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Volumn 20, Issue 14, 2006, Pages

Diapedesis of monocytes is associated with MMP-mediated occludin disappearance in brain endothelial cells

Author keywords

Blood brain barrier; Diapedesis; Matrix metalloproteinase; Occludin; Tight junction

Indexed keywords

GREEN FLUORESCENT PROTEIN; MATRIX METALLOPROTEINASE; MATRIX METALLOPROTEINASE INHIBITOR; OCCLUDIN; PROTEIN ZO1; BB 3103; HYDROXAMIC ACID; MEMBRANE PROTEIN; PHOSPHOPROTEIN; ZONULA OCCLUDENS 1 PROTEIN; ZONULA OCCLUDENS-1 PROTEIN;

EID: 33845665284     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fj.06-6099fje     Document Type: Article
Times cited : (108)

References (59)
  • 1
    • 0017116756 scopus 로고
    • Substructure of intercellular junctions in freeze-fractured alveolar-capillary membranes of mouse lung
    • Schneeberger, E. E., and Karnovsky, M. J. (1976) Substructure of intercellular junctions in freeze-fractured alveolar-capillary membranes of mouse lung. Circ. Res. 38, 404-411
    • (1976) Circ. Res. , vol.38 , pp. 404-411
    • Schneeberger, E.E.1    Karnovsky, M.J.2
  • 2
    • 0016140812 scopus 로고
    • Structure and function of intercellular junctions
    • Staehelin, L. A. (1974) Structure and function of intercellular junctions. Int. Rev. Cytol. 39, 191-283
    • (1974) Int. Rev. Cytol. , vol.39 , pp. 191-283
    • Staehelin, L.A.1
  • 3
    • 0032936851 scopus 로고    scopus 로고
    • The cell biology of the blood-brain barrier
    • Rubin, L. L., and Staddon, J. M. (1999) The cell biology of the blood-brain barrier. Annu. Rev. Neurosci. 22, 11-28
    • (1999) Annu. Rev. Neurosci. , vol.22 , pp. 11-28
    • Rubin, L.L.1    Staddon, J.M.2
  • 4
    • 0033866453 scopus 로고    scopus 로고
    • Monocyte infiltration is highly associated with loss of the tight junction protein zonula occludens in HIV-1-associated dementia
    • Boven, L. A., Middel, J., Verhoef, J., De Groot, C. J., and Nottet, H. S. (2000) Monocyte infiltration is highly associated with loss of the tight junction protein zonula occludens in HIV-1-associated dementia. Neuropathol. Appl. Neurobiol. 26, 356-360
    • (2000) Neuropathol. Appl. Neurobiol. , vol.26 , pp. 356-360
    • Boven, L.A.1    Middel, J.2    Verhoef, J.3    De Groot, C.J.4    Nottet, H.S.5
  • 6
    • 0141926694 scopus 로고    scopus 로고
    • Tight junctional abnormality in multiple sclerosis white matter affects all calibres of vessel and is associated with blood-brain barrier leakage and active demyelination
    • Kirk, J., Plumb, J., Mirakhur, M., and McQuaid, S. (2003) Tight junctional abnormality in multiple sclerosis white matter affects all calibres of vessel and is associated with blood-brain barrier leakage and active demyelination. J. Pathol. 201, 319-327
    • (2003) J. Pathol. , vol.201 , pp. 319-327
    • Kirk, J.1    Plumb, J.2    Mirakhur, M.3    McQuaid, S.4
  • 7
    • 0036211141 scopus 로고    scopus 로고
    • Abnormal endothelial tight junctions in active lesions and normal-appearing white matter in multiple sclerosis
    • Plumb, J., McQuaid, S., Mirakhur, M., and Kirk, J. (2002) Abnormal endothelial tight junctions in active lesions and normal-appearing white matter in multiple sclerosis. Brain Pathol. 12, 154-169
    • (2002) Brain Pathol. , vol.12 , pp. 154-169
    • Plumb, J.1    McQuaid, S.2    Mirakhur, M.3    Kirk, J.4
  • 9
    • 0036084919 scopus 로고    scopus 로고
    • Cerebral microvascular changes in permeability and tight junctions induced by hypoxiareoxygenation
    • Mark, K. S., and Davis, T. P. (2002) Cerebral microvascular changes in permeability and tight junctions induced by hypoxiareoxygenation. Am. J. Physiol. 282, H1485-H1494
    • (2002) Am. J. Physiol. , vol.282
    • Mark, K.S.1    Davis, T.P.2
  • 11
    • 0032547833 scopus 로고    scopus 로고
    • A single gene product, claudin-1 or 2, reconstitutes tight junction strands and recruits occludin in fibroblasts
    • Furuse, M., Sasaki, H., Fujimoto, K., and Tsukita, S. (1998) A single gene product, claudin-1 or 2, reconstitutes tight junction strands and recruits occludin in fibroblasts. J. Cell Biol. 143, 391-401
    • (1998) J. Cell Biol. , vol.143 , pp. 391-401
    • Furuse, M.1    Sasaki, H.2    Fujimoto, K.3    Tsukita, S.4
  • 14
    • 0034038626 scopus 로고    scopus 로고
    • Multiple domains of occludin are involved in the regulation of paracellular permeability
    • Balda, M. S., Flores-Maldonado, C., Cereijido, M., and Matter, K. (2000) Multiple domains of occludin are involved in the regulation of paracellular permeability. J. Cell. Biochem. 78, 85-96
    • (2000) J. Cell. Biochem. , vol.78 , pp. 85-96
    • Balda, M.S.1    Flores-Maldonado, C.2    Cereijido, M.3    Matter, K.4
  • 15
    • 0028110309 scopus 로고
    • Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions
    • Furuse, M., Itoh, M., Hirase, T., Nagafuchi, A., Yonemura, S., Tsukita, S., and Tsukita, S. (1994) Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions. J. Cell Biol. 127, 1617-1626
    • (1994) J. Cell Biol. , vol.127 , pp. 1617-1626
    • Furuse, M.1    Itoh, M.2    Hirase, T.3    Nagafuchi, A.4    Yonemura, S.5    Tsukita, S.6    Tsukita, S.7
  • 16
    • 0032491391 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton
    • Fanning, A. S., Jameson, B. J., Jesaitis, L. A., and Anderson, J. M. (1998) The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton. J. Biol. Chem. 273, 29745-29753
    • (1998) J. Biol. Chem. , vol.273 , pp. 29745-29753
    • Fanning, A.S.1    Jameson, B.J.2    Jesaitis, L.A.3    Anderson, J.M.4
  • 17
    • 0032489875 scopus 로고    scopus 로고
    • ZO-3, a novel member of the MAGUK protein family found at the tight junction, interacts with ZO-1 and occludin
    • Haskins, J., Gu, L., Wittchen, E. S., Hibbard, J., and Stevenson, B. R. (1998) ZO-3, a novel member of the MAGUK protein family found at the tight junction, interacts with ZO-1 and occludin. J. Cell Biol. 141, 199-208
    • (1998) J. Cell Biol. , vol.141 , pp. 199-208
    • Haskins, J.1    Gu, L.2    Wittchen, E.S.3    Hibbard, J.4    Stevenson, B.R.5
  • 18
    • 0037336565 scopus 로고    scopus 로고
    • Signalling to and from tight junctions
    • Matter, K., and Balda, M. S. (2003) Signalling to and from tight junctions. Nat. Rev. Mol. Cell. Biol. 4, 225-236
    • (2003) Nat. Rev. Mol. Cell. Biol. , vol.4 , pp. 225-236
    • Matter, K.1    Balda, M.S.2
  • 19
    • 0030113804 scopus 로고    scopus 로고
    • Cell signalling: MAGUK magic
    • Anderson, J. M. (1996) Cell signalling: MAGUK magic. Curr. Biol. 6, 382-384
    • (1996) Curr. Biol. , vol.6 , pp. 382-384
    • Anderson, J.M.1
  • 21
    • 0036644958 scopus 로고    scopus 로고
    • Extracellular proteolysis in brain injury and inflammation: Role for plasminogen activators and matrix metalloproteinases
    • Lo, E. H., Wang, X., and Cuzner, M. L. (2002) Extracellular proteolysis in brain injury and inflammation: role for plasminogen activators and matrix metalloproteinases. J. Neurosci. Res. 69, 1-9
    • (2002) J. Neurosci. Res. , vol.69 , pp. 1-9
    • Lo, E.H.1    Wang, X.2    Cuzner, M.L.3
  • 22
    • 0036737795 scopus 로고    scopus 로고
    • Matrix metalloproteinases in neuroinflammation
    • Rosenberg, G. A. (2002) Matrix metalloproteinases in neuroinflammation. Glia 39, 279-291
    • (2002) Glia , vol.39 , pp. 279-291
    • Rosenberg, G.A.1
  • 23
    • 0030560709 scopus 로고    scopus 로고
    • SV40 large T immortalised cell lines of the rat blood-brain and blood-retinal barriers retain their phenotypic and immunological characteristics
    • Greenwood, J., Pryce, G., Devine, L., Male, D. K., dos Santos, W. L., Calder, V. L., and Adamson, P. (1996) SV40 large T immortalised cell lines of the rat blood-brain and blood-retinal barriers retain their phenotypic and immunological characteristics. J. Neuroimmunol. 71, 51-63
    • (1996) J. Neuroimmunol. , vol.71 , pp. 51-63
    • Greenwood, J.1    Pryce, G.2    Devine, L.3    Male, D.K.4    Dos Santos, W.L.5    Calder, V.L.6    Adamson, P.7
  • 25
    • 0029833422 scopus 로고    scopus 로고
    • Episomal vectors rapidly and stably produce high-titer recombinant retrovirus
    • Kinsella, T. M., and Nolan, G. P. (1996) Episomal vectors rapidly and stably produce high-titer recombinant retrovirus. Hum. Gene Ther. 7, 1405-1413
    • (1996) Hum. Gene Ther. , vol.7 , pp. 1405-1413
    • Kinsella, T.M.1    Nolan, G.P.2
  • 28
    • 0032567764 scopus 로고    scopus 로고
    • In vitro degradation of endothelial catenins by a neutrophil protease
    • Moll, T., Dejana, E., and Vestweber, D. (1998) In vitro degradation of endothelial catenins by a neutrophil protease. J. Cell Biol. 140, 403-407
    • (1998) J. Cell Biol. , vol.140 , pp. 403-407
    • Moll, T.1    Dejana, E.2    Vestweber, D.3
  • 30
    • 0034121588 scopus 로고    scopus 로고
    • Dexamethasone regulation of matrix metalloproteinase expression in CNS vascular endothelium
    • Harkness, K. A., Adamson, P., Sussman, J. D., vies-Jones, G. A., Greenwood, J., and Woodroofe, M. N. (2000) Dexamethasone regulation of matrix metalloproteinase expression in CNS vascular endothelium. Brain 123, 698-709
    • (2000) Brain , vol.123 , pp. 698-709
    • Harkness, K.A.1    Adamson, P.2    Sussman, J.D.3    Vies-Jones, G.A.4    Greenwood, J.5    Woodroofe, M.N.6
  • 31
    • 0034977693 scopus 로고    scopus 로고
    • Inflammatory pain alters blood-brain barrier permeability and tight junctional protein expression
    • Huber, J. D., Witt, K. A., Hom, S., Egleton, R. D., Mark, K. S., and Davis, T. P. (2001) Inflammatory pain alters blood-brain barrier permeability and tight junctional protein expression. Am. J. Physiol. 280, H1241-H1248
    • (2001) Am. J. Physiol. , vol.280
    • Huber, J.D.1    Witt, K.A.2    Hom, S.3    Egleton, R.D.4    Mark, K.S.5    Davis, T.P.6
  • 32
    • 0036784006 scopus 로고    scopus 로고
    • Blood-brain barrier tight junctions are altered during a 72-h exposure to lambda-carrageenan-induced inflammatory pain
    • Huber, J. D., Hau, V. S., Borg, L., Campos, C. R., Egleton, R. D., and Davis, T. P. (2002) Blood-brain barrier tight junctions are altered during a 72-h exposure to lambda-carrageenan-induced inflammatory pain. Am. J. Physiol. 283, H1531-H1537
    • (2002) Am. J. Physiol. , vol.283
    • Huber, J.D.1    Hau, V.S.2    Borg, L.3    Campos, C.R.4    Egleton, R.D.5    Davis, T.P.6
  • 33
    • 0032543607 scopus 로고    scopus 로고
    • Loss of the tight junction proteins occludin and zonula occludens-1 from cerebral vascular endothelium during neutrophil-induced blood-brain barrier breakdown in vivo
    • Bolton, S. J., Anthony, D. C., and Perry, V. H. (1998) Loss of the tight junction proteins occludin and zonula occludens-1 from cerebral vascular endothelium during neutrophil-induced blood-brain barrier breakdown in vivo. Neuroscience 86, 1245-1257
    • (1998) Neuroscience , vol.86 , pp. 1245-1257
    • Bolton, S.J.1    Anthony, D.C.2    Perry, V.H.3
  • 34
  • 35
    • 23244447749 scopus 로고    scopus 로고
    • Leukocyte diapedesis in vivo induces transient loss of tight junction protein at the blood-retina barrier
    • Xu, H., Dawson, R., Crane, I. J., and Liversidge, J. (2005) Leukocyte diapedesis in vivo induces transient loss of tight junction protein at the blood-retina barrier. Invest Ophthalmol. Vis. Sci. 46, 2487-2494
    • (2005) Invest Ophthalmol. Vis. Sci. , vol.46 , pp. 2487-2494
    • Xu, H.1    Dawson, R.2    Crane, I.J.3    Liversidge, J.4
  • 36
    • 0033979993 scopus 로고    scopus 로고
    • Inflammation and stroke: Putative role for cytokines, adhesion molecules and iNOS in brain response to ischemia
    • del Zoppo G., Ginis, I., Hallenbeck, J. M., Iadecola, C., Wang, X., and Feuerstein, G. Z. (2000) Inflammation and stroke: putative role for cytokines, adhesion molecules and iNOS in brain response to ischemia. Brain Pathol. 10, 95-112
    • (2000) Brain Pathol. , vol.10 , pp. 95-112
    • Del Zoppo, G.1    Ginis, I.2    Hallenbeck, J.M.3    Iadecola, C.4    Wang, X.5    Feuerstein, G.Z.6
  • 38
    • 7244248569 scopus 로고    scopus 로고
    • A transmigratory cup in leukocyte diapedesis both through individual vascular endothelial cells and between them
    • Carman, C. V., and Springer, T. A. (2004) A transmigratory cup in leukocyte diapedesis both through individual vascular endothelial cells and between them. J. Cell Biol. 167, 377-388
    • (2004) J. Cell Biol. , vol.167 , pp. 377-388
    • Carman, C.V.1    Springer, T.A.2
  • 39
    • 0032536833 scopus 로고    scopus 로고
    • Neutrophils emigrate from venules by a transendothelial cell pathway in response to FMLP
    • Feng, D., Nagy, J. A., Pyne, K., Dvorak, H. F., and Dvorak, A. M. (1998) Neutrophils emigrate from venules by a transendothelial cell pathway in response to FMLP. J. Exp. Med. 187, 903-915
    • (1998) J. Exp. Med. , vol.187 , pp. 903-915
    • Feng, D.1    Nagy, J.A.2    Pyne, K.3    Dvorak, H.F.4    Dvorak, A.M.5
  • 40
    • 16344368162 scopus 로고    scopus 로고
    • Diapedesis of mononuclear cells across cerebral venules during experimental autoimmune encephalomyelitis leaves tight junctions intact
    • Wolburg, H., Wolburg-Buchholz, K., and Engelhardt, B. (2005) Diapedesis of mononuclear cells across cerebral venules during experimental autoimmune encephalomyelitis leaves tight junctions intact. Acta Neuropathol. (Berlin) 109, 181-190
    • (2005) Acta Neuropathol. (Berlin) , vol.109 , pp. 181-190
    • Wolburg, H.1    Wolburg-Buchholz, K.2    Engelhardt, B.3
  • 41
    • 0034627829 scopus 로고    scopus 로고
    • Monocytes induce reversible focal changes in vascular endothelial cadherin complex during transendothelial migration under flow
    • Allport, J. R., Muller, W. A., and Luscinskas, F. W. (2000) Monocytes induce reversible focal changes in vascular endothelial cadherin complex during transendothelial migration under flow. J. Cell Biol. 148, 203-216
    • (2000) J. Cell Biol. , vol.148 , pp. 203-216
    • Allport, J.R.1    Muller, W.A.2    Luscinskas, F.W.3
  • 42
    • 0030872246 scopus 로고    scopus 로고
    • Endothelial-dependent mechanisms regulate leukocyte transmigration: A process involving the proteasome and disruption of the vascular endothelial-cadherin complex at endothelial cell-to-cell junctions
    • Allport, J. R., Ding, H., Collins, T., Gerritsen, M. E., and Luscinskas, F. W. (1997) Endothelial-dependent mechanisms regulate leukocyte transmigration: a process involving the proteasome and disruption of the vascular endothelial-cadherin complex at endothelial cell-to-cell junctions. J. Exp. Med. 186, 517-527
    • (1997) J. Exp. Med. , vol.186 , pp. 517-527
    • Allport, J.R.1    Ding, H.2    Collins, T.3    Gerritsen, M.E.4    Luscinskas, F.W.5
  • 43
    • 0035881250 scopus 로고    scopus 로고
    • Real-time imaging of vascular endothelial-cadherin during leukocyte transmigration across endothelium
    • Shaw, S. K., Bamba, P. S., Perkins, B. N., and Luscinskas, F. W. (2001) Real-time imaging of vascular endothelial-cadherin during leukocyte transmigration across endothelium. J. Immunol. 167, 2323-2330
    • (2001) J. Immunol. , vol.167 , pp. 2323-2330
    • Shaw, S.K.1    Bamba, P.S.2    Perkins, B.N.3    Luscinskas, F.W.4
  • 44
    • 0035958937 scopus 로고    scopus 로고
    • Claudin promotes activation of pro-matrix metalloproteinase-2 mediated by membrane-type matrix metalloproteinases
    • Miyamori, H., Takino, T., Kobayashi, Y., Tokai, H., Itoh, Y., Seiki, M., and Sato, H. (2001) Claudin promotes activation of pro-matrix metalloproteinase-2 mediated by membrane-type matrix metalloproteinases. J. Biol. Chem. 276, 28204-28211
    • (2001) J. Biol. Chem. , vol.276 , pp. 28204-28211
    • Miyamori, H.1    Takino, T.2    Kobayashi, Y.3    Tokai, H.4    Itoh, Y.5    Seiki, M.6    Sato, H.7
  • 45
    • 24744470324 scopus 로고    scopus 로고
    • Membrane-type 1 matrix metalloproteinase expression is regulated by zonula occludens-1 in human breast cancer cells
    • Polette, M., Gilles, C., Nawrocki-Raby, B., Lohi, J., Hunziker, W., Foidart, J. M., and Birembaut, P. (2005) Membrane-type 1 matrix metalloproteinase expression is regulated by zonula occludens-1 in human breast cancer cells. Cancer Res. 65, 7691-7698
    • (2005) Cancer Res. , vol.65 , pp. 7691-7698
    • Polette, M.1    Gilles, C.2    Nawrocki-Raby, B.3    Lohi, J.4    Hunziker, W.5    Foidart, J.M.6    Birembaut, P.7
  • 46
    • 0030043414 scopus 로고    scopus 로고
    • Overexpression of occludin, a tight junction-associated integral membrane protein, induces the formation of intracellular multilamellar bodies bearing tight junction-like structures
    • Furuse, M., Fujimoto, K., Sato, N., Hirase, T., Tsukita, S., and Tsukita, S. (1996) Overexpression of occludin, a tight junction-associated integral membrane protein, induces the formation of intracellular multilamellar bodies bearing tight junction-like structures. J. Cell Sci. 109, 429-435
    • (1996) J. Cell Sci. , vol.109 , pp. 429-435
    • Furuse, M.1    Fujimoto, K.2    Sato, N.3    Hirase, T.4    Tsukita, S.5    Tsukita, S.6
  • 47
    • 0030983484 scopus 로고    scopus 로고
    • Occludin confers adhesiveness when expressed in fibroblasts
    • Van Itallie, C. M., and Anderson, J. M. (1997) Occludin confers adhesiveness when expressed in fibroblasts. J. Cell Sci. 110, 1113-1121
    • (1997) J. Cell Sci. , vol.110 , pp. 1113-1121
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 48
    • 0037385335 scopus 로고    scopus 로고
    • Regulation and functional effects of monocyte migration across human brain-derived endothelial cells
    • Seguin, R., Biernacki, K., Rotondo, R. L., Prat, A., and Antel, J. P. (2003) Regulation and functional effects of monocyte migration across human brain-derived endothelial cells. J. Neuropathol. Exp. Neurol. 62, 412-419
    • (2003) J. Neuropathol. Exp. Neurol. , vol.62 , pp. 412-419
    • Seguin, R.1    Biernacki, K.2    Rotondo, R.L.3    Prat, A.4    Antel, J.P.5
  • 49
    • 0037155884 scopus 로고    scopus 로고
    • The tight junction-specific protein occludin is a functional target of the E3 ubiquitin-protein ligase itch
    • Traweger, A., Fang, D., Liu, Y. C., Stelzhammer, W., Krizbai, I. A., Fresser, F., Bauer, H. C., and Bauer, H. (2002) The tight junction-specific protein occludin is a functional target of the E3 ubiquitin-protein ligase itch. J. Biol. Chem. 277, 10201-10208
    • (2002) J. Biol. Chem. , vol.277 , pp. 10201-10208
    • Traweger, A.1    Fang, D.2    Liu, Y.C.3    Stelzhammer, W.4    Krizbai, I.A.5    Fresser, F.6    Bauer, H.C.7    Bauer, H.8
  • 50
    • 30044442771 scopus 로고    scopus 로고
    • MAP kinase interacts with occludin and mediates EGF-induced prevention of tight junction disruption by hydrogen peroxide
    • Basuroy, S., Seth, A., Elias, B., Naren, A., and Rao, R. (2005) MAP kinase interacts with occludin and mediates EGF-induced prevention of tight junction disruption by hydrogen peroxide. Biochem. J. 393, 69-77
    • (2005) Biochem. J. , vol.393 , pp. 69-77
    • Basuroy, S.1    Seth, A.2    Elias, B.3    Naren, A.4    Rao, R.5
  • 51
    • 1542677112 scopus 로고    scopus 로고
    • Role of phosphatidylinositol 3-kinase in oxidative stress-induced disruption of tight junctions
    • Sheth, P., Basuroy, S., Li, C., Naren, A. P., and Rao, R. K. (2003) Role of phosphatidylinositol 3-kinase in oxidative stress-induced disruption of tight junctions. J. Biol. Chem. 278, 49239-49245
    • (2003) J. Biol. Chem. , vol.278 , pp. 49239-49245
    • Sheth, P.1    Basuroy, S.2    Li, C.3    Naren, A.P.4    Rao, R.K.5
  • 52
    • 0031425958 scopus 로고    scopus 로고
    • Phosphorylation of occludin correlates with occludin localization and function at the tight junction
    • Wong, V. (1997) Phosphorylation of occludin correlates with occludin localization and function at the tight junction. Am. J. Physiol. 273, C1859-C1867
    • (1997) Am. J. Physiol. , vol.273
    • Wong, V.1
  • 53
  • 54
    • 0346851871 scopus 로고    scopus 로고
    • Tyrosine phosphatase inhibition induces loss of blood-brain barrier integrity by matrix metalloproteinase-dependent and -independent pathways
    • Lohmann, C., Krischke, M., Wegener, J., and Galla, H. J. (2004) Tyrosine phosphatase inhibition induces loss of blood-brain barrier integrity by matrix metalloproteinase-dependent and -independent pathways. Brain Res. 995, 184-196
    • (2004) Brain Res. , vol.995 , pp. 184-196
    • Lohmann, C.1    Krischke, M.2    Wegener, J.3    Galla, H.J.4
  • 55
    • 0033491912 scopus 로고    scopus 로고
    • Occludin proteolysis and increased permeability in endothelial cells through tyrosine phosphatase inhibition
    • Wachtel, M., Frei, K., Ehler, E., Fontana, A., Winterhalter, K., and Gloor, S. M. (1999) Occludin proteolysis and increased permeability in endothelial cells through tyrosine phosphatase inhibition. J. Cell Sci. 112, 4347-4356
    • (1999) J. Cell Sci. , vol.112 , pp. 4347-4356
    • Wachtel, M.1    Frei, K.2    Ehler, E.3    Fontana, A.4    Winterhalter, K.5    Gloor, S.M.6
  • 56
    • 25844525721 scopus 로고    scopus 로고
    • Ischemia injury alters endothelial cell properties of kidney cortex: Stimulation of MMP-9
    • Caron, A., Desrosiers, R. R., and Beliveau, R. (2005) Ischemia injury alters endothelial cell properties of kidney cortex: stimulation of MMP-9. Exp. Cell Res. 310, 105-116
    • (2005) Exp. Cell Res. , vol.310 , pp. 105-116
    • Caron, A.1    Desrosiers, R.R.2    Beliveau, R.3
  • 57
    • 18744362465 scopus 로고    scopus 로고
    • Matrix metalloproteinases in early diabetic retinopathy and their role in alteration of the blood-retinal barrier
    • Giebel, S. J., Menicucci, G., McGuire, P. G., and Das, A. (2005) Matrix metalloproteinases in early diabetic retinopathy and their role in alteration of the blood-retinal barrier. Lab. Invest. 85, 597-607
    • (2005) Lab. Invest. , vol.85 , pp. 597-607
    • Giebel, S.J.1    Menicucci, G.2    McGuire, P.G.3    Das, A.4
  • 58
    • 0035097495 scopus 로고    scopus 로고
    • TGF-beta increases retinal endothelial cell permeability by increasing MMP-9: Possible role of glial cells in endothelial barrier function
    • Behzadian, M. A., Wang, X. L., Windsor, L. J., Ghaly, N., and Caldwell, R. B. (2001) TGF-beta increases retinal endothelial cell permeability by increasing MMP-9: possible role of glial cells in endothelial barrier function. Invest. Ophthalmol. Vis. Sci. 42, 853-859
    • (2001) Invest. Ophthalmol. Vis. Sci. , vol.42 , pp. 853-859
    • Behzadian, M.A.1    Wang, X.L.2    Windsor, L.J.3    Ghaly, N.4    Caldwell, R.B.5
  • 59
    • 11144221616 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 knockout confers resistance to corneal epithelial barrier disruption in experimental dry eye
    • Pflugfelder, S. C., Farley, W., Luo, L., Chen, L. Z., de Paiva, C. S., Olmos, L. C., Li, D. Q., and Fini, M. E. (2005) Matrix metalloproteinase-9 knockout confers resistance to corneal epithelial barrier disruption in experimental dry eye. Am. J. Pathol. 166, 61-71
    • (2005) Am. J. Pathol. , vol.166 , pp. 61-71
    • Pflugfelder, S.C.1    Farley, W.2    Luo, L.3    Chen, L.Z.4    De Paiva, C.S.5    Olmos, L.C.6    Li, D.Q.7    Fini, M.E.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.