메뉴 건너뛰기




Volumn 1326, Issue , 2010, Pages 114-127

Metalloproteinase mediated occludin cleavage in the cerebral microcapillary endothelium under pathological conditions

Author keywords

Blood brain barrier; Cerebral ischemia reperfusion; Claudin 5; Hydrogen peroxide; Matrix metalloproteinase; Occludin

Indexed keywords

CLAUDIN 5; GELATINASE A; GELATINASE B; HYDROGEN PEROXIDE; ILOMASTAT; OCCLUDIN;

EID: 77950048543     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.brainres.2010.02.054     Document Type: Article
Times cited : (88)

References (52)
  • 1
    • 57349199721 scopus 로고    scopus 로고
    • Vascular endothelial growth factor mediates the estrogen-induced breakdown of tight junctions between and increase in proliferation of microvessel endothelial cells in the baboon endometrium
    • Aberdeen G.W., Wiegand S.J., Bonagura Jr. T.W., Pepe G.J., and Albrecht E.D. Vascular endothelial growth factor mediates the estrogen-induced breakdown of tight junctions between and increase in proliferation of microvessel endothelial cells in the baboon endometrium. Endocrinology 149 (2008) 6076-6083
    • (2008) Endocrinology , vol.149 , pp. 6076-6083
    • Aberdeen, G.W.1    Wiegand, S.J.2    Bonagura Jr., T.W.3    Pepe, G.J.4    Albrecht, E.D.5
  • 2
    • 48249103532 scopus 로고    scopus 로고
    • Tissue plasminogen activator (tPA) and matrix metalloproteinases in the pathogenesis of stroke: therapeutic strategies
    • Adibhatla R.M., and Hatcher J.F. Tissue plasminogen activator (tPA) and matrix metalloproteinases in the pathogenesis of stroke: therapeutic strategies. CNS Neurol. Disord. Drug Targets 7 (2008) 243-253
    • (2008) CNS Neurol. Disord. Drug Targets , vol.7 , pp. 243-253
    • Adibhatla, R.M.1    Hatcher, J.F.2
  • 3
    • 0028799226 scopus 로고
    • Tight junctions and the molecular basis for regulation of paracellular permeability
    • Anderson J.M., and Van Itallie C.M. Tight junctions and the molecular basis for regulation of paracellular permeability. Am. J. Physiol. 269 (1995) G467-G475
    • (1995) Am. J. Physiol. , vol.269
    • Anderson, J.M.1    Van Itallie, C.M.2
  • 5
    • 0035914359 scopus 로고    scopus 로고
    • Protein kinase C regulates the phosphorylation and cellular localization of occludin
    • Andreeva A.Y., Krause E., Muller E.C., Blasig I.E., and Utepbergenov D.I. Protein kinase C regulates the phosphorylation and cellular localization of occludin. J. Biol. Chem. 276 (2001) 38480-38486
    • (2001) J. Biol. Chem. , vol.276 , pp. 38480-38486
    • Andreeva, A.Y.1    Krause, E.2    Muller, E.C.3    Blasig, I.E.4    Utepbergenov, D.I.5
  • 6
    • 0032769698 scopus 로고    scopus 로고
    • A dominant mutant of occludin disrupts tight junction structure and function
    • Bamforth S.D., Kniesel U., Wolburg H., Engelhardt B., and Risau W. A dominant mutant of occludin disrupts tight junction structure and function. J. Cell Sci. 112 Pt 12 (1999) 1879-1888
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 12 , pp. 1879-1888
    • Bamforth, S.D.1    Kniesel, U.2    Wolburg, H.3    Engelhardt, B.4    Risau, W.5
  • 8
    • 59349113948 scopus 로고    scopus 로고
    • Diverse roles of matrix metalloproteinases and tissue inhibitors of metalloproteinases in neuroinflammation and cerebral ischemia
    • Candelario-Jalil E., Yang Y., and Rosenberg G.A. Diverse roles of matrix metalloproteinases and tissue inhibitors of metalloproteinases in neuroinflammation and cerebral ischemia. Neuroscience 158 3 (2008) 983-994
    • (2008) Neuroscience , vol.158 , Issue.3 , pp. 983-994
    • Candelario-Jalil, E.1    Yang, Y.2    Rosenberg, G.A.3
  • 9
    • 0348141854 scopus 로고    scopus 로고
    • Activation systems for latent matrix metalloproteinase-2 are upregulated immediately after focal cerebral ischemia
    • Chang D.I., Hosomi N., Lucero J., Heo J.H., Abumiya T., Mazar A.P., and del Zoppo G.J. Activation systems for latent matrix metalloproteinase-2 are upregulated immediately after focal cerebral ischemia. J. Cereb. Blood Flow Metab. 23 (2003) 1408-1419
    • (2003) J. Cereb. Blood Flow Metab. , vol.23 , pp. 1408-1419
    • Chang, D.I.1    Hosomi, N.2    Lucero, J.3    Heo, J.H.4    Abumiya, T.5    Mazar, A.P.6    del Zoppo, G.J.7
  • 10
    • 0037214278 scopus 로고    scopus 로고
    • Glutathione peroxidase-1 contributes to the neuroprotection seen in the superoxide dismutase-1 transgenic mouse in response to ischemia/reperfusion injury
    • Crack P.J., Taylor J.M., de Haan J.B., Kola I., Hertzog P., and Iannello R.C. Glutathione peroxidase-1 contributes to the neuroprotection seen in the superoxide dismutase-1 transgenic mouse in response to ischemia/reperfusion injury. J. Cereb. Blood Flow Metab. 23 (2003) 19-22
    • (2003) J. Cereb. Blood Flow Metab. , vol.23 , pp. 19-22
    • Crack, P.J.1    Taylor, J.M.2    de Haan, J.B.3    Kola, I.4    Hertzog, P.5    Iannello, R.C.6
  • 11
    • 67249111377 scopus 로고    scopus 로고
    • Differential phosphorylation of occludin and tricellulin by CK2 and CK1
    • Dorfel M.J., Westphal J.K., and Huber O. Differential phosphorylation of occludin and tricellulin by CK2 and CK1. Ann. N. Y. Acad. Sci. 1165 (2009) 69-73
    • (2009) Ann. N. Y. Acad. Sci. , vol.1165 , pp. 69-73
    • Dorfel, M.J.1    Westphal, J.K.2    Huber, O.3
  • 12
    • 59449086585 scopus 로고    scopus 로고
    • Phosphorylation of Tyr-398 and Tyr-402 in occludin prevents its interaction with ZO-1 and destabilizes its assembly at the tight junctions
    • Elias B.C., Suzuki T., Seth A., Giorgianni F., Kale G., Shen L., Turner J.R., Naren A., Desiderio D.M., and Rao R. Phosphorylation of Tyr-398 and Tyr-402 in occludin prevents its interaction with ZO-1 and destabilizes its assembly at the tight junctions. J. Biol. Chem. 284 (2009) 1559-1569
    • (2009) J. Biol. Chem. , vol.284 , pp. 1559-1569
    • Elias, B.C.1    Suzuki, T.2    Seth, A.3    Giorgianni, F.4    Kale, G.5    Shen, L.6    Turner, J.R.7    Naren, A.8    Desiderio, D.M.9    Rao, R.10
  • 13
    • 50249125886 scopus 로고    scopus 로고
    • Inhibiting matrix metalloproteinase-2 reduces protein release into coronary effluent from isolated rat hearts during ischemia-reperfusion
    • Fert-Bober J., Leon H., Sawicka J., Basran R.S., Devon R.M., Schulz R., and Sawicki G. Inhibiting matrix metalloproteinase-2 reduces protein release into coronary effluent from isolated rat hearts during ischemia-reperfusion. Basic Res. Cardiol. 103 (2008) 431-443
    • (2008) Basic Res. Cardiol. , vol.103 , pp. 431-443
    • Fert-Bober, J.1    Leon, H.2    Sawicka, J.3    Basran, R.S.4    Devon, R.M.5    Schulz, R.6    Sawicki, G.7
  • 14
    • 0035194622 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibition prevents oxidative stress-associated blood-brain barrier disruption after transient focal cerebral ischemia
    • Gasche Y., Copin J.C., Sugawara T., Fujimura M., and Chan P.H. Matrix metalloproteinase inhibition prevents oxidative stress-associated blood-brain barrier disruption after transient focal cerebral ischemia. J. Cereb. Blood Flow Metab. 21 (2001) 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
  • 15
    • 63149195539 scopus 로고    scopus 로고
    • Anti-endothelial antibodies interfere in apoptotic cell clearance and promote thrombosis in patients with antiphospholipid syndrome
    • Graham A., Ford I., Morrison R., Barker R.N., Greaves M., and Erwig L.P. Anti-endothelial antibodies interfere in apoptotic cell clearance and promote thrombosis in patients with antiphospholipid syndrome. J. Immunol. 182 (2009) 1756-1762
    • (2009) J. Immunol. , vol.182 , pp. 1756-1762
    • Graham, A.1    Ford, I.2    Morrison, R.3    Barker, R.N.4    Greaves, M.5    Erwig, L.P.6
  • 16
    • 0142026252 scopus 로고    scopus 로고
    • Cyclic AMP induces phosphorylation of claudin-5 immunoprecipitates and expression of claudin-5 gene in blood-brain-barrier endothelial cells via protein kinase A-dependent and -independent pathways
    • Ishizaki T., Chiba H., Kojima T., Fujibe M., Soma T., Miyajima H., Nagasawa K., Wada I., and Sawada N. Cyclic AMP induces phosphorylation of claudin-5 immunoprecipitates and expression of claudin-5 gene in blood-brain-barrier endothelial cells via protein kinase A-dependent and -independent pathways. Exp. Cell Res. 290 2 (2003) 275-288
    • (2003) Exp. Cell Res. , vol.290 , Issue.2 , pp. 275-288
    • Ishizaki, T.1    Chiba, H.2    Kojima, T.3    Fujibe, M.4    Soma, T.5    Miyajima, H.6    Nagasawa, K.7    Wada, I.8    Sawada, N.9
  • 18
    • 0030572716 scopus 로고    scopus 로고
    • Differential response in the release of hydrogen peroxide between astroglial cells and endothelial cells following hypoxia/reoxygenation
    • Kondo T., Kinouchi H., Kawase M., and Yoshimoto T. Differential response in the release of hydrogen peroxide between astroglial cells and endothelial cells following hypoxia/reoxygenation. Neurosci. Lett. 215 (1996) 103-106
    • (1996) Neurosci. Lett. , vol.215 , pp. 103-106
    • Kondo, T.1    Kinouchi, H.2    Kawase, M.3    Yoshimoto, T.4
  • 20
    • 0242609993 scopus 로고    scopus 로고
    • Interactions between p38 mitogen-activated protein kinase and caspase-3 in cerebral endothelial cell death after hypoxia-reoxygenation
    • Lee S.R., and Lo E.H. Interactions between p38 mitogen-activated protein kinase and caspase-3 in cerebral endothelial cell death after hypoxia-reoxygenation. Stroke 34 (2003) 2704-2709
    • (2003) Stroke , vol.34 , pp. 2704-2709
    • Lee, S.R.1    Lo, E.H.2
  • 21
    • 77449093031 scopus 로고    scopus 로고
    • Altered distribution of tight junction proteins after intestinal ischemia/reperfusion injury in rats
    • Li Q., Zhang Q., Wang C., Liu X., Qu L., Gu L., Li N., and Li J. Altered distribution of tight junction proteins after intestinal ischemia/reperfusion injury in rats. J. Cell. Mol. Med. 13 (2009) 4061-4076
    • (2009) J. Cell. Mol. Med. , vol.13 , pp. 4061-4076
    • Li, Q.1    Zhang, Q.2    Wang, C.3    Liu, X.4    Qu, L.5    Gu, L.6    Li, N.7    Li, J.8
  • 22
    • 58149326864 scopus 로고    scopus 로고
    • Normobaric hyperoxia attenuates early blood-brain barrier disruption by inhibiting MMP-9-mediated occludin degradation in focal cerebral ischemia
    • Liu W., Hendren J., Qin X.J., Shen J., and Liu K.J. Normobaric hyperoxia attenuates early blood-brain barrier disruption by inhibiting MMP-9-mediated occludin degradation in focal cerebral ischemia. J. Neurochem. 108 (2009) 811-820
    • (2009) J. Neurochem. , vol.108 , pp. 811-820
    • Liu, W.1    Hendren, J.2    Qin, X.J.3    Shen, J.4    Liu, K.J.5
  • 23
    • 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. Tyrosine phosphatase inhibition induces loss of blood-brain barrier integrity by matrix metalloproteinase-dependent and -independent pathways. Brain Res. 995 (2004) 184-196
    • (2004) Brain Res. , vol.995 , pp. 184-196
    • Lohmann, C.1    Krischke, M.2    Wegener, J.3    Galla, H.J.4
  • 26
    • 33747436236 scopus 로고    scopus 로고
    • Amyloid beta-peptide1-42 alters tight junction protein distribution and expression in brain microvessel endothelial cells
    • Marco S., and Skaper S.D. Amyloid beta-peptide1-42 alters tight junction protein distribution and expression in brain microvessel endothelial cells. Neurosci. Lett. 401 3 (2006) 219-224
    • (2006) Neurosci. Lett. , vol.401 , Issue.3 , pp. 219-224
    • Marco, S.1    Skaper, S.D.2
  • 27
    • 14844299760 scopus 로고    scopus 로고
    • Hypoxia-enhanced expression of the proprotein convertase furin is mediated by hypoxia-inducible factor-1: impact on the bioactivation of proproteins
    • McMahon S., Grondin F., McDonald P.P., Richard D.E., and Dubois C.M. Hypoxia-enhanced expression of the proprotein convertase furin is mediated by hypoxia-inducible factor-1: impact on the bioactivation of proproteins. J. Biol. Chem. 280 (2005) 6561-6569
    • (2005) J. Biol. Chem. , vol.280 , pp. 6561-6569
    • McMahon, S.1    Grondin, F.2    McDonald, P.P.3    Richard, D.E.4    Dubois, C.M.5
  • 28
    • 33845656103 scopus 로고    scopus 로고
    • A neurovascular niche for neurogenesis after stroke
    • Ohab J.J., Fleming S., Blesch A., and Carmichael S.T. A neurovascular niche for neurogenesis after stroke. J. Neurosci. 26 (2006) 13007-13016
    • (2006) J. Neurosci. , vol.26 , pp. 13007-13016
    • Ohab, J.J.1    Fleming, S.2    Blesch, A.3    Carmichael, S.T.4
  • 29
    • 66149102423 scopus 로고    scopus 로고
    • Mechanisms of endothelial dysfunction, injury, and death
    • Pober J.S., Min W., and Bradley J.R. Mechanisms of endothelial dysfunction, injury, and death. Annu. Rev. Pathol. 4 (2009) 71-95
    • (2009) Annu. Rev. Pathol. , vol.4 , pp. 71-95
    • Pober, J.S.1    Min, W.2    Bradley, J.R.3
  • 30
    • 33845665284 scopus 로고    scopus 로고
    • Diapedesis of monocytes is associated with MMP-mediated occludin disappearance in brain endothelial cells
    • Reijerkerk A., Kooij G., van der Pol S.M., Khazen S., Dijkstra C.D., and de Vries H.E. Diapedesis of monocytes is associated with MMP-mediated occludin disappearance in brain endothelial cells. FASEB J. 20 (2006) 2550-2552
    • (2006) FASEB J. , vol.20 , pp. 2550-2552
    • Reijerkerk, A.1    Kooij, G.2    van der Pol, S.M.3    Khazen, S.4    Dijkstra, C.D.5    de Vries, H.E.6
  • 31
    • 0028825270 scopus 로고
    • Matrix metalloproteinases in brain injury
    • Rosenberg G.A. Matrix metalloproteinases in brain injury. J. Neurotrauma 12 (1995) 833-842
    • (1995) J. Neurotrauma , vol.12 , pp. 833-842
    • Rosenberg, G.A.1
  • 32
    • 0031693557 scopus 로고    scopus 로고
    • Matrix metalloproteinases and TIMPs are associated with blood-brain barrier opening after reperfusion in rat brain
    • Rosenberg G.A., Estrada E.Y., and Dencoff J.E. Matrix metalloproteinases and TIMPs are associated with blood-brain barrier opening after reperfusion in rat brain. Stroke 29 (1998) 2189-2195
    • (1998) Stroke , vol.29 , pp. 2189-2195
    • Rosenberg, G.A.1    Estrada, E.Y.2    Dencoff, J.E.3
  • 33
    • 34547793659 scopus 로고    scopus 로고
    • Vasogenic edema due to tight junction disruption by matrix metalloproteinases in cerebral ischemia
    • Rosenberg G.A., and Yang Y. Vasogenic edema due to tight junction disruption by matrix metalloproteinases in cerebral ischemia. Neurosurg. Focus 22 (2007) E4
    • (2007) Neurosurg. Focus , vol.22
    • Rosenberg, G.A.1    Yang, Y.2
  • 34
    • 0030982357 scopus 로고    scopus 로고
    • Possible involvement of phosphorylation of occludin in tight junction formation
    • Sakakibara A., Furuse M., Saitou M., Ando-Akatsuka Y., and Tsukita S. Possible involvement of phosphorylation of occludin in tight junction formation. J. Cell Biol. 137 (1997) 1393-1401
    • (1997) J. Cell Biol. , vol.137 , pp. 1393-1401
    • Sakakibara, A.1    Furuse, M.2    Saitou, M.3    Ando-Akatsuka, Y.4    Tsukita, S.5
  • 36
    • 0025227858 scopus 로고
    • Cleavage specificity of human skin type IV collagenase (gelatinase). Identification of cleavage sites in type I gelatin, with confirmation using synthetic peptides
    • Seltzer J.L., Akers K.T., Weingarten H., Grant G.A., McCourt D.W., and Eisen A.Z. Cleavage specificity of human skin type IV collagenase (gelatinase). Identification of cleavage sites in type I gelatin, with confirmation using synthetic peptides. J. Biol. Chem. 265 (1990) 20409-20413
    • (1990) J. Biol. Chem. , vol.265 , pp. 20409-20413
    • Seltzer, J.L.1    Akers, K.T.2    Weingarten, H.3    Grant, G.A.4    McCourt, D.W.5    Eisen, A.Z.6
  • 37
    • 62549153549 scopus 로고    scopus 로고
    • Cyclin-dependent kinase-5 targeting for ischaemic stroke
    • Slevin M., and Krupinski J. Cyclin-dependent kinase-5 targeting for ischaemic stroke. Curr. Opin. Pharmacol. 9 (2009) 119-124
    • (2009) Curr. Opin. Pharmacol. , vol.9 , pp. 119-124
    • Slevin, M.1    Krupinski, J.2
  • 38
    • 67650511699 scopus 로고    scopus 로고
    • Caveolae-mediated internalization of occludin and claudin-5 during CCL2-induced tight junction remodeling in brain endothelial cells
    • Stamatovic S.M., Keep R.F., Wang M.M., Jankovic I., and Andjelkovic A.V. Caveolae-mediated internalization of occludin and claudin-5 during CCL2-induced tight junction remodeling in brain endothelial cells. J. Biol. Chem. 284 28 (2009) 19053-19066
    • (2009) J. Biol. Chem. , vol.284 , Issue.28 , pp. 19053-19066
    • Stamatovic, S.M.1    Keep, R.F.2    Wang, M.M.3    Jankovic, I.4    Andjelkovic, A.V.5
  • 39
    • 0035188727 scopus 로고    scopus 로고
    • How matrix metalloproteinases regulate cell behavior
    • Sternlicht M.D., and Werb Z. How matrix metalloproteinases regulate cell behavior. Annu. Rev. Cell Dev. Biol. 17 (2001) 463-516
    • (2001) Annu. Rev. Cell Dev. Biol. , vol.17 , pp. 463-516
    • Sternlicht, M.D.1    Werb, Z.2
  • 43
    • 67149108182 scopus 로고    scopus 로고
    • Inhibition of Src activity decreases tyrosine phosphorylation of occludin in brain capillaries and attenuates increase in permeability of the blood-brain barrier after transient focal cerebral ischemia
    • Takenaga Y., Takagi N., Murotomi K., Tanonaka K., and Takeo S. Inhibition of Src activity decreases tyrosine phosphorylation of occludin in brain capillaries and attenuates increase in permeability of the blood-brain barrier after transient focal cerebral ischemia. J. Cereb. Blood Flow Metab. 29 (2009) 1099-1108
    • (2009) J. Cereb. Blood Flow Metab. , vol.29 , pp. 1099-1108
    • Takenaga, Y.1    Takagi, N.2    Murotomi, K.3    Tanonaka, K.4    Takeo, S.5
  • 44
    • 0033168966 scopus 로고    scopus 로고
    • Occludin and claudins in tight-junction strands: leading or supporting players?
    • Tsukita S., and Furuse M. Occludin and claudins in tight-junction strands: leading or supporting players?. Trends Cell Biol. 9 (1999) 268-273
    • (1999) Trends Cell Biol. , vol.9 , pp. 268-273
    • Tsukita, S.1    Furuse, M.2
  • 46
    • 39749086955 scopus 로고    scopus 로고
    • Endothelial cell aging and apoptosis in prevention and disease: E-selectin expression and modulation as a model
    • Vannini N., Pfeffer U., Lorusso G., Noonan D.M., and Albini A. Endothelial cell aging and apoptosis in prevention and disease: E-selectin expression and modulation as a model. Curr. Pharm. Des. 14 (2008) 221-225
    • (2008) Curr. Pharm. Des. , vol.14 , pp. 221-225
    • Vannini, N.1    Pfeffer, U.2    Lorusso, G.3    Noonan, D.M.4    Albini, A.5
  • 47
    • 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. Occludin proteolysis and increased permeability in endothelial cells through tyrosine phosphatase inhibition. J. Cell Sci. 112 Pt 23 (1999) 4347-4356
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 23 , pp. 4347-4356
    • Wachtel, M.1    Frei, K.2    Ehler, E.3    Fontana, A.4    Winterhalter, K.5    Gloor, S.M.6
  • 48
    • 48249105125 scopus 로고    scopus 로고
    • Targeting extracellular matrix proteolysis for hemorrhagic complications of tPA stroke therapy
    • Wang X., Rosell A., and Lo E.H. Targeting extracellular matrix proteolysis for hemorrhagic complications of tPA stroke therapy. CNS Neurol. Disord. Drug Targets 7 (2008) 235-242
    • (2008) CNS Neurol. Disord. Drug Targets , vol.7 , pp. 235-242
    • Wang, X.1    Rosell, A.2    Lo, E.H.3
  • 49
    • 0031884257 scopus 로고    scopus 로고
    • Overexpression of human glutathione peroxidase protects transgenic mice against focal cerebral ischemia/reperfusion damage
    • Weisbrot-Lefkowitz M., Reuhl K., Perry B., Chan P.H., Inouye M., and Mirochnitchenko O. Overexpression of human glutathione peroxidase protects transgenic mice against focal cerebral ischemia/reperfusion damage. Brain Res. Mol. Brain Res. 53 (1998) 333-338
    • (1998) Brain Res. Mol. Brain Res. , vol.53 , pp. 333-338
    • Weisbrot-Lefkowitz, M.1    Reuhl, K.2    Perry, B.3    Chan, P.H.4    Inouye, M.5    Mirochnitchenko, O.6
  • 50
    • 37249084760 scopus 로고    scopus 로고
    • Reoxygenation stress on blood-brain barrier paracellular permeability and edema in the rat
    • Witt K.A., Mark K.S., Sandoval K.E., and Davis T.P. Reoxygenation stress on blood-brain barrier paracellular permeability and edema in the rat. Microvasc. Res. 75 (2008) 91-96
    • (2008) Microvasc. Res. , vol.75 , pp. 91-96
    • Witt, K.A.1    Mark, K.S.2    Sandoval, K.E.3    Davis, T.P.4
  • 52
    • 33947493391 scopus 로고    scopus 로고
    • Matrix metalloproteinase-mediated disruption of tight junction proteins in cerebral vessels is reversed by synthetic matrix metalloproteinase inhibitor in focal ischemia in rat
    • Yang Y., Estrada E.Y., Thompson J.F., Liu W., and Rosenberg G.A. Matrix metalloproteinase-mediated disruption of tight junction proteins in cerebral vessels is reversed by synthetic matrix metalloproteinase inhibitor in focal ischemia in rat. J. Cereb. Blood Flow Metab. 27 (2007) 697-709
    • (2007) J. Cereb. Blood Flow Metab. , vol.27 , pp. 697-709
    • Yang, Y.1    Estrada, E.Y.2    Thompson, J.F.3    Liu, W.4    Rosenberg, G.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.