, Bourque C, Agre P, et al. (1997) Specialized membrane domains for water transport in glial cells: high-resolution immunogold cytochemistry of aquaporin-4 in rat brain. J Neurosci 17: 171-180.
    • (1997) J Neurosci , vol.17 , pp. 171-180
    • Nielsen, S.1    Nagelhus, E.A.2    Amiry-Moghaddam, M.3    Bourque, C.4    Agre, P.5
  • 3
    • 33845974872 scopus 로고    scopus 로고
    • Greatly impaired migration of implanted aquaporin-4-deficient astroglial cells in mouse brain toward a site of injury
    • Auguste KI, Jin S, Uchida K, Yan D, Manley GT, et al. (2007) Greatly impaired migration of implanted aquaporin-4-deficient astroglial cells in mouse brain toward a site of injury. FASEB J 21: 108-116.
    • (2007) FASEB J , vol.21 , pp. 108-116
    • Auguste, K.I.1    Jin, S.2    Uchida, K.3    Yan, D.4    Manley, G.T.5
  • 4
    • 0033966090 scopus 로고    scopus 로고
    • Aquaporin-4 deletion in mice reduces brain edema after acute water intoxication and ischemic stroke
    • Manley GT, Fujimura M, Ma T, Noshita N, Filiz F, et al. (2000) Aquaporin-4 deletion in mice reduces brain edema after acute water intoxication and ischemic stroke. Nat Med 6: 159-163.
    • (2000) Nat Med , vol.6 , pp. 159-163
    • Manley, G.T.1    Fujimura, M.2    Ma, T.3    Noshita, N.4    Filiz, F.5
  • 6
    • 0030955183 scopus 로고    scopus 로고
    • Generation and phenotype of a transgenic knockout mouse lacking the mercurial-insensitive water channel aquaporin-4
    • Ma T, Yang B, Gillespie A, Carlson EJ, Epstein CJ, et al. (1997) Generation and phenotype of a transgenic knockout mouse lacking the mercurial-insensitive water channel aquaporin-4. J Clin Invest 100: 957-962.
    • (1997) J Clin Invest , vol.100 , pp. 957-962
    • Ma, T.1    Yang, B.2    Gillespie, A.3    Carlson, E.J.4    Epstein, C.J.5
  • 7
    • 47249135565 scopus 로고    scopus 로고
    • Glial cell aquaporin-4 overexpression in transgenic mice accelerates cytotoxic brain swelling
    • Yang B, Zador Z, Verkman AS, (2008) Glial cell aquaporin-4 overexpression in transgenic mice accelerates cytotoxic brain swelling. J Biol Chem 283: 15280-15286.
    • (2008) J Biol Chem , vol.283 , pp. 15280-15286
    • Yang, B.1    Zador, Z.2    Verkman, A.S.3
  • 8
    • 33745066806 scopus 로고    scopus 로고
    • Accelerated progression of kaolin-induced hydrocephalus in aquaporin-4-deficient mice
    • Bloch O, Auguste KI, Manley GT, Verkman AS, (2006) Accelerated progression of kaolin-induced hydrocephalus in aquaporin-4-deficient mice. J Cereb Blood Flow Metab 26: 1527-1537.
    • (2006) J Cereb Blood Flow Metab , vol.26 , pp. 1527-1537
    • Bloch, O.1    Auguste, K.I.2    Manley, G.T.3    Verkman, A.S.4
  • 9
    • 24344500555 scopus 로고    scopus 로고
    • Aquaporin-4 gene deletion in mice increases focal edema associated with staphylococcal brain abscess
    • Bloch O, Papadopoulos MC, Manley GT, Verkman AS, (2005) Aquaporin-4 gene deletion in mice increases focal edema associated with staphylococcal brain abscess. J Neurochem 95: 254-262.
    • (2005) J Neurochem , vol.95 , pp. 254-262
    • Bloch, O.1    Papadopoulos, M.C.2    Manley, G.T.3    Verkman, A.S.4
  • 10
    • 77950370875 scopus 로고    scopus 로고
    • Increased brain edema in aqp4-null mice in an experimental model of subarachnoid hemorrhage
    • Tait MJ, Saadoun S, Bell BA, Verkman AS, Papadopoulos MC, (2010) Increased brain edema in aqp4-null mice in an experimental model of subarachnoid hemorrhage. Neuroscience 167: 60-67.
    • (2010) Neuroscience , vol.167 , pp. 60-67
    • Tait, M.J.1    Saadoun, S.2    Bell, B.A.3    Verkman, A.S.4    Papadopoulos, M.C.5
  • 11
    • 33744923211 scopus 로고    scopus 로고
    • Quaternary ammonium compounds as water channel blockers. Specificity, potency, and site of action
    • Detmers FJ, de Groot BL, Muller EM, Hinton A, Konings IB, et al. (2006) Quaternary ammonium compounds as water channel blockers. Specificity, potency, and site of action. J Biol Chem 281: 14207-14214.
    • (2006) J Biol Chem , vol.281 , pp. 14207-14214
    • Detmers, F.J.1    de Groot, B.L.2    Muller, E.M.3    Hinton, A.4    Konings, I.B.5
  • 13
    • 57649184995 scopus 로고    scopus 로고
    • Support for small molecule inhibition of aquaporin 4
    • Huber VJ, (2009) Support for small molecule inhibition of aquaporin 4. Bioorg Med Chem 17: 425-426.
    • (2009) Bioorg Med Chem , vol.17 , pp. 425-426
    • Huber, V.J.1
  • 15
    • 70349619660 scopus 로고    scopus 로고
    • Automated cell-based assay for screening of aquaporin inhibitors
    • Mola MG, Nicchia GP, Svelto M, Spray DC, Frigeri A, (2009) Automated cell-based assay for screening of aquaporin inhibitors. Anal Chem 81: 8219-8229.
    • (2009) Anal Chem , vol.81 , pp. 8219-8229
    • Mola, M.G.1    Nicchia, G.P.2    Svelto, M.3    Spray, D.C.4    Frigeri, A.5
  • 16
    • 60649086355 scopus 로고    scopus 로고
    • Acetazolamide reversibly inhibits water conduction by aquaporin-4
    • Tanimura Y, Hiroaki Y, Fujiyoshi Y, (2009) Acetazolamide reversibly inhibits water conduction by aquaporin-4. J Struct Biol 166: 16-21.
    • (2009) J Struct Biol , vol.166 , pp. 16-21
    • Tanimura, Y.1    Hiroaki, Y.2    Fujiyoshi, Y.3
  • 17
    • 53749084968 scopus 로고    scopus 로고
    • Changes in ocular aquaporin-4 (AQP4) expression following retinal injury
    • Dibas A, Yang MH, He S, Bobich J, Yorio T, (2008) Changes in ocular aquaporin-4 (AQP4) expression following retinal injury. Mol Vis 14: 1770-1783.
    • (2008) Mol Vis , vol.14 , pp. 1770-1783
    • Dibas, A.1    Yang, M.H.2    He, S.3    Bobich, J.4    Yorio, T.5
  • 18
    • 48449085609 scopus 로고    scopus 로고
    • Lack of aquaporin-4 water transport inhibition by antiepileptics and arylsulfonamides
    • Yang B, Zhang H, Verkman AS, (2008) Lack of aquaporin-4 water transport inhibition by antiepileptics and arylsulfonamides. Bioorg Med Chem 16: 7489-7493.
    • (2008) Bioorg Med Chem , vol.16 , pp. 7489-7493
    • Yang, B.1    Zhang, H.2    Verkman, A.S.3
  • 19
    • 0034068415 scopus 로고    scopus 로고
    • Brain dystrophin, neurogenetics and mental retardation
    • Mehler MF, (2000) Brain dystrophin, neurogenetics and mental retardation. Brain Res Brain Res Rev 32: 277-307.
    • (2000) Brain Res Brain Res Rev , vol.32 , pp. 277-307
    • Mehler, M.F.1
  • 20
    • 0028877455 scopus 로고
    • Muscular dystrophies: diseases of the dystrophin-glycoprotein complex
    • Worton R, (1995) Muscular dystrophies: diseases of the dystrophin-glycoprotein complex. Science 270: 755-756.
    • (1995) Science , vol.270 , pp. 755-756
    • Worton, R.1
  • 21
    • 0027321171 scopus 로고
    • Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin
    • Gee SH, Blacher RW, Douville PJ, Provost PR, Yurchenco PD, et al. (1993) Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin. J Biol Chem 268: 14972-14980.
    • (1993) J Biol Chem , vol.268 , pp. 14972-14980
    • Gee, S.H.1    Blacher, R.W.2    Douville, P.J.3    Provost, P.R.4    Yurchenco, P.D.5
  • 22
    • 0028178082 scopus 로고
    • Dystroglycan-alpha, a dystrophin-associated glycoprotein, is a functional agrin receptor
    • Gee SH, Montanaro F, Lindenbaum MH, Carbonetto S, (1994) Dystroglycan-alpha, a dystrophin-associated glycoprotein, is a functional agrin receptor. Cell 77: 675-686.
    • (1994) Cell , vol.77 , pp. 675-686
    • Gee, S.H.1    Montanaro, F.2    Lindenbaum, M.H.3    Carbonetto, S.4
  • 23
    • 0031770342 scopus 로고    scopus 로고
    • The relationship between perlecan and dystroglycan and its implication in the formation of the neuromuscular junction
    • Peng HB, Ali AA, Daggett DF, Rauvala H, Hassell JR, et al. (1998) The relationship between perlecan and dystroglycan and its implication in the formation of the neuromuscular junction. Cell Adhes Commun 5: 475-489.
    • (1998) Cell Adhes Commun , vol.5 , pp. 475-489
    • Peng, H.B.1    Ali, A.A.2    Daggett, D.F.3    Rauvala, H.4    Hassell, J.R.5
  • 24
    • 0035939672 scopus 로고    scopus 로고
    • A stoichiometric complex of neurexins and dystroglycan in brain
    • Sugita S, Saito F, Tang J, Satz J, Campbell K, et al. (2001) A stoichiometric complex of neurexins and dystroglycan in brain. J Cell Biol 154: 435-445.
    • (2001) J Cell Biol , vol.154 , pp. 435-445
    • Sugita, S.1    Saito, F.2    Tang, J.3    Satz, J.4    Campbell, K.5
  • 25
    • 36249022059 scopus 로고    scopus 로고
    • Distribution of potassium ion and water permeable channels at perivascular glia in brain and retina of the Large(myd) mouse
    • Rurak J, Noel G, Lui L, Joshi B, Moukhles H, (2007) Distribution of potassium ion and water permeable channels at perivascular glia in brain and retina of the Large(myd) mouse. J Neurochem 103: 1940-1953.
    • (2007) J Neurochem , vol.103 , pp. 1940-1953
    • Rurak, J.1    Noel, G.2    Lui, L.3    Joshi, B.4    Moukhles, H.5
  • 26
    • 33646530740 scopus 로고    scopus 로고
    • Assembly of a perivascular astrocyte protein scaffold at the mammalian blood-brain barrier is dependent on alpha-syntrophin
    • Bragg AD, Amiry-Moghaddam M, Ottersen OP, Adams ME, Froehner SC, (2006) Assembly of a perivascular astrocyte protein scaffold at the mammalian blood-brain barrier is dependent on alpha-syntrophin. Glia 53: 879-890.
    • (2006) Glia , vol.53 , pp. 879-890
    • Bragg, A.D.1    Amiry-Moghaddam, M.2    Ottersen, O.P.3    Adams, M.E.4    Froehner, S.C.5
  • 27
    • 3943068322 scopus 로고    scopus 로고
    • Laminin-induced aggregation of the inwardly rectifying potassium channel, Kir4.1, and the water-permeable channel, AQP4, via a dystroglycan-containing complex in astrocytes
    • Guadagno E, Moukhles H, (2004) Laminin-induced aggregation of the inwardly rectifying potassium channel, Kir4.1, and the water-permeable channel, AQP4, via a dystroglycan-containing complex in astrocytes. Glia 47: 138-149.
    • (2004) Glia , vol.47 , pp. 138-149
    • Guadagno, E.1    Moukhles, H.2
  • 28
    • 67749142283 scopus 로고    scopus 로고
    • Interdependence of laminin-mediated clustering of lipid rafts and the dystrophin complex in astrocytes
    • Noel G, Tham DK, Moukhles H, (2009) Interdependence of laminin-mediated clustering of lipid rafts and the dystrophin complex in astrocytes. J Biol Chem 284: 19694-19704.
    • (2009) J Biol Chem , vol.284 , pp. 19694-19704
    • Noel, G.1    Tham, D.K.2    Moukhles, H.3
  • 29
    • 0037452611 scopus 로고    scopus 로고
    • An alpha-syntrophin-dependent pool of AQP4 in astroglial end-feet confers bidirectional water flow between blood and brain
    • Amiry-Moghaddam M, Otsuka T, Hurn PD, Traystman RJ, Haug FM, et al. (2003) An alpha-syntrophin-dependent pool of AQP4 in astroglial end-feet confers bidirectional water flow between blood and brain. Proc Natl Acad Sci U S A 100: 2106-2111.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 2106-2111
    • Amiry-Moghaddam, M.1    Otsuka, T.2    Hurn, P.D.3    Traystman, R.J.4    Haug, F.M.5
  • 31
    • 0038407772 scopus 로고    scopus 로고
    • Severe alterations of endothelial and glial cells in the blood-brain barrier of dystrophic mdx mice
    • Nico B, Frigeri A, Nicchia GP, Corsi P, Ribatti D, et al. (2003) Severe alterations of endothelial and glial cells in the blood-brain barrier of dystrophic mdx mice. Glia 42: 235-251.
    • (2003) Glia , vol.42 , pp. 235-251
    • Nico, B.1    Frigeri, A.2    Nicchia, G.P.3    Corsi, P.4    Ribatti, D.5
  • 32
    • 9344259114 scopus 로고    scopus 로고
    • Anchoring of aquaporin-4 in brain: molecular mechanisms and implications for the physiology and pathophysiology of water transport
    • Amiry-Moghaddam M, Frydenlund DS, Ottersen OP, (2004) Anchoring of aquaporin-4 in brain: molecular mechanisms and implications for the physiology and pathophysiology of water transport. Neuroscience 129: 999-1010.
    • (2004) Neuroscience , vol.129 , pp. 999-1010
    • Amiry-Moghaddam, M.1    Frydenlund, D.S.2    Ottersen, O.P.3
  • 33
  • 34
    • 34447538141 scopus 로고    scopus 로고
    • High-throughput screening assays for the identification of chemical probes
    • Inglese J, Johnson RL, Simeonov A, Xia M, Zheng W, et al. (2007) High-throughput screening assays for the identification of chemical probes. Nat Chem Biol 3: 466-479.
    • (2007) Nat Chem Biol , vol.3 , pp. 466-479
    • Inglese, J.1    Johnson, R.L.2    Simeonov, A.3    Xia, M.4    Zheng, W.5
  • 35
    • 0035878554 scopus 로고    scopus 로고
    • Processing of beta-dystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycan complex
    • Yamada H, Saito F, Fukuta-Ohi H, Zhong D, Hase A, et al. (2001) Processing of beta-dystroglycan by matrix metalloproteinase disrupts the link between the extracellular matrix and cell membrane via the dystroglycan complex. Hum Mol Genet 10: 1563-1569.
    • (2001) Hum Mol Genet , vol.10 , pp. 1563-1569
    • Yamada, H.1    Saito, F.2    Fukuta-Ohi, H.3    Zhong, D.4    Hase, A.5
  • 36
    • 33645869560 scopus 로고    scopus 로고
    • Dystroglycan is selectively cleaved at the parenchymal basement membrane at sites of leukocyte extravasation in experimental autoimmune encephalomyelitis
    • Agrawal S, Anderson P, Durbeej M, van Rooijen N, Ivars F, et al. (2006) Dystroglycan is selectively cleaved at the parenchymal basement membrane at sites of leukocyte extravasation in experimental autoimmune encephalomyelitis. J Exp Med 203: 1007-1019.
    • (2006) J Exp Med , vol.203 , pp. 1007-1019
    • Agrawal, S.1    Anderson, P.2    Durbeej, M.3    van Rooijen, N.4    Ivars, F.5
  • 37
    • 31044440813 scopus 로고    scopus 로고
    • TIMP3 mutation in Sorsby's fundus dystrophy: molecular insights
    • Li Z, Clarke MP, Barker MD, McKie N, (2005) TIMP3 mutation in Sorsby's fundus dystrophy: molecular insights. Expert Rev Mol Med 7: 1-15.
    • (2005) Expert Rev Mol Med , vol.7 , pp. 1-15
    • Li, Z.1    Clarke, M.P.2    Barker, M.D.3    McKie, N.4
  • 38
    • 4444336981 scopus 로고    scopus 로고
    • Application of quantitative structure-toxicity relationships for the comparison of the cytotoxicity of 14 p-benzoquinone congeners in primary cultured rat hepatocytes versus PC12 cells
    • Siraki AG, Chan TS, O'Brien PJ, (2004) Application of quantitative structure-toxicity relationships for the comparison of the cytotoxicity of 14 p-benzoquinone congeners in primary cultured rat hepatocytes versus PC12 cells. Toxicol Sci 81: 148-159.
    • (2004) Toxicol Sci , vol.81 , pp. 148-159
    • Siraki, A.G.1    Chan, T.S.2    O'Brien, P.J.3
  • 39
    • 0023927330 scopus 로고
    • Near stoichiometric, irreversible inactivation of bacterial collagenases by o-chloranil (3,4,5,6-tetrachloro-1,2-benzoquinone)
    • Makinen PL, Makinen KK, (1988) Near stoichiometric, irreversible inactivation of bacterial collagenases by o-chloranil (3,4,5,6-tetrachloro-1,2-benzoquinone). Biochem Biophys Res Commun 153: 74-80.
    • (1988) Biochem Biophys Res Commun , vol.153 , pp. 74-80
    • Makinen, P.L.1    Makinen, K.K.2
  • 40
    • 0034643274 scopus 로고    scopus 로고
    • Increased aquaporin-4 immunoreactivity in rat brain in response to systemic hyponatremia
    • Vajda Z, Promeneur D, Doczi T, Sulyok E, Frokiaer J, et al. (2000) Increased aquaporin-4 immunoreactivity in rat brain in response to systemic hyponatremia. Biochem Biophys Res Commun 270: 495-503.
    • (2000) Biochem Biophys Res Commun , vol.270 , pp. 495-503
    • Vajda, Z.1    Promeneur, D.2    Doczi, T.3    Sulyok, E.4    Frokiaer, J.5
  • 41
    • 4644314913 scopus 로고    scopus 로고
    • Aquaporin-4 facilitates reabsorption of excess fluid in vasogenic brain edema
    • Papadopoulos MC, Manley GT, Krishna S, Verkman AS, (2004) Aquaporin-4 facilitates reabsorption of excess fluid in vasogenic brain edema. FASEB J 18: 1291-1293.
    • (2004) FASEB J , vol.18 , pp. 1291-1293
    • Papadopoulos, M.C.1    Manley, G.T.2    Krishna, S.3    Verkman, A.S.4
  • 42
    • 0029872357 scopus 로고    scopus 로고
    • Oxidative DNA lesions in V79 cells mediated by pentachlorophenol metabolites
    • Dahlhaus M, Almstadt E, Henschke P, Luttgert S, Appel KE, (1996) Oxidative DNA lesions in V79 cells mediated by pentachlorophenol metabolites. Arch Toxicol 70: 457-460.
    • (1996) Arch Toxicol , vol.70 , pp. 457-460
    • Dahlhaus, M.1    Almstadt, E.2    Henschke, P.3    Luttgert, S.4    Appel, K.E.5
  • 43
    • 0034956503 scopus 로고    scopus 로고
    • Association of quinone-induced platelet anti-aggregation with cytotoxicity
    • Kim SR, Lee JY, Lee MY, Chung SM, Bae ON, et al. (2001) Association of quinone-induced platelet anti-aggregation with cytotoxicity. Toxicol Sci 62: 176-182.
    • (2001) Toxicol Sci , vol.62 , pp. 176-182
    • Kim, S.R.1    Lee, J.Y.2    Lee, M.Y.3    Chung, S.M.4    Bae, O.N.5
  • 44
    • 0030927683 scopus 로고    scopus 로고
    • Characterization of the hypo-osmolarity-induced Ca2+ response in cultured rat astrocytes
    • Fischer R, Schliess F, Haussinger D, (1997) Characterization of the hypo-osmolarity-induced Ca2+ response in cultured rat astrocytes. Glia 20: 51-58.
    • (1997) Glia , vol.20 , pp. 51-58
    • Fischer, R.1    Schliess, F.2    Haussinger, D.3
  • 45
    • 0026461474 scopus 로고
    • Reperfusion paradox: a novel mode of glial cell injury
    • Kim-Lee MH, Stokes BT, Yates AJ, (1992) Reperfusion paradox: a novel mode of glial cell injury. Glia 5: 56-64.
    • (1992) Glia , vol.5 , pp. 56-64
    • Kim-Lee, M.H.1    Stokes, B.T.2    Yates, A.J.3
  • 46
    • 0030442437 scopus 로고    scopus 로고
    • Ultrastructural changes in the blood-brain barrier in rats after treatment with nimodipine and flunarizine. A comparison
    • Zumkeller M, Dietz H, (1996) Ultrastructural changes in the blood-brain barrier in rats after treatment with nimodipine and flunarizine. A comparison. Neurosurg Rev 19: 253-260.
    • (1996) Neurosurg Rev , vol.19 , pp. 253-260
    • Zumkeller, M.1    Dietz, H.2
  • 47
    • 0023760283 scopus 로고
    • Cerebral protective effect of flunarizine in a canine model of cerebral ischaemia
    • Abiko H, Mizoi K, Suzuki J, Oba M, Yoshimoto T, (1988) Cerebral protective effect of flunarizine in a canine model of cerebral ischaemia. Neurol Res 10: 145-150.
    • (1988) Neurol Res , vol.10 , pp. 145-150
    • Abiko, H.1    Mizoi, K.2    Suzuki, J.3    Oba, M.4    Yoshimoto, T.5
  • 48
    • 0028058866 scopus 로고
    • Interstitial and tissue cations and electrical potential after experimental spinal cord injury
    • Leybaert L, De Ley G, (1994) Interstitial and tissue cations and electrical potential after experimental spinal cord injury. Exp Brain Res 100: 369-375.
    • (1994) Exp Brain Res , vol.100 , pp. 369-375
    • Leybaert, L.1    de Ley, G.2
  • 49
    • 0022899213 scopus 로고
    • Is there a need for alternative approaches in the therapy of cerebrovascular disorders?
    • Hartmann A, (1986) Is there a need for alternative approaches in the therapy of cerebrovascular disorders? Eur Neurol 25 (Suppl 1): 7-26.
    • (1986) Eur Neurol , vol.25 , Issue.SUPPL. 1 , pp. 7-26
    • Hartmann, A.1
  • 50
    • 34447503275 scopus 로고    scopus 로고
    • Beta-dystroglycan as a target for MMP-9, in response to enhanced neuronal activity
    • Michaluk P, Kolodziej L, Mioduszewska B, Wilczynski GM, Dzwonek J, et al. (2007) Beta-dystroglycan as a target for MMP-9, in response to enhanced neuronal activity. J Biol Chem 282: 16036-16041.
    • (2007) J Biol Chem , vol.282 , pp. 16036-16041
    • Michaluk, P.1    Kolodziej, L.2    Mioduszewska, B.3    Wilczynski, G.M.4    Dzwonek, J.5
  • 51
    • 4344578294 scopus 로고    scopus 로고
    • Proteolytic enzymes and altered glycosylation modulate dystroglycan function in carcinoma cells
    • Singh J, Itahana Y, Knight-Krajewski S, Kanagawa M, Campbell KP, et al. (2004) Proteolytic enzymes and altered glycosylation modulate dystroglycan function in carcinoma cells. Cancer Res 64: 6152-6159.
    • (2004) Cancer Res , vol.64 , pp. 6152-6159
    • Singh, J.1    Itahana, Y.2    Knight-Krajewski, S.3    Kanagawa, M.4    Campbell, K.P.5
  • 52
    • 34047114464 scopus 로고    scopus 로고
    • Oxidative stress activates protein tyrosine kinase and matrix metalloproteinases leading to blood-brain barrier dysfunction
    • Haorah J, Ramirez SH, Schall K, Smith D, Pandya R, et al. (2007) Oxidative stress activates protein tyrosine kinase and matrix metalloproteinases leading to blood-brain barrier dysfunction. J Neurochem 101: 566-576.
    • (2007) J Neurochem , vol.101 , pp. 566-576
    • Haorah, J.1    Ramirez, S.H.2    Schall, K.3    Smith, D.4    Pandya, R.5
  • 53
    • 67650153191 scopus 로고    scopus 로고
    • Involvement of ROS in BBB dysfunction
    • Pun PB, Lu J, Moochhala S, (2009) Involvement of ROS in BBB dysfunction. Free Radic Res 43: 348-364.
    • (2009) Free Radic Res , vol.43 , pp. 348-364
    • Pun, P.B.1    Lu, J.2    Moochhala, S.3
  • 54
    • 0037738484 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 in pneumococcal meningitis: activation via an oxidative pathway
    • Meli DN, Christen S, Leib SL, (2003) Matrix metalloproteinase-9 in pneumococcal meningitis: activation via an oxidative pathway. J Infect Dis 187: 1411-1415.
    • (2003) J Infect Dis , vol.187 , pp. 1411-1415
    • Meli, D.N.1    Christen, S.2    Leib, S.L.3
  • 55
    • 41149104941 scopus 로고    scopus 로고
    • The rapid decrease in astrocyte-associated dystroglycan expression by focal cerebral ischemia is protease-dependent
    • Milner R, Hung S, Wang X, Spatz M, del Zoppo GJ, (2008) The rapid decrease in astrocyte-associated dystroglycan expression by focal cerebral ischemia is protease-dependent. J Cereb Blood Flow Metab 28: 812-823.
    • (2008) J Cereb Blood Flow Metab , vol.28 , pp. 812-823
    • Milner, R.1    Hung, S.2    Wang, X.3    Spatz, M.4    del Zoppo, G.J.5
  • 56
    • 64649093828 scopus 로고    scopus 로고
    • Inhibition of gelatinase activity reduces neural injury in an ex vivo model of hypoxia-ischemia
    • Leonardo CC, Hall AA, Collier LA, Gottschall PE, Pennypacker KR, (2009) Inhibition of gelatinase activity reduces neural injury in an ex vivo model of hypoxia-ischemia. Neuroscience 160: 755-766.
    • (2009) Neuroscience , vol.160 , pp. 755-766
    • Leonardo, C.C.1    Hall, A.A.2    Collier, L.A.3    Gottschall, P.E.4    Pennypacker, K.R.5
  • 57
    • 33645022060 scopus 로고    scopus 로고
    • Synaptic remodeling induced by axotomy of superior cervical ganglion neurons: Involvement of metalloproteinase-2
    • Paggi P, De Stefano ME, Petrucci TC, (2006) Synaptic remodeling induced by axotomy of superior cervical ganglion neurons: Involvement of metalloproteinase-2. J Physiol Paris 99: 119-124.
    • (2006) J Physiol Paris , vol.99 , pp. 119-124
    • Paggi, P.1    de Stefano, M.E.2    Petrucci, T.C.3
  • 59
    • 33646835580 scopus 로고    scopus 로고
    • Characterization of the protease activity that cleaves the extracellular domain of beta-dystroglycan
    • Zhong D, Saito F, Saito Y, Nakamura A, Shimizu T, et al. (2006) Characterization of the protease activity that cleaves the extracellular domain of beta-dystroglycan. Biochem Biophys Res Commun 345: 867-871.
    • (2006) Biochem Biophys Res Commun , vol.345 , pp. 867-871
    • Zhong, D.1    Saito, F.2    Saito, Y.3    Nakamura, A.4    Shimizu, T.5
  • 61
    • 33646584823 scopus 로고    scopus 로고
    • Recent advances in MMP inhibitor design
    • Fisher JF, Mobashery S, (2006) Recent advances in MMP inhibitor design. Cancer Metastasis Rev 25: 115-136.
    • (2006) Cancer Metastasis Rev , vol.25 , pp. 115-136
    • Fisher, J.F.1    Mobashery, S.2
  • 62
    • 0036512208 scopus 로고    scopus 로고
    • New functions for the matrix metalloproteinases in cancer progression
    • Egeblad M, Werb Z, (2002) New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2: 161-174.
    • (2002) Nat Rev Cancer , vol.2 , pp. 161-174
    • Egeblad, M.1    Werb, Z.2
  • 64
    • 10744221757 scopus 로고    scopus 로고
    • Differential inhibition of membrane type 3 (MT3)-matrix metalloproteinase (MMP) and MT1-MMP by tissue inhibitor of metalloproteinase (TIMP)-2 and TIMP-3 rgulates pro-MMP-2 activation
    • Zhao H, Bernardo MM, Osenkowski P, Sohail A, Pei D, et al. (2004) Differential inhibition of membrane type 3 (MT3)-matrix metalloproteinase (MMP) and MT1-MMP by tissue inhibitor of metalloproteinase (TIMP)-2 and TIMP-3 rgulates pro-MMP-2 activation. J Biol Chem 279: 8592-8601.
    • (2004) J Biol Chem , vol.279 , pp. 8592-8601
    • Zhao, H.1    Bernardo, M.M.2    Osenkowski, P.3    Sohail, A.4    Pei, D.5
  • 65
    • 2542551340 scopus 로고    scopus 로고
    • Reperfusion-induced oxidative/nitrative injury to neurovascular unit after focal cerebral ischemia
    • Gursoy-Ozdemir Y, Can A, Dalkara T, (2004) Reperfusion-induced oxidative/nitrative injury to neurovascular unit after focal cerebral ischemia. Stroke 35: 1449-1453.
    • (2004) Stroke , vol.35 , pp. 1449-1453
    • Gursoy-Ozdemir, Y.1    Can, A.2    Dalkara, T.3


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