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Volumn 1623, Issue , 2015, Pages 39-52

Targeting transporters: Promoting blood-brain barrier repair in response to oxidative stress injury

Author keywords

Bloodbrain barrier; Endothelial cell; Membrane transporter; Multidrug resistance proteins; Organic anion transporting polypeptides; Oxidative stress

Indexed keywords

ABC TRANSPORTER; CARRIER PROTEIN; GLUTATHIONE; SOLUTE CARRIER TRANSPORTER; TIGHT JUNCTION PROTEIN; UNCLASSIFIED DRUG;

EID: 84941316599     PISSN: 00068993     EISSN: 18726240     Source Type: Journal    
DOI: 10.1016/j.brainres.2015.03.018     Document Type: Review
Times cited : (55)

References (170)
  • 2
    • 0036891988 scopus 로고    scopus 로고
    • Nicotine and cotinine modulate cerebral microvascular permeability and protein expression of ZO-1 through nicotinic acetylcholine receptors expressed on brain endothelial cells
    • T.J. Abbruscato, S.P. Lopez, K.S. Mark, B.T. Hawkins, and T.P. Davis Nicotine and cotinine modulate cerebral microvascular permeability and protein expression of ZO-1 through nicotinic acetylcholine receptors expressed on brain endothelial cells J. Pharm. Sci. 91 2002 2525 2538
    • (2002) J. Pharm. Sci. , vol.91 , pp. 2525-2538
    • Abbruscato, T.J.1    Lopez, S.P.2    Mark, K.S.3    Hawkins, B.T.4    Davis, T.P.5
  • 3
    • 78650785470 scopus 로고    scopus 로고
    • The role of the breast cancer resistance protein (ABCG2) in the distribution of sorafenib to the brain
    • S. Agarwal, R. Sane, J.R. Ohlfest, and W.F. Elmquist The role of the breast cancer resistance protein (ABCG2) in the distribution of sorafenib to the brain J. Pharmacol. Exp. Ther. 336 2011 223 233
    • (2011) J. Pharmacol. Exp. Ther. , vol.336 , pp. 223-233
    • Agarwal, S.1    Sane, R.2    Ohlfest, J.R.3    Elmquist, W.F.4
  • 5
    • 80052256102 scopus 로고    scopus 로고
    • Targeting the Nrf2-Keap1 antioxidant defence pathway for neurovascular protection in stroke
    • A. Alfieri, S. Srivastava, R.C.M. Siow, M. Modo, P.A. Fraser, and G.E. Mann Targeting the Nrf2-Keap1 antioxidant defence pathway for neurovascular protection in stroke J. Physiol. 58 2011 4125 4136
    • (2011) J. Physiol. , vol.58 , pp. 4125-4136
    • Alfieri, A.1    Srivastava, S.2    Siow, R.C.M.3    Modo, M.4    Fraser, P.A.5    Mann, G.E.6
  • 6
    • 65049090568 scopus 로고    scopus 로고
    • Plasma membrane glutathione transporters and their roles in cell physiology and pathophysiology
    • N. Ballatori, S.M. Krance, R. Marchan, and C.L. Hammond Plasma membrane glutathione transporters and their roles in cell physiology and pathophysiology Mol. Asp. Med. 30 2009 13 28
    • (2009) Mol. ASP. Med. , vol.30 , pp. 13-28
    • Ballatori, N.1    Krance, S.M.2    Marchan, R.3    Hammond, C.L.4
  • 7
    • 45749127384 scopus 로고    scopus 로고
    • Identification of regions required for apical membrane localization of human multidrug resistance protein 2
    • P.E. Bandler, C.J. Westlake, C.E. Grant, S.P. Cole, and R.G. Deeley Identification of regions required for apical membrane localization of human multidrug resistance protein 2 Mol. Pharmacol. 74 2008 9 19
    • (2008) Mol. Pharmacol. , vol.74 , pp. 9-19
    • Bandler, P.E.1    Westlake, C.J.2    Grant, C.E.3    Cole, S.P.4    Deeley, R.G.5
  • 8
    • 79751532850 scopus 로고    scopus 로고
    • Long-term high-dose atorvastatin decreases brain oxidative and nitrosative stress in a preclinical model of Alzheimer disease: A novel mechanism of action
    • E. Barone, G. Cenini, F. Di Domenico, S. Martin, R. Sultana, C. Mancuso, M.P. Murphy, E. Head, and D.A. Butterfield Long-term high-dose atorvastatin decreases brain oxidative and nitrosative stress in a preclinical model of Alzheimer disease: a novel mechanism of action Pharmacol. Res. 63 2011 172 180
    • (2011) Pharmacol. Res. , vol.63 , pp. 172-180
    • Barone, E.1    Cenini, G.2    Di Domenico, F.3    Martin, S.4    Sultana, R.5    Mancuso, C.6    Murphy, M.P.7    Head, E.8    Butterfield, D.A.9
  • 9
    • 44349163325 scopus 로고    scopus 로고
    • Coordinated nuclear receptor regulation of the efflux transporter, Mrp2, and the phase-II metabolizing enzyme, GSTpi, at the blood-brain barrier
    • B. Bauer, A.M. Hartz, J.R. Lucking, X. Yang, G.M. Pollack, and D.S. Miller Coordinated nuclear receptor regulation of the efflux transporter, Mrp2, and the phase-II metabolizing enzyme, GSTpi, at the blood-brain barrier J. Cereb. Blood Flow Metab. 28 2008 1222 1234
    • (2008) J. Cereb. Blood Flow Metab. , vol.28 , pp. 1222-1234
    • Bauer, B.1    Hartz, A.M.2    Lucking, J.R.3    Yang, X.4    Pollack, G.M.5    Miller, D.S.6
  • 10
    • 84920568095 scopus 로고    scopus 로고
    • "you shall not pass"-tight junctions of the blood brain barrier
    • H.C. Bauer, I.A. Krizbal, H. Bauer, and A. Traweger "You shall not pass"-tight junctions of the blood brain barrier Front. Neurosci. 8 2014 392
    • (2014) Front. Neurosci. , vol.8 , pp. 392
    • Bauer, H.C.1    Krizbal, I.A.2    Bauer, H.3    Traweger, A.4
  • 11
    • 0030823912 scopus 로고    scopus 로고
    • P-glycoprotein is strongly expressed in the luminal membranes of the endothelium of blood vessels in the brain
    • E. Beaulieu, M. Demeule, L. Ghitescu, and R. Beliveau P-glycoprotein is strongly expressed in the luminal membranes of the endothelium of blood vessels in the brain Biochem. J. 326 1997 539 544
    • (1997) Biochem. J. , vol.326 , pp. 539-544
    • Beaulieu, E.1    Demeule, M.2    Ghitescu, L.3    Beliveau, R.4
  • 13
    • 0347986547 scopus 로고    scopus 로고
    • The tight junction protein ZO-2 associates with Jun, Fos and C/EBP transcription factors in epithelial cells
    • A. Betanzos, M. Huerta, E. Lopez-Bayghen, E. Azuara, J. Amerena, and L. Gonzalez-Mariscal The tight junction protein ZO-2 associates with Jun, Fos and C/EBP transcription factors in epithelial cells Exp. Cell Res. 292 2004 51 66
    • (2004) Exp. Cell Res. , vol.292 , pp. 51-66
    • Betanzos, A.1    Huerta, M.2    Lopez-Bayghen, E.3    Azuara, E.4    Amerena, J.5    Gonzalez-Mariscal, L.6
  • 15
    • 12444249974 scopus 로고    scopus 로고
    • Hypoxia/aglycemia alters expression of occludin and actin in brain endothelial cells
    • R.C. Brown, and T.P. Davis Hypoxia/aglycemia alters expression of occludin and actin in brain endothelial cells Biochem. Biophys. Res. Commun. 327 2005 1114 1123
    • (2005) Biochem. Biophys. Res. Commun. , vol.327 , pp. 1114-1123
    • Brown, R.C.1    Davis, T.P.2
  • 16
    • 0025048342 scopus 로고
    • Electrical resistance across the blood-brain barrier in anaesthetized rats: A developmental study
    • A.M. Butt, H.C. Jones, and N.J. Abbott Electrical resistance across the blood-brain barrier in anaesthetized rats: a developmental study J. Physiol. 429 1990 47 62
    • (1990) J. Physiol. , vol.429 , pp. 47-62
    • Butt, A.M.1    Jones, H.C.2    Abbott, N.J.3
  • 17
    • 79959953827 scopus 로고    scopus 로고
    • Cholesterol-independent neuroprotective and neurotoxic activities of statins: Perspectives for statin use in Alzheimer disease and other age-related neurodegenerative disorders
    • D.A. Butterfield, E. Barone, and C. Mancuso Cholesterol-independent neuroprotective and neurotoxic activities of statins: perspectives for statin use in Alzheimer disease and other age-related neurodegenerative disorders Pharmacol. Res. 64 2011 180 186
    • (2011) Pharmacol. Res. , vol.64 , pp. 180-186
    • Butterfield, D.A.1    Barone, E.2    Mancuso, C.3
  • 18
    • 84874665034 scopus 로고    scopus 로고
    • Mrp1 is essential for sphingolipid signaling to p-glycoprotein in mouse blood-brain and blood-spinal cord barriers
    • T.A. Cartwright, C.R. Campos, R.E. Cannon, and D.S. Miller Mrp1 is essential for sphingolipid signaling to p-glycoprotein in mouse blood-brain and blood-spinal cord barriers J. Cereb. Blood Flow Metab. 33 2013 381 388
    • (2013) J. Cereb. Blood Flow Metab. , vol.33 , pp. 381-388
    • Cartwright, T.A.1    Campos, C.R.2    Cannon, R.E.3    Miller, D.S.4
  • 19
    • 38549136148 scopus 로고    scopus 로고
    • Blood-brain barrier genomics and cloning of a novel organic anion transporter
    • C. Chu, J.Y. Li, R.J. Boado, and W.M. Pardridge Blood-brain barrier genomics and cloning of a novel organic anion transporter J. Cereb. Blood Flow Metab. 28 2008 291 301
    • (2008) J. Cereb. Blood Flow Metab. , vol.28 , pp. 291-301
    • Chu, C.1    Li, J.Y.2    Boado, R.J.3    Pardridge, W.M.4
  • 20
    • 2542501568 scopus 로고    scopus 로고
    • Transcellular transport as a mechanism of blood-brain barrier disruption during stroke
    • M.J. Cipolla, R. Crete, L. Vitullo, and R.D. Rix Transcellular transport as a mechanism of blood-brain barrier disruption during stroke Front. Biosci. 9 2004 777 785
    • (2004) Front. Biosci. , vol.9 , pp. 777-785
    • Cipolla, M.J.1    Crete, R.2    Vitullo, L.3    Rix, R.D.4
  • 21
    • 77949913306 scopus 로고    scopus 로고
    • Neuroprotection of early and short-time applying atorvastatin in the acute phase of cerebral ischemia: Down-regulated 12/15-LOX, p38MAPK and cPLA2 expression, ameliorated BBB permeability
    • L. Cui, X. Zhang, R. Yang, L. Wang, L. Liu, M. Li, and W. Du Neuroprotection of early and short-time applying atorvastatin in the acute phase of cerebral ischemia: down-regulated 12/15-LOX, p38MAPK and cPLA2 expression, ameliorated BBB permeability Brain Res. 1325 2010 164 173
    • (2010) Brain Res. , vol.1325 , pp. 164-173
    • Cui, L.1    Zhang, X.2    Yang, R.3    Wang, L.4    Liu, L.5    Li, M.6    Du, W.7
  • 22
    • 33646754516 scopus 로고    scopus 로고
    • Multidrug resistance-associated proteins: Expression and function in the central nervous system
    • S. Dallas, D.S. Miller, and R. Bendayan Multidrug resistance-associated proteins: expression and function in the central nervous system Pharmacol. Rev. 58 2006 140 161
    • (2006) Pharmacol. Rev. , vol.58 , pp. 140-161
    • Dallas, S.1    Miller, D.S.2    Bendayan, R.3
  • 23
    • 35948984530 scopus 로고    scopus 로고
    • P-glycoprotein and breast cancer resistance protein: Two dominant transporters working together in limiting the brain penetration of topotecan
    • N.A. de Vries, J. Zhao, E. Kroon, T. Buckle, J.H. Beijnen, and O. van Tellingen P-glycoprotein and breast cancer resistance protein: two dominant transporters working together in limiting the brain penetration of topotecan Clin. Cancer Res. 13 2007 6440 6449
    • (2007) Clin. Cancer Res. , vol.13 , pp. 6440-6449
    • De Vries, N.A.1    Zhao, J.2    Kroon, E.3    Buckle, T.4    Beijnen, J.H.5    Van Tellingen, O.6
  • 24
    • 0033754531 scopus 로고    scopus 로고
    • The molecular organization of endothelial junctions and their functional role in vascular morphogenesis and permability
    • E. Dejana, M.G. Lampugnani, O. Martinez-Estrada, and G. Bazzoni The molecular organization of endothelial junctions and their functional role in vascular morphogenesis and permability Int. J. Dev. Biol. 44 2000 743 748
    • (2000) Int. J. Dev. Biol. , vol.44 , pp. 743-748
    • Dejana, E.1    Lampugnani, M.G.2    Martinez-Estrada, O.3    Bazzoni, G.4
  • 25
    • 0142104985 scopus 로고    scopus 로고
    • Smad-dependent and Smad-independent pathways in TGF-beta family signaling
    • R. Derynck, and Y.E. Zhang Smad-dependent and Smad-independent pathways in TGF-beta family signaling Nature 425 2003 577 584
    • (2003) Nature , vol.425 , pp. 577-584
    • Derynck, R.1    Zhang, Y.E.2
  • 27
    • 0032491391 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton
    • A.S. Fanning, B.J. Jameson, L.A. Jesaitis, and J.M. Anderson The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton J. Biol. Chem. 273 1998 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
  • 29
    • 0036354737 scopus 로고    scopus 로고
    • Hypoxia-induced hyperpermeability in brain microvessel endothelial cells involves VEGF-mediated changes in the expression of zonula occludens-1
    • S. Fischer, M. Wobben, H.H. Marti, D. Renz, and W. Schaper Hypoxia-induced hyperpermeability in brain microvessel endothelial cells involves VEGF-mediated changes in the expression of zonula occludens-1 Microvasc. Res. 63 2002 70 80
    • (2002) Microvasc. Res. , vol.63 , pp. 70-80
    • Fischer, S.1    Wobben, M.2    Marti, H.H.3    Renz, D.4    Schaper, W.5
  • 30
    • 45549102801 scopus 로고    scopus 로고
    • Differential effects of hydrocortisone and TNFalpha on tight junction proteins in an in vitro model of the human blood-brain barrier
    • C. Forster, M. Burek, I.A. Romero, B. Weksler, P.O. Couraud, and D. Drenckhahn Differential effects of hydrocortisone and TNFalpha on tight junction proteins in an in vitro model of the human blood-brain barrier J. Physiol. 586 2008 1937 1949
    • (2008) J. Physiol. , vol.586 , pp. 1937-1949
    • Forster, C.1    Burek, M.2    Romero, I.A.3    Weksler, B.4    Couraud, P.O.5    Drenckhahn, D.6
  • 32
    • 0033571047 scopus 로고    scopus 로고
    • Manner of interaction of heterogeneous claudin species within and between tight junction strands
    • M. Furuse, H. Sasaki, and S. Tsukita Manner of interaction of heterogeneous claudin species within and between tight junction strands J. Cell Biol. 147 1999 891 903
    • (1999) J. Cell Biol. , vol.147 , pp. 891-903
    • Furuse, M.1    Sasaki, H.2    Tsukita, S.3
  • 33
  • 34
    • 84901009773 scopus 로고    scopus 로고
    • Inhibition of Rho-kinase protects cerebral barrier from ischaemia-evoked injury through modulations of endothelial cell oxidative stress and tight junctions
    • C.L. Gibson, K. Srivastava, N. Sprigg, P.M. Bath, and U. Bayraktutan Inhibition of Rho-kinase protects cerebral barrier from ischaemia-evoked injury through modulations of endothelial cell oxidative stress and tight junctions J. Neurochem. 129 2014 816 826
    • (2014) J. Neurochem. , vol.129 , pp. 816-826
    • Gibson, C.L.1    Srivastava, K.2    Sprigg, N.3    Bath, P.M.4    Bayraktutan, U.5
  • 35
    • 0033585840 scopus 로고    scopus 로고
    • P-glycoprotein on astrocyte foot processes of unfized isolated human brain capillaries
    • P.L. Golden, and W.M. Pardridge P-glycoprotein on astrocyte foot processes of unfized isolated human brain capillaries Brain Res. 819 1999 143 146
    • (1999) Brain Res. , vol.819 , pp. 143-146
    • Golden, P.L.1    Pardridge, W.M.2
  • 37
    • 0029744106 scopus 로고    scopus 로고
    • The junction-associated protein, zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cellcell contacts
    • C.J. Gottardi, M. Arpin, A.S. Fanning, and D. Louvard The junction-associated protein, zonula occludens-1, localizes to the nucleus before the maturation and during the remodeling of cellcell contacts Proc. Natl. Acad. Sci. USA 93 1996 10779 10784
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 10779-10784
    • Gottardi, C.J.1    Arpin, M.2    Fanning, A.S.3    Louvard, D.4
  • 40
    • 1242272736 scopus 로고    scopus 로고
    • Organic anion transporting polypeptides of the OATP/ SLC21 family: Phylogenetic classification as OATP/ SLCO superfamily, new nomenclature and molecular/functional properties
    • B. Hagenbuch, and P.J. Meier Organic anion transporting polypeptides of the OATP/ SLC21 family: phylogenetic classification as OATP/ SLCO superfamily, new nomenclature and molecular/functional properties Pflugers Arch. 447 2004 653 665
    • (2004) Pflugers Arch. , vol.447 , pp. 653-665
    • Hagenbuch, B.1    Meier, P.J.2
  • 41
    • 78149477007 scopus 로고    scopus 로고
    • Regulation of ABC transportes at the blood-brain barrier: New targets for CNS therapy
    • A.M. Hartz, and B. Bauer Regulation of ABC transportes at the blood-brain barrier: new targets for CNS therapy Mol. Interv. 10 2010 293 304
    • (2010) Mol. Interv. , vol.10 , pp. 293-304
    • Hartz, A.M.1    Bauer, B.2
  • 43
    • 3342986458 scopus 로고    scopus 로고
    • Effect of lambda-carrageenan-induced inflammatory pain on brain uptake of codeine and antinociception
    • V.S. Hau, J.D. Huber, C.R. Campos, R.T. Davis, and T.P. Davis Effect of lambda-carrageenan-induced inflammatory pain on brain uptake of codeine and antinociception Brain Res. 1018 2004 257 264
    • (2004) Brain Res. , vol.1018 , pp. 257-264
    • Hau, V.S.1    Huber, J.D.2    Campos, C.R.3    Davis, R.T.4    Davis, T.P.5
  • 44
    • 5644226650 scopus 로고    scopus 로고
    • Nicotine increases in vivo blood-brain barrier permeability and alters cerebral microvascular tight junction protein distribution
    • B.T. Hawkins, T.J. Abbruscato, R.D. Egleton, R.C. Brown, J.D. Huber, C.R. Campos, and T.P. Davis Nicotine increases in vivo blood-brain barrier permeability and alters cerebral microvascular tight junction protein distribution Brain Res. 1027 2004 48 58
    • (2004) Brain Res. , vol.1027 , pp. 48-58
    • Hawkins, B.T.1    Abbruscato, T.J.2    Egleton, R.D.3    Brown, R.C.4    Huber, J.D.5    Campos, C.R.6    Davis, T.P.7
  • 45
    • 22944483792 scopus 로고    scopus 로고
    • The blood-brain barrier/neurovascular unit in health and disease
    • B.T. Hawkins, and T.P. Davis The blood-brain barrier/neurovascular unit in health and disease Pharmacol. Rev. 57 2005 173 185
    • (2005) Pharmacol. Rev. , vol.57 , pp. 173-185
    • Hawkins, B.T.1    Davis, T.P.2
  • 46
    • 33751017688 scopus 로고    scopus 로고
    • Decreased blood-brain barrier permeability to fluorescein in streptozotocin-treated rats
    • B.T. Hawkins, S.M. Ocheltree, K.M. Norwood, and R.D. Egleton Decreased blood-brain barrier permeability to fluorescein in streptozotocin-treated rats Neurosci. Lett. 411 2007 1 5
    • (2007) Neurosci. Lett. , vol.411 , pp. 1-5
    • Hawkins, B.T.1    Ocheltree, S.M.2    Norwood, K.M.3    Egleton, R.D.4
  • 47
    • 0141534255 scopus 로고    scopus 로고
    • Transcription factor Nrf2 is required for the constitutive and inducible expression of multidrug resistance-associated protein 1 in mouse embryo fibroblasts
    • A. Hayashi, H. Suzuki, K. Itoh, M. Yamamoto, and Y. Sugiyama Transcription factor Nrf2 is required for the constitutive and inducible expression of multidrug resistance-associated protein 1 in mouse embryo fibroblasts Biochem. Biophys. Res. Commun. 310 2003 824 829
    • (2003) Biochem. Biophys. Res. Commun. , vol.310 , pp. 824-829
    • Hayashi, A.1    Suzuki, H.2    Itoh, K.3    Yamamoto, M.4    Sugiyama, Y.5
  • 48
    • 19544376509 scopus 로고    scopus 로고
    • Free radicals as triggers of brain edema formation after stroke
    • J.H. Heo, S.W. Han, and S.K. Lee Free radicals as triggers of brain edema formation after stroke Free Radic. Biol. Med. 39 2005 51 70
    • (2005) Free Radic. Biol. Med. , vol.39 , pp. 51-70
    • Heo, J.H.1    Han, S.W.2    Lee, S.K.3
  • 49
    • 30144440842 scopus 로고    scopus 로고
    • Multidrug resistance protein 1-mediated export of glutathione and glutathione disulfide from brain astrocytes
    • J. Hirrlinger, and R. Dringen Multidrug resistance protein 1-mediated export of glutathione and glutathione disulfide from brain astrocytes Methods Enzymol. 400 2005 395 409
    • (2005) Methods Enzymol. , vol.400 , pp. 395-409
    • Hirrlinger, J.1    Dringen, R.2
  • 50
    • 0035145779 scopus 로고    scopus 로고
    • The multidrug resistance protein MRP1 mediates the release of glutathione disulfide from rat astrocytes during oxidative stress
    • J. Hirrlinger, J. Konig, D. Keppler, J. Lindenau, J.B. Schulz, and R. Dringen The multidrug resistance protein MRP1 mediates the release of glutathione disulfide from rat astrocytes during oxidative stress J. Neurochem. 76 2001 627 636
    • (2001) J. Neurochem. , vol.76 , pp. 627-636
    • Hirrlinger, J.1    Konig, J.2    Keppler, D.3    Lindenau, J.4    Schulz, J.B.5    Dringen, R.6
  • 51
    • 58549116078 scopus 로고    scopus 로고
    • Inflammatory mediators and blood brain barrier disruption in fatal brain edema of diabetic ketoacidosis
    • W.H. Hoffman, S.M. Stamatovic, and A.V. Andjelkovic Inflammatory mediators and blood brain barrier disruption in fatal brain edema of diabetic ketoacidosis Brain Res. 1254 2009 138 148
    • (2009) Brain Res. , vol.1254 , pp. 138-148
    • Hoffman, W.H.1    Stamatovic, S.M.2    Andjelkovic, A.V.3
  • 52
    • 33746925983 scopus 로고    scopus 로고
    • Up-regulation of P-glycoprotein expression by glutathione depletion-induced oxidative stress in rat brain microvessel endothelial cells
    • H. Hong, Y. Lu, Z.N. Ji, and G.Q. Liu Up-regulation of P-glycoprotein expression by glutathione depletion-induced oxidative stress in rat brain microvessel endothelial cells J. Neurochem. 98 2006 1465 1473
    • (2006) J. Neurochem. , vol.98 , pp. 1465-1473
    • Hong, H.1    Lu, Y.2    Ji, Z.N.3    Liu, G.Q.4
  • 53
    • 3342996554 scopus 로고    scopus 로고
    • Functional expression of rat ABCG2 on the luminal side of brain capillaries and its enhancement by astrocyte-derived soluble factor(s)
    • S. Hori, S. Ohtsuki, M. Tachikawa, N. Kimura, T. Kondo, M. Watanabe, E. Nakashima, and T. Terasaki Functional expression of rat ABCG2 on the luminal side of brain capillaries and its enhancement by astrocyte-derived soluble factor(s) J. Neurochem. 90 2004 526 536
    • (2004) J. Neurochem. , vol.90 , pp. 526-536
    • Hori, S.1    Ohtsuki, S.2    Tachikawa, M.3    Kimura, N.4    Kondo, T.5    Watanabe, M.6    Nakashima, E.7    Terasaki, T.8
  • 55
    • 84906083466 scopus 로고    scopus 로고
    • Hypoxia induces FoxO3-mediated dysfunction of blood-brain barrier
    • S.W. Hyun, and Y.S. Jung Hypoxia induces FoxO3-mediated dysfunction of blood-brain barrier Biochem. Biophys. Res. Commun. 450 2014 1638 1642
    • (2014) Biochem. Biophys. Res. Commun. , vol.450 , pp. 1638-1642
    • Hyun, S.W.1    Jung, Y.S.2
  • 56
    • 79955922988 scopus 로고    scopus 로고
    • Specific role of tight junction proteins claudin-5, occludin, and ZO-1 of the blood-brain barrier in a focal cerebral ischemic insult
    • H. Jiao, Z. Wang, Y. Liu, P. Wang, and Y. Xue Specific role of tight junction proteins claudin-5, occludin, and ZO-1 of the blood-brain barrier in a focal cerebral ischemic insult J. Mol. Neurosci. 44 2011 130 139
    • (2011) J. Mol. Neurosci. , vol.44 , pp. 130-139
    • Jiao, H.1    Wang, Z.2    Liu, Y.3    Wang, P.4    Xue, Y.5
  • 58
    • 77649180644 scopus 로고    scopus 로고
    • In vitro antioxidant activity of pravastatin provides vascular protection
    • M. Kassan, M.J. Montero, and M.A. Sevilla In vitro antioxidant activity of pravastatin provides vascular protection Eur. J. Pharmacol. 630 2010 107 111
    • (2010) Eur. J. Pharmacol. , vol.630 , pp. 107-111
    • Kassan, M.1    Montero, M.J.2    Sevilla, M.A.3
  • 59
    • 24344454692 scopus 로고    scopus 로고
    • Poly(ADP-ribosyl)ation by PARP-1: PAR-laying NAD+ into a nuclear signal
    • M.Y. Kim, T. Zhang, and W.L. Kraus Poly(ADP-ribosyl)ation by PARP-1: PAR-laying NAD+ into a nuclear signal Genes Dev. 19 2005 1951 1967
    • (2005) Genes Dev. , vol.19 , pp. 1951-1967
    • Kim, M.Y.1    Zhang, T.2    Kraus, W.L.3
  • 60
    • 33646376661 scopus 로고    scopus 로고
    • Effects of LPS stimulation on the expression of prostaglandin carriers in the cells of the blood-brain and blood-cerebrospinal fluid barriers
    • B. Kis, T. Isse, J.A. Snipes, L. Chen, H. Yamashita, Y. Ueta, and D.W. Busija Effects of LPS stimulation on the expression of prostaglandin carriers in the cells of the blood-brain and blood-cerebrospinal fluid barriers J. Appl. Physiol. 100 2006 1392 1399
    • (2006) J. Appl. Physiol. , vol.100 , pp. 1392-1399
    • Kis, B.1    Isse, T.2    Snipes, J.A.3    Chen, L.4    Yamashita, H.5    Ueta, Y.6    Busija, D.W.7
  • 61
    • 77952393660 scopus 로고    scopus 로고
    • Kinetic analysis of the cooperation of P-glycoprotein (P-gp/Abcb1) and breast cancer resistance protein (Bcrp/Abcg2) in limiting the brain and testis penetration of erlotinib, flavopiridol, and mitoxantrone
    • H. Kodaira, H. Kusuhara, J. Ushiki, E. Fuse, and Y. Sugiyama Kinetic analysis of the cooperation of P-glycoprotein (P-gp/Abcb1) and breast cancer resistance protein (Bcrp/Abcg2) in limiting the brain and testis penetration of erlotinib, flavopiridol, and mitoxantrone J. Pharmacol. Exp. Ther. 333 2010 788 796
    • (2010) J. Pharmacol. Exp. Ther. , vol.333 , pp. 788-796
    • Kodaira, H.1    Kusuhara, H.2    Ushiki, J.3    Fuse, E.4    Sugiyama, Y.5
  • 62
    • 12344261030 scopus 로고    scopus 로고
    • Active efflux across the blood-brain barrier: Role of the solute carrier family
    • H. Kusuhara, and Y. Sugiyama Active efflux across the blood-brain barrier: role of the solute carrier family NeuroRx 2 2005 73 85
    • (2005) NeuroRx , vol.2 , pp. 73-85
    • Kusuhara, H.1    Sugiyama, Y.2
  • 63
    • 0032922584 scopus 로고    scopus 로고
    • Small synthetic peptides homologous to segments of the first external loop of occludin impair tight junction resealing
    • F. Lacaz-Vieira, M.M. Jaeger, P. Farshori, and B. Kachar Small synthetic peptides homologous to segments of the first external loop of occludin impair tight junction resealing J. Membr. Biol. 168 1999 289 297
    • (1999) J. Membr. Biol. , vol.168 , pp. 289-297
    • Lacaz-Vieira, F.1    Jaeger, M.M.2    Farshori, P.3    Kachar, B.4
  • 64
    • 40949088574 scopus 로고    scopus 로고
    • The control of endothelial cell functions by adherens junctions
    • M.G. Lampugnani, and E. Dejana The control of endothelial cell functions by adherens junctions Novartis Found. Symp. 283 2007 4 13
    • (2007) Novartis Found. Symp. , vol.283 , pp. 4-13
    • Lampugnani, M.G.1    Dejana, E.2
  • 65
    • 34249879813 scopus 로고    scopus 로고
    • Expression of the ATP-binding cassette membrane transporter, ABCG2, in human and rodent brain microvessel endothelial and glial cell culture systems
    • G. Lee, K. Babakhanian, M. Ramaswamy, A. Prat, K. Wosik, and R. Bendayan Expression of the ATP-binding cassette membrane transporter, ABCG2, in human and rodent brain microvessel endothelial and glial cell culture systems Pharm. Res. 24 2007 1262 1274
    • (2007) Pharm. Res. , vol.24 , pp. 1262-1274
    • Lee, G.1    Babakhanian, K.2    Ramaswamy, M.3    Prat, A.4    Wosik, K.5    Bendayan, R.6
  • 66
    • 11844267237 scopus 로고    scopus 로고
    • Investigation of efflux transport of dehydroepiandrosterone sulfate and mitoxantrone at the mouse blood-brain barrier: A minor role of breast cancer resistance protein
    • Y.J. Lee, H. Kusuhara, J.W. Jonker, A.H. Schinkel, and Y. Sugiyama Investigation of efflux transport of dehydroepiandrosterone sulfate and mitoxantrone at the mouse blood-brain barrier: a minor role of breast cancer resistance protein J. Pharmacol. Exp. Ther. 312 2005 44 52
    • (2005) J. Pharmacol. Exp. Ther. , vol.312 , pp. 44-52
    • Lee, Y.J.1    Kusuhara, H.2    Jonker, J.W.3    Schinkel, A.H.4    Sugiyama, Y.5
  • 68
    • 84875867483 scopus 로고    scopus 로고
    • Transport of A1 adenosine receptor agonist tecadenoson by human and mouse nucleoside transporters: Evidence for blood-brain barrier transport by murine equilibrative nucleoside transporter 1 mENT1
    • E.I. Lepist, V.L. Damaraju, J. Zhang, W.P. Gati, S.Y. Yao, K.M. Smith, E. Karpinski, J.D. Young, K.H. Leung, and C.E. Cass Transport of A1 adenosine receptor agonist tecadenoson by human and mouse nucleoside transporters: evidence for blood-brain barrier transport by murine equilibrative nucleoside transporter 1 mENT1 Drug Metab. Dispos. 41 2013 916 922
    • (2013) Drug Metab. Dispos. , vol.41 , pp. 916-922
    • Lepist, E.I.1    Damaraju, V.L.2    Zhang, J.3    Gati, W.P.4    Yao, S.Y.5    Smith, K.M.6    Karpinski, E.7    Young, J.D.8    Leung, K.H.9    Cass, C.E.10
  • 69
    • 17544368685 scopus 로고    scopus 로고
    • Multidrug resistance proteins: Role of P-glycoprotein, MRP1, MRP2, and BCRP (ABCG2) in tissue defense
    • E.M. Leslie, R.G. Deeley, and S.P. Cole Multidrug resistance proteins: role of P-glycoprotein, MRP1, MRP2, and BCRP (ABCG2) in tissue defense Toxicol. Appl. Pharmacol. 204 2005 216 237
    • (2005) Toxicol. Appl. Pharmacol. , vol.204 , pp. 216-237
    • Leslie, E.M.1    Deeley, R.G.2    Cole, S.P.3
  • 70
    • 84905586728 scopus 로고    scopus 로고
    • Evaluation of the protective potential of brain microvascular endothelial cell autophagy on blood-brain barrier integrity during experimental cerebral ischemia-reperfusion injury
    • H. Li, A. Gao, D. Feng, Y. Wang, L. Zhang, Y. Cui, B. Li, Z. Wang, and G. Chen Evaluation of the protective potential of brain microvascular endothelial cell autophagy on blood-brain barrier integrity during experimental cerebral ischemia-reperfusion injury Transl. Stroke Res. 5 2014 618 626
    • (2014) Transl. Stroke Res. , vol.5 , pp. 618-626
    • Li, H.1    Gao, A.2    Feng, D.3    Wang, Y.4    Zhang, L.5    Cui, Y.6    Li, B.7    Wang, Z.8    Chen, G.9
  • 71
    • 84863715209 scopus 로고    scopus 로고
    • Glutathione in cerebral microvascular endothelial biology and pathobiology: Implications for brain homeostasis
    • W. Li, C. Busu, M.L. Circu, and T.Y. Aw Glutathione in cerebral microvascular endothelial biology and pathobiology: implications for brain homeostasis Int. J. Cell Biol. 2012 2012 434971
    • (2012) Int. J. Cell Biol. , vol.2012 , pp. 434971
    • Li, W.1    Busu, C.2    Circu, M.L.3    Aw, T.Y.4
  • 72
    • 77956247309 scopus 로고    scopus 로고
    • Oxidative stress increases blood-brain barrier permeability and induces alterations in occludin during hypoxia-reoxygenation
    • J.J. Lochhead, G. McCaffrey, C.E. Quigley, J. Finch, K.M. DeMarco, N. Nametz, and T.P. Davis Oxidative stress increases blood-brain barrier permeability and induces alterations in occludin during hypoxia-reoxygenation J. Cereb. Blood Flow Metab. 30 2010 1625 1636
    • (2010) J. Cereb. Blood Flow Metab. , vol.30 , pp. 1625-1636
    • Lochhead, J.J.1    McCaffrey, G.2    Quigley, C.E.3    Finch, J.4    DeMarco, K.M.5    Nametz, N.6    Davis, T.P.7
  • 74
    • 84867034260 scopus 로고    scopus 로고
    • Role of Nrf2 in oxidative stress and toxicity
    • Q. Ma Role of Nrf2 in oxidative stress and toxicity Annu. Rev. Pharmacol. Toxiciol. 53 2013 401 426
    • (2013) Annu. Rev. Pharmacol. Toxiciol. , vol.53 , pp. 401-426
    • Ma, Q.1
  • 76
    • 0036084919 scopus 로고    scopus 로고
    • Cerebral microvascular changes in permeability and tight junctions induced by hypoxia-reoxygenation
    • K.S. Mark, and T.P. Davis Cerebral microvascular changes in permeability and tight junctions induced by hypoxia-reoxygenation Am. J. Physiol. Heart Circ. Physiol. 282 2002 H1485 H1494
    • (2002) Am. J. Physiol. Heart Circ. Physiol. , vol.282 , pp. H1485-H1494
    • Mark, K.S.1    Davis, T.P.2
  • 79
    • 50849106047 scopus 로고    scopus 로고
    • Occludin oligomeric assembly at tight junctions of the blood-brain barrier is disrupted by peripheral inflammatory hyperalgesia
    • G. McCaffrey, M.J. Seelbach, W.D. Staatz, N. Nametz, C. Quigley, C.R. Campos, T.A. Brooks, and T.P. Davis Occludin oligomeric assembly at tight junctions of the blood-brain barrier is disrupted by peripheral inflammatory hyperalgesia J. Neurochem. 106 2008 2395 2409
    • (2008) J. Neurochem. , vol.106 , pp. 2395-2409
    • McCaffrey, G.1    Seelbach, M.J.2    Staatz, W.D.3    Nametz, N.4    Quigley, C.5    Campos, C.R.6    Brooks, T.A.7    Davis, T.P.8
  • 80
    • 77149179101 scopus 로고    scopus 로고
    • Adherens junction: Molecular architecture and regulation
    • W. Meng, and M. Takeichi Adherens junction: molecular architecture and regulation Cold Spring Harb. Perspect. Biol. 1 2009 a002899
    • (2009) Cold Spring Harb. Perspect. Biol. , vol.1 , pp. a002899
    • Meng, W.1    Takeichi, M.2
  • 81
    • 0033664346 scopus 로고    scopus 로고
    • Xenobiotic transport across isolated brain microvessels studied by confocal microscopy
    • D.S. Miller, S.N. Nobmann, H. Gutmann, M. Toeroek, J. Drewe, and G. Fricker Xenobiotic transport across isolated brain microvessels studied by confocal microscopy Mol. Pharmacol. 58 2000 1357 1367
    • (2000) Mol. Pharmacol. , vol.58 , pp. 1357-1367
    • Miller, D.S.1    Nobmann, S.N.2    Gutmann, H.3    Toeroek, M.4    Drewe, J.5    Fricker, G.6
  • 82
    • 33645304045 scopus 로고    scopus 로고
    • The multidrug resistance protein 1 (Mrp1), but not Mrp5, mediates export of glutathione and glutathione disulfide from brain astrocytes
    • T. Minich, J. Riemer, J.B. Schulz, P. Wielinga, J. Wijnholds, and R. Dringen The multidrug resistance protein 1 (Mrp1), but not Mrp5, mediates export of glutathione and glutathione disulfide from brain astrocytes J. Neurochem. 97 2006 373 384
    • (2006) J. Neurochem. , vol.97 , pp. 373-384
    • Minich, T.1    Riemer, J.2    Schulz, J.B.3    Wielinga, P.4    Wijnholds, J.5    Dringen, R.6
  • 83
    • 79954990740 scopus 로고    scopus 로고
    • Organic anion transporter 3 mediates the efflux transport of an amphipathic organic anion, dehydroepiandrosterone sulfate, across the blood-brain barrier in mice
    • M. Miyajima, H. Kusuhara, M. Fujishima, Y. Adachi, and Y. Sugiyama Organic anion transporter 3 mediates the efflux transport of an amphipathic organic anion, dehydroepiandrosterone sulfate, across the blood-brain barrier in mice Drug Metab. Dispos. 39 2011 814 819
    • (2011) Drug Metab. Dispos. , vol.39 , pp. 814-819
    • Miyajima, M.1    Kusuhara, H.2    Fujishima, M.3    Adachi, Y.4    Sugiyama, Y.5
  • 84
    • 0034577887 scopus 로고    scopus 로고
    • Glutathione homeostasis and leukotriene-induced permeability in human blood-brain barrier endothelial cells subjected to in vitro ischemia
    • A. Muruganandam, C. Smith, R. Ball, T. Herring, and D. Stanimirovic Glutathione homeostasis and leukotriene-induced permeability in human blood-brain barrier endothelial cells subjected to in vitro ischemia Acta Neurochir. Suppl. 76 2000 29 34
    • (2000) Acta Neurochir. Suppl. , vol.76 , pp. 29-34
    • Muruganandam, A.1    Smith, C.2    Ball, R.3    Herring, T.4    Stanimirovic, D.5
  • 85
    • 0035081376 scopus 로고    scopus 로고
    • Temporal profiles of the levels of endogenous antioxidants after four-vessel occlusion in rats
    • K. Namba, Y. Takeda, K. Sunami, and M. Hirakawa Temporal profiles of the levels of endogenous antioxidants after four-vessel occlusion in rats J. Neurosurg. Anesthesiol. 13 2001 131 137
    • (2001) J. Neurosurg. Anesthesiol. , vol.13 , pp. 131-137
    • Namba, K.1    Takeda, Y.2    Sunami, K.3    Hirakawa, M.4
  • 86
    • 52549132911 scopus 로고    scopus 로고
    • Role of the p38 mitogen-activated protein kinase/cytosolic phospholipase A2 signaling pathway in blood-brain barrier disruption after focal cerebral ischemia and reperfusion
    • C. Nito, H. Kamada, H. Endo, K. Niizuma, D.J. Myer, and P.H. Chan Role of the p38 mitogen-activated protein kinase/cytosolic phospholipase A2 signaling pathway in blood-brain barrier disruption after focal cerebral ischemia and reperfusion J. Cereb. Blood Flow Metab. 28 2008 1686 1696
    • (2008) J. Cereb. Blood Flow Metab. , vol.28 , pp. 1686-1696
    • Nito, C.1    Kamada, H.2    Endo, H.3    Niizuma, K.4    Myer, D.J.5    Chan, P.H.6
  • 87
    • 84872159164 scopus 로고    scopus 로고
    • Quantitative targeted absolute proteomic analysis of transporters and junction proteins for validation of human cerebral microvascular endothelial cell line hCMEC/D3 as a human blood-brain barrier model
    • S. Ohtsuki, C. Ikeda, Y. Uchida, Y. Sakamoto, F. Miller, F. Glacial, X. Decleves, J.M. Scherrmann, P.O. Couraud, Y. Kubo, M. Tachikawa, and T. Terasaki Quantitative targeted absolute proteomic analysis of transporters and junction proteins for validation of human cerebral microvascular endothelial cell line hCMEC/D3 as a human blood-brain barrier model Mol. Pharm. 10 2013 289 296
    • (2013) Mol. Pharm. , vol.10 , pp. 289-296
    • Ohtsuki, S.1    Ikeda, C.2    Uchida, Y.3    Sakamoto, Y.4    Miller, F.5    Glacial, F.6    Decleves, X.7    Scherrmann, J.M.8    Couraud, P.O.9    Kubo, Y.10    Tachikawa, M.11    Terasaki, T.12
  • 88
    • 0017487289 scopus 로고
    • The large apparent work capability of the blood-brain barrier: A study of the mitochondrial content of capillary endothelial cells in brain and other tissues of the rat
    • W.H. Oldendorf, M.E. Cornford, and W.J. Brown The large apparent work capability of the blood-brain barrier: a study of the mitochondrial content of capillary endothelial cells in brain and other tissues of the rat Ann. Neurol. 1 1977 409 417
    • (1977) Ann. Neurol. , vol.1 , pp. 409-417
    • Oldendorf, W.H.1    Cornford, M.E.2    Brown, W.J.3
  • 89
    • 59649111761 scopus 로고    scopus 로고
    • Limited brain distribution of [3R,4R,5S]-4-acetamido-5-amino-3-(1-ethylpropoxy)-1-cyclohexene-1-carboxylate phosphate (Ro 64-0802), a pharmacologically active form of oseltamivir, by active efflux across the blood-brain barrier mediated by organic anion transporter 3 (Oat3/Slc22a8) and multidrug resistance-associated protein 4 (Mrp4/Abcc4)
    • A. Ose, M. Ito, H. Kusuhara, K. Yamatsugu, M. Kanai, M. Shibasaki, M. Hosokawa, J.D. Schuetz, and Y. Sugiyama Limited brain distribution of [3R,4R,5S]-4-acetamido-5-amino-3-(1-ethylpropoxy)-1-cyclohexene-1-carboxylate phosphate (Ro 64-0802), a pharmacologically active form of oseltamivir, by active efflux across the blood-brain barrier mediated by organic anion transporter 3 (Oat3/Slc22a8) and multidrug resistance-associated protein 4 (Mrp4/Abcc4) Drug Metab. Dispos. 37 2009 315 321
    • (2009) Drug Metab. Dispos. , vol.37 , pp. 315-321
    • Ose, A.1    Ito, M.2    Kusuhara, H.3    Yamatsugu, K.4    Kanai, M.5    Shibasaki, M.6    Hosokawa, M.7    Schuetz, J.D.8    Sugiyama, Y.9
  • 90
    • 73149094513 scopus 로고    scopus 로고
    • Functional characterization of mouse organic anion transporting peptide 1a4 in the uptake and efflux of drugs across the blood-brain barrier
    • A. Ose, H. Kusuhara, C. Endo, K. Tohyama, M. Miyajima, S. Kitamura, and Y. Sugiyama Functional characterization of mouse organic anion transporting peptide 1a4 in the uptake and efflux of drugs across the blood-brain barrier Drug Metab. Dispos. 38 2010 168 176
    • (2010) Drug Metab. Dispos. , vol.38 , pp. 168-176
    • Ose, A.1    Kusuhara, H.2    Endo, C.3    Tohyama, K.4    Miyajima, M.5    Kitamura, S.6    Sugiyama, Y.7
  • 91
    • 33846863589 scopus 로고    scopus 로고
    • Nitric oxide and peroxynitrite in health and disease
    • P. Pacher, J.S. Beckman, and L. Liaudet Nitric oxide and peroxynitrite in health and disease Physiol. Rev. 87 2007 315 424
    • (2007) Physiol. Rev. , vol.87 , pp. 315-424
    • Pacher, P.1    Beckman, J.S.2    Liaudet, L.3
  • 92
    • 84860535245 scopus 로고    scopus 로고
    • Three decades of Pgp inhibitors: Skimming through several generations and scaffolds
    • A. Palmeira, E. Sousa, M.H. Vasconcelos, and M.M. Pinto Three decades of Pgp inhibitors: skimming through several generations and scaffolds Curr. Med. Chem. 19 2012 1946 2025
    • (2012) Curr. Med. Chem. , vol.19 , pp. 1946-2025
    • Palmeira, A.1    Sousa, E.2    Vasconcelos, M.H.3    Pinto, M.M.4
  • 93
    • 0033748201 scopus 로고    scopus 로고
    • Measurement of glutathione oxidation and 8-hydroxy-2′-deoxyguanosine accumulation in the gerbil hippocampus following global ischemia
    • E.M. Park, J.H. Choi, J.S. Park, M.Y. han, and Y.M. Park Measurement of glutathione oxidation and 8-hydroxy-2′-deoxyguanosine accumulation in the gerbil hippocampus following global ischemia Brain Res. Protoc. 6 2000 25 32
    • (2000) Brain Res. Protoc. , vol.6 , pp. 25-32
    • Park, E.M.1    Choi, J.H.2    Park, J.S.3    Han, M.Y.4    Park, Y.M.5
  • 94
    • 84896695953 scopus 로고    scopus 로고
    • Atorvastatin attenuates neuropathic pain in rat neuropathy model by down-regulating oxidative damage at peripheral, spinal and supraspinal levels
    • N.N. Pathak, V. Balaganur, M.C. Lingaraju, V. Kant, N. Latief, A.S. More, D. Kumar, D. Kumar, and S.K. Tandan Atorvastatin attenuates neuropathic pain in rat neuropathy model by down-regulating oxidative damage at peripheral, spinal and supraspinal levels Neurochem. Int. 68 2014 1 9
    • (2014) Neurochem. Int. , vol.68 , pp. 1-9
    • Pathak, N.N.1    Balaganur, V.2    Lingaraju, M.C.3    Kant, V.4    Latief, N.5    More, A.S.6    Kumar, D.7    Kumar, D.8    Tandan, S.K.9
  • 95
    • 0033104810 scopus 로고    scopus 로고
    • Canalicular multispecific organic transporter/multidrug resistance protein 2 mediates low-affinity transport of reduced glutathione
    • C.C. Paulusma, M.A. van Geer, R. Evers, M. Heijn, R. Ottenhoff, P. Borst, and R.P. Oude Elferink Canalicular multispecific organic transporter/multidrug resistance protein 2 mediates low-affinity transport of reduced glutathione Biochem. J. 338 1999 393 401
    • (1999) Biochem. J. , vol.338 , pp. 393-401
    • Paulusma, C.C.1    Van Geer, M.A.2    Evers, R.3    Heijn, M.4    Ottenhoff, R.5    Borst, P.6    Oude Elferink, R.P.7
  • 97
    • 0028822474 scopus 로고
    • Hypoxia increases the susceptibility to oxidant stress and the permeability of the blood-brain barrier endothelial cell monolayer
    • M. Plateel, M.P. Dehouck, G. Torpier, R. Cecchelli, and E. Tessier Hypoxia increases the susceptibility to oxidant stress and the permeability of the blood-brain barrier endothelial cell monolayer J. Neurochem. 65 1995 2138 2145
    • (1995) J. Neurochem. , vol.65 , pp. 2138-2145
    • Plateel, M.1    Dehouck, M.P.2    Torpier, G.3    Cecchelli, R.4    Tessier, E.5
  • 98
    • 41149132355 scopus 로고    scopus 로고
    • Simvastatin reduces the association of NMDA receptors to lipid rafts: A cholesterol-mediated effect in neuroprotection
    • J. Ponce, N.P. de la Ossa, O. Hurtado, M. Millan, J.F. Arenillas, A. Davalos, and T. Gasull Simvastatin reduces the association of NMDA receptors to lipid rafts: a cholesterol-mediated effect in neuroprotection Stroke 39 2008 1269 1275
    • (2008) Stroke , vol.39 , pp. 1269-1275
    • Ponce, J.1    De La Ossa, N.P.2    Hurtado, O.3    Millan, M.4    Arenillas, J.F.5    Davalos, A.6    Gasull, T.7
  • 99
    • 77955316820 scopus 로고    scopus 로고
    • Modulating P-glycoprotein regulation: Future perspectives for pharmacoresistant epilepsies?
    • H. Potschka Modulating P-glycoprotein regulation: future perspectives for pharmacoresistant epilepsies? Epilepsia 51 2010 1333 1347
    • (2010) Epilepsia , vol.51 , pp. 1333-1347
    • Potschka, H.1
  • 100
    • 80051728609 scopus 로고    scopus 로고
    • Molecular biology of the blood-brain and the blood-cerebrospinal fluid barriers: Similarities and differences
    • Z. Redzic Molecular biology of the blood-brain and the blood-cerebrospinal fluid barriers: similarities and differences Fluids Barriers CNS 8 2011 3
    • (2011) Fluids Barriers CNS , vol.8 , pp. 3
    • Redzic, Z.1
  • 103
    • 49349102757 scopus 로고    scopus 로고
    • Subcellular localization of transporters along the rat blood-brain barrier and blood-cerebral-spinal fluid barrier by in vivo biotinylation
    • L.M. Roberts, D.S. Black, C. Raman, K. Woodford, M. Zhou, J.E. Haggerty, A.T. Yan, S.E. Cwirla, and K.K. Grindstaff Subcellular localization of transporters along the rat blood-brain barrier and blood-cerebral-spinal fluid barrier by in vivo biotinylation Neuroscience 155 2008 423 438
    • (2008) Neuroscience , vol.155 , pp. 423-438
    • Roberts, L.M.1    Black, D.S.2    Raman, C.3    Woodford, K.4    Zhou, M.5    Haggerty, J.E.6    Yan, A.T.7    Cwirla, S.E.8    Grindstaff, K.K.9
  • 105
    • 84903751395 scopus 로고    scopus 로고
    • Downregulation of blood-brain barrier phenotype by proinflammatory cytokines involves NADPH oxidase-dependent ROS generation: Consequences for interendothelial adherens and tight junctions
    • K.D. Rochfort, L.E. Collins, R.P. Murphy, and P.M. Cummins Downregulation of blood-brain barrier phenotype by proinflammatory cytokines involves NADPH oxidase-dependent ROS generation: consequences for interendothelial adherens and tight junctions PLoS One 9 2014 e101815
    • (2014) PLoS One , vol.9 , pp. e101815
    • Rochfort, K.D.1    Collins, L.E.2    Murphy, R.P.3    Cummins, P.M.4
  • 106
    • 0030854715 scopus 로고    scopus 로고
    • Cellular energy utilization and molecular origin of standard metabolic rate in mammals
    • D.F. Rolfe, and G.C. Brown Cellular energy utilization and molecular origin of standard metabolic rate in mammals Physiol. Rev. 77 1997 731 758
    • (1997) Physiol. Rev. , vol.77 , pp. 731-758
    • Rolfe, D.F.1    Brown, G.C.2
  • 107
    • 48249151774 scopus 로고    scopus 로고
    • HIV-1 viral envelope glycoprotein gp120 produces oxidative stress and regulates the functional expression of multidrug resistance protein-1 (Mrp1) in glial cells
    • P.T. Ronaldson, and R. Bendayan HIV-1 viral envelope glycoprotein gp120 produces oxidative stress and regulates the functional expression of multidrug resistance protein-1 (Mrp1) in glial cells J. Neurochem. 106 2008 1298 1313
    • (2008) J. Neurochem. , vol.106 , pp. 1298-1313
    • Ronaldson, P.T.1    Bendayan, R.2
  • 108
    • 84866665561 scopus 로고    scopus 로고
    • Blood-brain barrier integrity and glial support: Mechanisms that can be targeted for novel therapeutic approaches in stroke
    • P.T. Ronaldson, and T.P. Davis Blood-brain barrier integrity and glial support: mechanisms that can be targeted for novel therapeutic approaches in stroke Curr. Pharm. Des. 18 2012 3624 3644
    • (2012) Curr. Pharm. Des. , vol.18 , pp. 3624-3644
    • Ronaldson, P.T.1    Davis, T.P.2
  • 109
    • 84878231468 scopus 로고    scopus 로고
    • Targeted drug delivery to treat pain and cerebral hypoxia
    • P.T. Ronaldson, and T.P. Davis Targeted drug delivery to treat pain and cerebral hypoxia Pharmacol. Rev. 65 2013 291 314
    • (2013) Pharmacol. Rev. , vol.65 , pp. 291-314
    • Ronaldson, P.T.1    Davis, T.P.2
  • 110
    • 67349173648 scopus 로고    scopus 로고
    • Transforming growth factor-beta signaling alters substrate permeability and tight junction protein expression at the blood-brain barrier during inflammatory pain
    • P.T. Ronaldson, K.M. DeMarco, L. Sanchez-Covarrubias, C.M. Solinsky, and T.P. Davis Transforming growth factor-beta signaling alters substrate permeability and tight junction protein expression at the blood-brain barrier during inflammatory pain J. Cereb. Blood Flow Metab. 29 2009 1084 1098
    • (2009) J. Cereb. Blood Flow Metab. , vol.29 , pp. 1084-1098
    • Ronaldson, P.T.1    DeMarco, K.M.2    Sanchez-Covarrubias, L.3    Solinsky, C.M.4    Davis, T.P.5
  • 111
    • 79952001112 scopus 로고    scopus 로고
    • Inflammatory pain signals an increase in functional expression of organic anion transporting polypeptide 1a4 at the blood-brain barrier
    • P.T. Ronaldson, J.D. Finch, K.M. DeMarco, C.E. Quigley, and T.P. Davis Inflammatory pain signals an increase in functional expression of organic anion transporting polypeptide 1a4 at the blood-brain barrier J. Pharmacol. Exp. Ther. 336 2011 827 839
    • (2011) J. Pharmacol. Exp. Ther. , vol.336 , pp. 827-839
    • Ronaldson, P.T.1    Finch, J.D.2    DeMarco, K.M.3    Quigley, C.E.4    Davis, T.P.5
  • 112
    • 62149143407 scopus 로고    scopus 로고
    • Regulation of ABC membrane transporters in glial cells: Relevance to the pharmacotherapy of brain HIV-1 infection
    • P.T. Ronaldson, Y. Persidsky, and R. Bendayan Regulation of ABC membrane transporters in glial cells: relevance to the pharmacotherapy of brain HIV-1 infection Glia 56 2008 1711 1735
    • (2008) Glia , vol.56 , pp. 1711-1735
    • Ronaldson, P.T.1    Persidsky, Y.2    Bendayan, R.3
  • 113
    • 33751288381 scopus 로고    scopus 로고
    • Superoxide, peroxynitrite and oxidative/nitrative stress in inflammation
    • D. Salvemini, T.M. Doyle, and S. Cuzzocrea Superoxide, peroxynitrite and oxidative/nitrative stress in inflammation Biochem. Soc. Trans. 34 2006 965 970
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 965-970
    • Salvemini, D.1    Doyle, T.M.2    Cuzzocrea, S.3
  • 116
    • 53749096762 scopus 로고    scopus 로고
    • Blood-brain barrier tight junction permeability and ischemic stroke
    • K.E. Sandoval, and K.A. Witt Blood-brain barrier tight junction permeability and ischemic stroke Neurobiol. Dis. 32 2008 200 219
    • (2008) Neurobiol. Dis. , vol.32 , pp. 200-219
    • Sandoval, K.E.1    Witt, K.A.2
  • 117
    • 1542548173 scopus 로고    scopus 로고
    • P-glycoprotein and caveolin-1alpha in endothelium and astrocytes of primate brain
    • F. Schlachetzki, and W.M. Pardridge P-glycoprotein and caveolin-1alpha in endothelium and astrocytes of primate brain Neuroreport 14 2003 2041 2046
    • (2003) Neuroreport , vol.14 , pp. 2041-2046
    • Schlachetzki, F.1    Pardridge, W.M.2
  • 119
    • 34547902120 scopus 로고    scopus 로고
    • Peripheral inflammatory hyperalgesia modulates morphine delivery to the brain: A role for P-glycoprotein
    • M.J. Seelbach, T.A. Brooks, R.D. Egleton, and T.P. Davis Peripheral inflammatory hyperalgesia modulates morphine delivery to the brain: a role for P-glycoprotein J. Neurochem. 102 2007 1677 1690
    • (2007) J. Neurochem. , vol.102 , pp. 1677-1690
    • Seelbach, M.J.1    Brooks, T.A.2    Egleton, R.D.3    Davis, T.P.4
  • 120
    • 84910680152 scopus 로고    scopus 로고
    • Inhibition of junctional adhesion molecule-A/LFA interaction attenuates leukocyte trafficking and inflammation in brain ischemia/reperfusion injury
    • N. Sladojevic, S.M. Stamatovic, R.F. Keep, J.J. Grailer, J.V. Sarma, P.A. Ward, and A.V. Andjelkovic Inhibition of junctional adhesion molecule-A/LFA interaction attenuates leukocyte trafficking and inflammation in brain ischemia/reperfusion injury Neurobiol. Dis. 67 2014 57 70
    • (2014) Neurobiol. Dis. , vol.67 , pp. 57-70
    • Sladojevic, N.1    Stamatovic, S.M.2    Keep, R.F.3    Grailer, J.J.4    Sarma, J.V.5    Ward, P.A.6    Andjelkovic, A.V.7
  • 122
    • 84877030960 scopus 로고    scopus 로고
    • Vascular oxidative stress and mitochondrial failure in the pathobiology of Alzheimers disease: A new approach to therapy
    • M. Sochocka, E.S. Koutsouraki, K. Gasiorowski, and J. Leszek Vascular oxidative stress and mitochondrial failure in the pathobiology of Alzheimers disease: a new approach to therapy CNS Neurol. Disord. Drug Targets 12 2013 870 881
    • (2013) CNS Neurol. Disord. Drug Targets , vol.12 , pp. 870-881
    • Sochocka, M.1    Koutsouraki, E.S.2    Gasiorowski, K.3    Leszek, J.4
  • 123
    • 84932168696 scopus 로고    scopus 로고
    • The heparan sulfate proteoglycan agrin contributes to barrier properties of mouse brain endothelial cells by stabilizing adherens junctions
    • E. Steiner, G.U. Enzmann, R. Lyck, S. Lin, M.A. Ruegg, S. Kroger, and B. Engelhardt The heparan sulfate proteoglycan agrin contributes to barrier properties of mouse brain endothelial cells by stabilizing adherens junctions Cell Tissue Res. 358 2014 465 479
    • (2014) Cell Tissue Res. , vol.358 , pp. 465-479
    • Steiner, E.1    Enzmann, G.U.2    Lyck, R.3    Lin, S.4    Ruegg, M.A.5    Kroger, S.6    Engelhardt, B.7
  • 124
    • 0023030826 scopus 로고
    • Identification of ZO-1: A high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia
    • B.R. Stevenson, J.D. Siliciano, M.S. Mooseker, and D.A. Goodenough Identification of ZO-1: a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia J. Cell Biol. 103 1986 755 766
    • (1986) J. Cell Biol. , vol.103 , pp. 755-766
    • Stevenson, B.R.1    Siliciano, J.D.2    Mooseker, M.S.3    Goodenough, D.A.4
  • 126
    • 33845212296 scopus 로고    scopus 로고
    • Role of SLC xenobiotic transporters and their regulatory mechanisms PDZ proteins in drug delivery and disposition
    • T. Sugiura, Y. Kato, and A. Tsuji Role of SLC xenobiotic transporters and their regulatory mechanisms PDZ proteins in drug delivery and disposition J. Control. Release 116 2006 238 246
    • (2006) J. Control. Release , vol.116 , pp. 238-246
    • Sugiura, T.1    Kato, Y.2    Tsuji, A.3
  • 127
    • 0242384851 scopus 로고    scopus 로고
    • Functional characterization of rat brain-specific organic anion transporter (Oatp14) at the blood-brain barrier: High affinity transporter for thyroxine
    • D. Sugiyama, H. Kusuhara, H. Taniguchi, S. Ishikawa, Y. Nozaki, H. Aburatani, and Y. Sugiyama Functional characterization of rat brain-specific organic anion transporter (Oatp14) at the blood-brain barrier: high affinity transporter for thyroxine J. Biol. Chem. 278 2003 43489 43495
    • (2003) J. Biol. Chem. , vol.278 , pp. 43489-43495
    • Sugiyama, D.1    Kusuhara, H.2    Taniguchi, H.3    Ishikawa, S.4    Nozaki, Y.5    Aburatani, H.6    Sugiyama, Y.7
  • 128
    • 84904557698 scopus 로고    scopus 로고
    • Arsenite stimulates glutathione export and glycolytic flux in viable primary rat brain astrocytes
    • N. Tadepalle, Y. Koehler, M. Brandmann, N. Meyer, and R. Dringen Arsenite stimulates glutathione export and glycolytic flux in viable primary rat brain astrocytes Neurochem. Int. 76 2014 1 11
    • (2014) Neurochem. Int. , vol.76 , pp. 1-11
    • Tadepalle, N.1    Koehler, Y.2    Brandmann, M.3    Meyer, N.4    Dringen, R.5
  • 129
    • 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
    • Y. Takenaga, N. Takagi, K. Murotomi, K. Tanonaka, and S. Takeo 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
  • 131
    • 84907996983 scopus 로고    scopus 로고
    • Drug delivery to the ischemic brain
    • B.J. Thompson, and P.T. Ronaldson Drug delivery to the ischemic brain Adv. Pharmacol. 71 2014 165 202
    • (2014) Adv. Pharmacol. , vol.71 , pp. 165-202
    • Thompson, B.J.1    Ronaldson, P.T.2
  • 132
    • 84897570512 scopus 로고    scopus 로고
    • Hypoxia/reoxygenation stress signals an increase in organic anion transporting polypeptide 1a4 (Oatp1a4) at the blood-brain barrier: Relevance to CNS drug delivery
    • B.J. Thompson, L. Sanchez-Covarrubias, L.M. Slosky, Y. Zhang, M.L. Laracuente, and P.T. Ronaldson Hypoxia/reoxygenation stress signals an increase in organic anion transporting polypeptide 1a4 (Oatp1a4) at the blood-brain barrier: relevance to CNS drug delivery J. Cereb. Blood Flow Metab. 34 2014 699 707
    • (2014) J. Cereb. Blood Flow Metab. , vol.34 , pp. 699-707
    • Thompson, B.J.1    Sanchez-Covarrubias, L.2    Slosky, L.M.3    Zhang, Y.4    Laracuente, M.L.5    Ronaldson, P.T.6
  • 133
    • 0033058448 scopus 로고    scopus 로고
    • Pravastatin, an HMG-CoA reductase inhibitor, is transported by rat organic anion transporting polypeptide, oatp2
    • T. Tokui, D. Nakai, R. Nakagomi, H. Yawo, T. Abe, and Y. Sugiyama Pravastatin, an HMG-CoA reductase inhibitor, is transported by rat organic anion transporting polypeptide, oatp2 Pharm. Res. 16 1999 904 908
    • (1999) Pharm. Res. , vol.16 , pp. 904-908
    • Tokui, T.1    Nakai, D.2    Nakagomi, R.3    Yawo, H.4    Abe, T.5    Sugiyama, Y.6
  • 134
    • 80053546097 scopus 로고    scopus 로고
    • Opioid transport by ATP-binding cassette transporters at the blood-brain barrier: Implications for neuropsychopharmacology
    • N. Tournier, X. Decleves, B. Saubamea, J.M. Scherrmann, and S. Cisternino Opioid transport by ATP-binding cassette transporters at the blood-brain barrier: implications for neuropsychopharmacology Curr. Pharm. Des. 17 2011 2829 2842
    • (2011) Curr. Pharm. Des. , vol.17 , pp. 2829-2842
    • Tournier, N.1    Decleves, X.2    Saubamea, B.3    Scherrmann, J.M.4    Cisternino, S.5
  • 135
    • 79953686193 scopus 로고    scopus 로고
    • Quantitative targeted absolute proteomics of human blood-brain barrier transporters and receptors
    • Y. Uchida, S. Ohtsuki, Y. Katsukura, C. Ikeda, T. Suzuki, J. Kamiie, and T. Terasaki Quantitative targeted absolute proteomics of human blood-brain barrier transporters and receptors J. Neurochem. 117 2011 333 345
    • (2011) J. Neurochem. , vol.117 , pp. 333-345
    • Uchida, Y.1    Ohtsuki, S.2    Katsukura, Y.3    Ikeda, C.4    Suzuki, T.5    Kamiie, J.6    Terasaki, T.7
  • 137
    • 7244219999 scopus 로고    scopus 로고
    • Establishment and characterization of cultured epithelial cells lacking expression of ZO-1
    • K. Umeda, T. Matsui, M. Nakayama, K. Furuse, H. Sasaki, M. Furuse, and S. Tsukita Establishment and characterization of cultured epithelial cells lacking expression of ZO-1 J. Biol. Chem. 279 2004 44785 44794
    • (2004) J. Biol. Chem. , vol.279 , pp. 44785-44794
    • Umeda, K.1    Matsui, T.2    Nakayama, M.3    Furuse, K.4    Sasaki, H.5    Furuse, M.6    Tsukita, S.7
  • 138
    • 0141919551 scopus 로고    scopus 로고
    • The breast cancer resistance protein (Bcrp1/Abcg2) restricts exposure to the dietary carcinogen 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine
    • A.E. van Herwaarden, J.W. Jonker, E. Wagenaar, R.F. Brinkhuis, J.H. Schellens, J.H. Beijnen, and A.H. Schinkel The breast cancer resistance protein (Bcrp1/Abcg2) restricts exposure to the dietary carcinogen 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine Cancer Res. 63 2003 6447 6452
    • (2003) Cancer Res. , vol.63 , pp. 6447-6452
    • Van Herwaarden, A.E.1    Jonker, J.W.2    Wagenaar, E.3    Brinkhuis, R.F.4    Schellens, J.H.5    Beijnen, J.H.6    Schinkel, A.H.7
  • 139
    • 59649102234 scopus 로고    scopus 로고
    • A functional role for sodium-dependent glucose transport across the blood-brain barrier during oxygen glucose deprivation
    • S. Vemula, K.E. Roder, T. Yang, G.J. Bhat, T.J. Thekkumkara, and T.J. Abbruscato A functional role for sodium-dependent glucose transport across the blood-brain barrier during oxygen glucose deprivation J. Pharmacol. Exp. Ther. 328 2009 487 495
    • (2009) J. Pharmacol. Exp. Ther. , vol.328 , pp. 487-495
    • Vemula, S.1    Roder, K.E.2    Yang, T.3    Bhat, G.J.4    Thekkumkara, T.J.5    Abbruscato, T.J.6
  • 140
    • 38549128935 scopus 로고    scopus 로고
    • VE-cadherin: The major endothelial adhesion molecule controlling cellular junctions and blood vessel formation
    • D. Vestweber VE-cadherin: the major endothelial adhesion molecule controlling cellular junctions and blood vessel formation Arterioscler. Thromb. Vasc. Biol. 28 2008 223 232
    • (2008) Arterioscler. Thromb. Vasc. Biol. , vol.28 , pp. 223-232
    • Vestweber, D.1
  • 141
    • 84897412061 scopus 로고    scopus 로고
    • Role of monocarboxylate transporters in drug delivery to the brain
    • N. Vijay, and M.E. Morris Role of monocarboxylate transporters in drug delivery to the brain Curr. Pharm. Des. 20 2014 1487 1498
    • (2014) Curr. Pharm. Des. , vol.20 , pp. 1487-1498
    • Vijay, N.1    Morris, M.E.2
  • 144
    • 84861885063 scopus 로고    scopus 로고
    • Junctional protein regulation by sphingosine kinase 2 contributes to blood-brain barrier protection in hypoxic preconditioning-induced cerebral ischemic tolerance
    • B.K. Wacker, A.B. Freie, J.L. Perfater, and J.M. Gidday Junctional protein regulation by sphingosine kinase 2 contributes to blood-brain barrier protection in hypoxic preconditioning-induced cerebral ischemic tolerance J. Cereb. Blood Flow Metab. 32 2012 1014 1023
    • (2012) J. Cereb. Blood Flow Metab. , vol.32 , pp. 1014-1023
    • Wacker, B.K.1    Freie, A.B.2    Perfater, J.L.3    Gidday, J.M.4
  • 145
    • 84902436456 scopus 로고    scopus 로고
    • Nrf2 upregulates ATP binding cassette transporter expression and activity at the blood-brain and blood-spinal cord barriers
    • X. Wang, C.R. Campos, J.C. Peart, L.K. Smith, J.L. Boni, R.E. Cannon, and D.S. Miller Nrf2 upregulates ATP binding cassette transporter expression and activity at the blood-brain and blood-spinal cord barriers J. Neurosci. 34 2014 8585 8593
    • (2014) J. Neurosci. , vol.34 , pp. 8585-8593
    • Wang, X.1    Campos, C.R.2    Peart, J.C.3    Smith, L.K.4    Boni, J.L.5    Cannon, R.E.6    Miller, D.S.7
  • 147
    • 79955734571 scopus 로고    scopus 로고
    • CRM197-induced blood-brain barrier permeability increase is mediated by upregulation of caveolin-1 protein
    • P. Wang, Y. Liu, X. Shang, and Y. Xue CRM197-induced blood-brain barrier permeability increase is mediated by upregulation of caveolin-1 protein J. Mol. Neurosci. 43 2011 485 492
    • (2011) J. Mol. Neurosci. , vol.43 , pp. 485-492
    • Wang, P.1    Liu, Y.2    Shang, X.3    Xue, Y.4
  • 148
    • 70350279309 scopus 로고    scopus 로고
    • The blood-brain barrier thyroxine transporter organic anion-transporting polypeptide 1c1 displays atypical transport kinetics
    • D.E. Westholm, D.R. Salo, K.J. Viken, J.N. Rumbley, and G.W. Anderson The blood-brain barrier thyroxine transporter organic anion-transporting polypeptide 1c1 displays atypical transport kinetics Endocrinology 150 2009 5153 5162
    • (2009) Endocrinology , vol.150 , pp. 5153-5162
    • Westholm, D.E.1    Salo, D.R.2    Viken, K.J.3    Rumbley, J.N.4    Anderson, G.W.5
  • 149
    • 59649083811 scopus 로고    scopus 로고
    • Competitive inhibition of organic anion transporting polypeptide 1c1-mediated thyroxine transport by the fenamate class of nonsteroidal antiinflammatory drugs
    • D.E. Westholm, D.D. Stenehjem, J.N. Rumbley, L.R. Drewes, and G.W. Anderson Competitive inhibition of organic anion transporting polypeptide 1c1-mediated thyroxine transport by the fenamate class of nonsteroidal antiinflammatory drugs Endocrinology 150 2009 1025 1032
    • (2009) Endocrinology , vol.150 , pp. 1025-1032
    • Westholm, D.E.1    Stenehjem, D.D.2    Rumbley, J.N.3    Drewes, L.R.4    Anderson, G.W.5
  • 150
    • 84880837497 scopus 로고    scopus 로고
    • Mechanisms of HIV entry into the CNS: Increased sensitivity of HIV infected CD14+CD16+ monocytes to CCL2 and key roles of CCR2, JAM-A, and ALCAM in diapedesis
    • D.W. Williams, T.M. Calderon, L. Lopez, L. Carvallo-Torres, P.J. Gaskill, E.A. Eugenin, S. Morgello, and J.W. Berman Mechanisms of HIV entry into the CNS: increased sensitivity of HIV infected CD14+CD16+ monocytes to CCL2 and key roles of CCR2, JAM-A, and ALCAM in diapedesis PLoS One 8 2013 e69270
    • (2013) PLoS One , vol.8 , pp. e69270
    • Williams, D.W.1    Calderon, T.M.2    Lopez, L.3    Carvallo-Torres, L.4    Gaskill, P.J.5    Eugenin, E.A.6    Morgello, S.7    Berman, J.W.8
  • 151
    • 26244447845 scopus 로고    scopus 로고
    • Cadherin-10 is a novel blood-brain barrier adhesion molecule in human and mouse
    • M.J. Williams, M.B. Lowrie, J.P. Bennett, J.A. Firth, and P. Clark Cadherin-10 is a novel blood-brain barrier adhesion molecule in human and mouse Brain Res. 1058 2005 62 72
    • (2005) Brain Res. , vol.1058 , pp. 62-72
    • Williams, M.J.1    Lowrie, M.B.2    Bennett, J.P.3    Firth, J.A.4    Clark, P.5
  • 152
    • 84884146100 scopus 로고    scopus 로고
    • Partial recovery of the damaged rat blood-brain barrier is mediated by adherens junction complexes, extracellular matrix remodeling and macrophage infiltration following focal astrocyte loss
    • C.L. Willis, R.B. Camire, S.A. Brule, and D.E. Ray Partial recovery of the damaged rat blood-brain barrier is mediated by adherens junction complexes, extracellular matrix remodeling and macrophage infiltration following focal astrocyte loss Neuroscience 250 2013 773 785
    • (2013) Neuroscience , vol.250 , pp. 773-785
    • Willis, C.L.1    Camire, R.B.2    Brule, S.A.3    Ray, D.E.4
  • 153
    • 6044260215 scopus 로고    scopus 로고
    • Reversible disruption of tight junction complexes in the rat blood-brain barrier following transitory focal astrocyte loss
    • C.L. Willis, L. Leach, G.J. Clarke, C.C. Nolan, and D.E. Ray Reversible disruption of tight junction complexes in the rat blood-brain barrier following transitory focal astrocyte loss Glia 48 2004 1 13
    • (2004) Glia , vol.48 , pp. 1-13
    • Willis, C.L.1    Leach, L.2    Clarke, G.J.3    Nolan, C.C.4    Ray, D.E.5
  • 154
    • 78049452265 scopus 로고    scopus 로고
    • Protein kinase C activation modulates reversible increase in cortical blood-brain barrier permeability and tight junction protein expression during hypoxia and posthypoxic reoxygenation
    • C.L. Willis, D.S. Meske, and T.P. Davis Protein kinase C activation modulates reversible increase in cortical blood-brain barrier permeability and tight junction protein expression during hypoxia and posthypoxic reoxygenation J. Cereb. Blood Flow Metab. 30 2010 1847 1859
    • (2010) J. Cereb. Blood Flow Metab. , vol.30 , pp. 1847-1859
    • Willis, C.L.1    Meske, D.S.2    Davis, T.P.3
  • 155
    • 1542515004 scopus 로고    scopus 로고
    • Focal astrocyte loss is followed by microvascular damage, with subsequent repair of the blood-brain barrier in the apparent absence of direct astrocytic contact
    • C.L. Willis, C.C. Nolan, S.N. Reith, T. Lister, M.J. Prior, C.J. Guerin, G. Mavroudis, and D.E. Ray Focal astrocyte loss is followed by microvascular damage, with subsequent repair of the blood-brain barrier in the apparent absence of direct astrocytic contact Glia 45 2004 325 337
    • (2004) Glia , vol.45 , pp. 325-337
    • Willis, C.L.1    Nolan, C.C.2    Reith, S.N.3    Lister, T.4    Prior, M.J.5    Guerin, C.J.6    Mavroudis, G.7    Ray, D.E.8
  • 156
    • 0344009459 scopus 로고    scopus 로고
    • Effects of hypoxia-reoxygenation on rat blood-brain barrier permeability and tight junctional protein expression
    • K.A. Witt, K.S. Mark, S. Hom, and T.P. Davis Effects of hypoxia-reoxygenation on rat blood-brain barrier permeability and tight junctional protein expression Am. J. Physiol. Heart Circ. Physiol. 285 2003 H2820 H2831
    • (2003) Am. J. Physiol. Heart Circ. Physiol. , vol.285 , pp. H2820-H2831
    • Witt, K.A.1    Mark, K.S.2    Hom, S.3    Davis, T.P.4
  • 157
    • 13244252689 scopus 로고    scopus 로고
    • Hypoxia-inducible factor and nuclear factor kappa-B activation in blood-brain barrier endothelium under hypoxic/reoxygenation stress
    • K.A. Witt, K.S. Mark, J. Huber, and T.P. Davis Hypoxia-inducible factor and nuclear factor kappa-B activation in blood-brain barrier endothelium under hypoxic/reoxygenation stress J. Neurochem. 92 2005 203 214
    • (2005) J. Neurochem. , vol.92 , pp. 203-214
    • Witt, K.A.1    Mark, K.S.2    Huber, J.3    Davis, T.P.4
  • 158
    • 37249084760 scopus 로고    scopus 로고
    • Reoxygenation stresson blood-brain barrier paracellular permeability and edema in the rat
    • K.A. Witt, K.S. Mark, K.E. Sandoval, and T.P. Davis Reoxygenation stresson 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
  • 159
    • 77953971007 scopus 로고    scopus 로고
    • Statins and neuroprotection: A prescription to move the field forward
    • W.G. Wood, G.P. Eckert, U. Igbavboa, and W.E. Muller Statins and neuroprotection: a prescription to move the field forward Ann. N. Y. Acad. Sci. 1199 2010 69 76
    • (2010) Ann. N. Y. Acad. Sci. , vol.1199 , pp. 69-76
    • Wood, W.G.1    Eckert, G.P.2    Igbavboa, U.3    Muller, W.E.4
  • 163
    • 37349023393 scopus 로고    scopus 로고
    • Enhancement of glucose transporter expression of brain endothelial cells by vascular endothelial growth factor derived from glioma exposed to hypoxia
    • W.L. Yeh, C.J. Lin, and W.M. Fu Enhancement of glucose transporter expression of brain endothelial cells by vascular endothelial growth factor derived from glioma exposed to hypoxia Mol. Pharmacol. 73 2008 170 177
    • (2008) Mol. Pharmacol. , vol.73 , pp. 170-177
    • Yeh, W.L.1    Lin, C.J.2    Fu, W.M.3
  • 164
    • 43649106042 scopus 로고    scopus 로고
    • Decreased junctional adhesion molecule-A expression during blood-brain barrier breakdown
    • D. Yeung, J.L. Manias, D.J. Stewart, and S. Nag Decreased junctional adhesion molecule-A expression during blood-brain barrier breakdown Acta Neuropathol. 115 2008 635 642
    • (2008) Acta Neuropathol. , vol.115 , pp. 635-642
    • Yeung, D.1    Manias, J.L.2    Stewart, D.J.3    Nag, S.4
  • 165
    • 84867574677 scopus 로고    scopus 로고
    • Induction of P-glcyoprotein and Bcrp at the rat blood-brain barrier following a subchronic morphine treatment is mediated through NMDA/COX-2 acitivation
    • S. Yousif, C. Chaves, S. Potin, I. Margalli, J.M. Scherrmann, and X. Decleves Induction of P-glcyoprotein and Bcrp at the rat blood-brain barrier following a subchronic morphine treatment is mediated through NMDA/COX-2 acitivation J. Neurochem. 123 2012 491 503
    • (2012) J. Neurochem. , vol.123 , pp. 491-503
    • Yousif, S.1    Chaves, C.2    Potin, S.3    Margalli, I.4    Scherrmann, J.M.5    Decleves, X.6
  • 167
    • 84891952619 scopus 로고    scopus 로고
    • Moderate hypoxia followed by reoxygenation results in blood-brain barrier breakdown via oxidative stress-dependent tight-junction protein disruption
    • C.M. Zehendner, L. Librizzi, J. Hedrich, N.M. Bauer, E.A. Angamo, M. de Curtis, and H.J. Luhmann Moderate hypoxia followed by reoxygenation results in blood-brain barrier breakdown via oxidative stress-dependent tight-junction protein disruption PLoS One 8 2013 e82823
    • (2013) PLoS One , vol.8 , pp. e82823
    • Zehendner, C.M.1    Librizzi, L.2    Hedrich, J.3    Bauer, N.M.4    Angamo, E.A.5    De Curtis, M.6    Luhmann, H.J.7
  • 168
    • 6344240461 scopus 로고    scopus 로고
    • Plasma membrane localization of multidrug resistance-associated protein homologs in brain capillary endothelial cells
    • Y. Zhang, J.D. Schuetz, W.F. Elmquist, and D.W. Miller Plasma membrane localization of multidrug resistance-associated protein homologs in brain capillary endothelial cells J. Pharmacol. Exp. Ther. 311 2004 449 455
    • (2004) J. Pharmacol. Exp. Ther. , vol.311 , pp. 449-455
    • Zhang, Y.1    Schuetz, J.D.2    Elmquist, W.F.3    Miller, D.W.4
  • 169
    • 66649132535 scopus 로고    scopus 로고
    • Breast cancer resistance protein interacts with various compounds in vitro, but plays a minor role in substrate efflux at the blood-brain barrier
    • R. Zhao, T.J. Raub, G.A. Sawada, S.C. Kasper, J.A. Bacon, A.S. Bridges, and G.M. Pollack Breast cancer resistance protein interacts with various compounds in vitro, but plays a minor role in substrate efflux at the blood-brain barrier Drug Metab. Dispos. 37 2009 1251 1258
    • (2009) Drug Metab. Dispos. , vol.37 , pp. 1251-1258
    • Zhao, R.1    Raub, T.J.2    Sawada, G.A.3    Kasper, S.C.4    Bacon, J.A.5    Bridges, A.S.6    Pollack, G.M.7
  • 170
    • 66449110827 scopus 로고    scopus 로고
    • The effect of breast cancer resistance protein and P-glycoprotein on the brain penetration of flavopiridol, imatinib mesylate (Gleevec), prazosin, and 2-methoxy-3-(4-(2-(5-methyl-2-phenyloxazol-4-yl)ethoxy)phenyl)propanoic acid (PF-407288) in mice
    • L. Zhou, K. Schmidt, F.R. Nelson, V. Zelesky, M.D. Troutman, and B. Feng The effect of breast cancer resistance protein and P-glycoprotein on the brain penetration of flavopiridol, imatinib mesylate (Gleevec), prazosin, and 2-methoxy-3-(4-(2-(5-methyl-2-phenyloxazol-4-yl)ethoxy)phenyl)propanoic acid (PF-407288) in mice Drug Metab. Dispos. 37 2009 946 955
    • (2009) Drug Metab. Dispos. , vol.37 , pp. 946-955
    • Zhou, L.1    Schmidt, K.2    Nelson, F.R.3    Zelesky, V.4    Troutman, M.D.5    Feng, B.6


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