메뉴 건너뛰기




Volumn 33, Issue 3, 2013, Pages 489-500

Claudin-5 controls intercellular barriers of human dermal microvascular but not human umbilical vein endothelial cells

Author keywords

endothelial cell; heterogeneity; microvessel; permeability; tight junction

Indexed keywords

CLAUDIN 5; VASCULAR ENDOTHELIAL CADHERIN;

EID: 84874387050     PISSN: 10795642     EISSN: 15244636     Source Type: Journal    
DOI: 10.1161/ATVBAHA.112.300893     Document Type: Article
Times cited : (70)

References (70)
  • 1
    • 84933886562 scopus 로고
    • The gradient of vascular permeability
    • Rous P, Gilding HP, Smith F. The gradient of vascular permeability. J Exp Med. 1930;51:807-830.
    • (1930) J Exp Med , vol.51 , pp. 807-830
    • Rous, P.1    Gilding, H.P.2    Smith, F.3
  • 2
    • 85011132117 scopus 로고
    • The gradient of vascular permeability: III. The gradient along the capillaries and venules of frog skin
    • Rous P, Smith F. The gradient of vascular permeability: III. The gradient along the capillaries and venules of frog skin. J Exp Med. 1931;53:219-242.
    • (1931) J Exp Med , vol.53 , pp. 219-242
    • Rous, P.1    Smith, F.2
  • 3
    • 85012772025 scopus 로고
    • The gradient of vascular permeability: IV. The permeability of the cutaneous venules and its functional significance
    • Smith F, Rous P. The gradient of vascular permeability: IV. The permeability of the cutaneous venules and its functional significance. J Exp Med. 1931;54:499-514.
    • (1931) J Exp Med , vol.54 , pp. 499-514
    • Smith, F.1    Rous, P.2
  • 4
    • 0006943326 scopus 로고
    • The gradient of vascular permeability: II. The conditions in frog and chicken muscle, and in the mammalian diaphragm
    • Smith F, Rous P. The gradient of vascular permeability: II. The conditions in frog and chicken muscle, and in the mammalian diaphragm. J Exp Med. 1931;53:195-217.
    • (1931) J Exp Med , vol.53 , pp. 195-217
    • Smith, F.1    Rous, P.2
  • 5
    • 79952955107 scopus 로고    scopus 로고
    • Microcirculatory exchange function
    • Tuma RF Duran WN Ley K eds. New York NY Elsevier-Academic Press
    • Duran WN, Sanchez FA, Breslin JW. Microcirculatory exchange function. In: Tuma, RF, Duran, WN, Ley, K, eds. Handbook of Physiology: Microcirculation. New York, NY: Elsevier-Academic Press; 2008:81-124.
    • (2008) Handbook of Physiology: Microcirculation , pp. 81-124
    • Duran, W.N.1    Sanchez, F.A.2    Breslin, J.W.3
  • 6
    • 77951697920 scopus 로고    scopus 로고
    • Regulation of endothelial permeability via paracellular and transcellular transport pathways
    • Komarova Y, Malik AB. Regulation of endothelial permeability via paracellular and transcellular transport pathways. Annu Rev Physiol. 2010;72:463-493.
    • (2010) Annu Rev Physiol , vol.72 , pp. 463-493
    • Komarova, Y.1    Malik, A.B.2
  • 7
    • 0016724876 scopus 로고
    • Segmental differentiations of cell junctions in the vascular endothelium. The microvasculature
    • Simionescu M, Simionescu N, Palade GE. Segmental differentiations of cell junctions in the vascular endothelium. The microvasculature. J Cell Biol. 1975;67:863-885.
    • (1975) J Cell Biol , vol.67 , pp. 863-885
    • Simionescu, M.1    Simionescu, N.2    Palade, G.E.3
  • 8
    • 0017861891 scopus 로고
    • Structural basis of permeability in sequential segments of the microvasculature of the diaphragm. II. Pathways followed by microperoxidase across the endothelium
    • Simionescu N, Simionescu M, Palade GE. Structural basis of permeability in sequential segments of the microvasculature of the diaphragm. II. Pathways followed by microperoxidase across the endothelium. Microvasc Res. 1978;15:17-36.
    • (1978) Microvasc Res , vol.15 , pp. 17-36
    • Simionescu, N.1    Simionescu, M.2    Palade, G.E.3
  • 9
    • 0019520573 scopus 로고
    • Segmental differentiation of endothelial intercellular junctions in intra-acinar arteries and veins of the rat lung
    • Schneeberger EE. Segmental differentiation of endothelial intercellular junctions in intra-acinar arteries and veins of the rat lung. Circ Res. 1981;49:1102-1111.
    • (1981) Circ Res , vol.49 , pp. 1102-1111
    • Schneeberger, E.E.1
  • 10
    • 0031156796 scopus 로고    scopus 로고
    • Vascular endothelial cadherin (VE-cadherin): Cloning and role in endothelial cell-cell adhesion
    • Ali J, Liao F, Martens E, Muller WA. Vascular endothelial cadherin (VE-cadherin): cloning and role in endothelial cell-cell adhesion. Microcirculation. 1997;4:267-277.
    • (1997) Microcirculation , vol.4 , pp. 267-277
    • Ali, J.1    Liao, F.2    Martens, E.3    Muller, W.A.4
  • 13
    • 0035869433 scopus 로고    scopus 로고
    • Monoclonal antibodies directed to different regions of vascular endothelial cadherin extracellular domain affect adhesion and clustering of the protein and modulate endothelial permeability
    • Corada M, Liao F, Lindgren M, Lampugnani MG, Breviario F, Frank R, Muller WA, Hicklin DJ, Bohlen P, Dejana E. Monoclonal antibodies directed to different regions of vascular endothelial cadherin extracellular domain affect adhesion and clustering of the protein and modulate endothelial permeability. Blood. 2001;97:1679-1684.
    • (2001) Blood , vol.97 , pp. 1679-1684
    • Corada, M.1    Liao, F.2    Lindgren, M.3    Lampugnani, M.G.4    Breviario, F.5    Frank, R.6    Muller, W.A.7    Hicklin, D.J.8    Bohlen, P.9    Dejana, E.10
  • 14
    • 0023225108 scopus 로고
    • Transformation of cell adhesion properties by exogenously introduced E-cadherin cDNA
    • Nagafuchi A, Shirayoshi Y, Okazaki K, Yasuda K, Takeichi M. Transformation of cell adhesion properties by exogenously introduced E-cadherin cDNA. Nature. 1987;329:341-343.
    • (1987) Nature , vol.329 , pp. 341-343
    • Nagafuchi, A.1    Shirayoshi, Y.2    Okazaki, K.3    Yasuda, K.4    Takeichi, M.5
  • 16
    • 59649092177 scopus 로고    scopus 로고
    • The control of vascular integrity by endothelial cell junctions: Molecular basis and pathological implications
    • Dejana E, Tournier-Lasserve E, Weinstein BM. The control of vascular integrity by endothelial cell junctions: molecular basis and pathological implications. Dev Cell. 2009;16:209-221.
    • (2009) Dev Cell , vol.16 , pp. 209-221
    • Dejana, E.1    Tournier-Lasserve, E.2    Weinstein, B.M.3
  • 17
    • 0347756750 scopus 로고    scopus 로고
    • Transference of recombinant VE-cadherin cytoplasmic domain alters endothelial junctional integrity and porcine microvascular permeability
    • Guo M, Wu MH, Granger HJ, Yuan SY. Transference of recombinant VE-cadherin cytoplasmic domain alters endothelial junctional integrity and porcine microvascular permeability. J Physiol (Lond). 2004;554(pt 1):78-88.
    • (2004) J Physiol (Lond) , vol.554 , Issue.PART 1 , pp. 78-88
    • Guo, M.1    Wu, M.H.2    Granger, H.J.3    Yuan, S.Y.4
  • 18
    • 0028900299 scopus 로고
    • The molecular organization of endothelial cell to cell junctions: Differential association of plakoglobin, beta-catenin, and alphacatenin with vascular endothelial cadherin (VE-cadherin)
    • Lampugnani MG, Corada M, Caveda L, Breviario F, Ayalon O, Geiger B, Dejana E. The molecular organization of endothelial cell to cell junctions: differential association of plakoglobin, beta-catenin, and alphacatenin with vascular endothelial cadherin (VE-cadherin). J Cell Biol. 1995;129:203-217.
    • (1995) J Cell Biol , vol.129 , pp. 203-217
    • Lampugnani, M.G.1    Corada, M.2    Caveda, L.3    Breviario, F.4    Ayalon, O.5    Geiger, B.6    Dejana, E.7
  • 20
    • 77951495204 scopus 로고    scopus 로고
    • Control of endothelial barrier function by regulating vascular endothelial-cadherin
    • Vestweber D, Broermann A, Schulte D. Control of endothelial barrier function by regulating vascular endothelial-cadherin. Curr Opin Hematol. 2010;17:230-236.
    • (2010) Curr Opin Hematol , vol.17 , pp. 230-236
    • Vestweber, D.1    Broermann, A.2    Schulte, D.3
  • 21
    • 0242456021 scopus 로고    scopus 로고
    • Cellular levels of p120 catenin function as a set point for cadherin expression levels in microvascular endothelial cells
    • Xiao K, Allison DF, Buckley KM, Kottke MD, Vincent PA, Faundez V, Kowalczyk AP. Cellular levels of p120 catenin function as a set point for cadherin expression levels in microvascular endothelial cells. J Cell Biol. 2003;163:535-545.
    • (2003) J Cell Biol , vol.163 , pp. 535-545
    • Xiao, K.1    Allison, D.F.2    Buckley, K.M.3    Kottke, M.D.4    Vincent, P.A.5    Faundez, V.6    Kowalczyk, A.P.7
  • 22
    • 33846065117 scopus 로고    scopus 로고
    • Depletion of E-cadherin disrupts establishment but not maintenance of cell junctions in Madin-Darby canine kidney epithelial cells
    • Capaldo CT, Macara IG. Depletion of E-cadherin disrupts establishment but not maintenance of cell junctions in Madin-Darby canine kidney epithelial cells. Mol Biol Cell. 2007;18:189-200.
    • (2007) Mol Biol Cell , vol.18 , pp. 189-200
    • Capaldo, C.T.1    MacAra, I.G.2
  • 23
    • 0033523758 scopus 로고    scopus 로고
    • Endothelial claudin: Claudin-5/TMVCF constitutes tight junction strands in endothelial cells
    • Morita K, Sasaki H, Furuse M, Tsukita S. Endothelial claudin: claudin-5/TMVCF constitutes tight junction strands in endothelial cells. J Cell Biol. 1999;147:185-194.
    • (1999) J Cell Biol , vol.147 , pp. 185-194
    • Morita, K.1    Sasaki, H.2    Furuse, M.3    Tsukita, S.4
  • 26
    • 0033571047 scopus 로고    scopus 로고
    • Manner of interaction of heterogeneous claudin species within and between tight junction strands
    • Furuse M, Sasaki H, Tsukita S. Manner of interaction of heterogeneous claudin species within and between tight junction strands. J Cell Biol. 1999;147:891-903.
    • (1999) J Cell Biol , vol.147 , pp. 891-903
    • Furuse, M.1    Sasaki, H.2    Tsukita, S.3
  • 28
    • 77953021608 scopus 로고    scopus 로고
    • Participation of the second extracellular loop of claudin-5 in paracellular tightening against ions, small and large molecules
    • Piehl C, Piontek J, Cording J, Wolburg H, Blasig IE. Participation of the second extracellular loop of claudin-5 in paracellular tightening against ions, small and large molecules. Cell Mol Life Sci. 2010;67:2131-2140.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 2131-2140
    • Piehl, C.1    Piontek, J.2    Cording, J.3    Wolburg, H.4    Blasig, I.E.5
  • 30
    • 0033598188 scopus 로고    scopus 로고
    • Ca(2+)-independent cell-adhesion activity of claudins, a family of integral membrane proteins localized at tight junctions
    • Kubota K, Furuse M, Sasaki H, Sonoda N, Fujita K, Nagafuchi A, Tsukita S. Ca(2+)-independent cell-adhesion activity of claudins, a family of integral membrane proteins localized at tight junctions. Curr Biol. 1999;9:1035-1038.
    • (1999) Curr Biol , vol.9 , pp. 1035-1038
    • Kubota, K.1    Furuse, M.2    Sasaki, H.3    Sonoda, N.4    Fujita, K.5    Nagafuchi, A.6    Tsukita, S.7
  • 31
    • 0033552629 scopus 로고    scopus 로고
    • Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins
    • Itoh M, Furuse M, Morita K, Kubota K, Saitou M, Tsukita S. Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins. J Cell Biol. 1999;147:1351-1363.
    • (1999) J Cell Biol , vol.147 , pp. 1351-1363
    • Itoh, M.1    Furuse, M.2    Morita, K.3    Kubota, K.4    Saitou, M.5    Tsukita, S.6
  • 32
    • 1542778870 scopus 로고    scopus 로고
    • Claudin-8 interacts with multi-PDZ domain protein 1 (MUPP1) and reduces paracellular conductance in epithelial cells
    • Jeansonne B, Lu Q, Goodenough DA, Chen YH. Claudin-8 interacts with multi-PDZ domain protein 1 (MUPP1) and reduces paracellular conductance in epithelial cells. Cell Mol Biol (Noisy-le-grand). 2003;49:13-21.
    • (2003) Cell Mol Biol (Noisy-le-grand) , vol.49 , pp. 13-21
    • Jeansonne, B.1    Lu, Q.2    Goodenough, D.A.3    Chen, Y.H.4
  • 33
    • 0037191066 scopus 로고    scopus 로고
    • Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells
    • Poliak S, Matlis S, Ullmer C, Scherer SS, Peles E. Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells. J Cell Biol. 2002;159:361-372.
    • (2002) J Cell Biol , vol.159 , pp. 361-372
    • Poliak, S.1    Matlis, S.2    Ullmer, C.3    Scherer, S.S.4    Peles, E.5
  • 34
    • 0033521140 scopus 로고    scopus 로고
    • Protein interactions at the tight junction. Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3
    • Wittchen ES, Haskins J, Stevenson BR. Protein interactions at the tight junction. Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3. J Biol Chem. 1999;274:35179-35185.
    • (1999) J Biol Chem , vol.274 , pp. 35179-35185
    • Wittchen, E.S.1    Haskins, J.2    Stevenson, B.R.3
  • 35
    • 0000752197 scopus 로고
    • Junctional complexes in various epithelia
    • Farquhar MG, Palade GE. Junctional complexes in various epithelia. J Cell Biol. 1963;17:375-412.
    • (1963) J Cell Biol , vol.17 , pp. 375-412
    • Farquhar, M.G.1    Palade, G.E.2
  • 36
    • 0036832157 scopus 로고    scopus 로고
    • Isolation and functional characterization of the actin binding region in the tight junction protein ZO-1
    • Fanning AS, Ma TY, Anderson JM. Isolation and functional characterization of the actin binding region in the tight junction protein ZO-1. FASEB J. 2002;16:1835-1837.
    • (2002) FASEB J , vol.16 , pp. 1835-1837
    • Fanning, A.S.1    Ma, T.Y.2    Anderson, J.M.3
  • 37
    • 77952756845 scopus 로고    scopus 로고
    • Molecular basis of the core structure of tight junctions
    • Furuse M. Molecular basis of the core structure of tight junctions. Cold Spring Harb Perspect Biol. 2010;2:a002907.
    • (2010) Cold Spring Harb Perspect Biol , vol.2
    • Furuse, M.1
  • 38
    • 39849103311 scopus 로고    scopus 로고
    • The cytoplasmic plaque of tight junctions: A scaffolding and signalling center
    • Guillemot L, Paschoud S, Pulimeno P, Foglia A, Citi S. The cytoplasmic plaque of tight junctions: a scaffolding and signalling center. Biochim Biophys Acta. 2008;1778:601-613.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 601-613
    • Guillemot, L.1    Paschoud, S.2    Pulimeno, P.3    Foglia, A.4    Citi, S.5
  • 39
    • 2442631580 scopus 로고    scopus 로고
    • Cell-cell junctions of dermal microvascular endothelial cells contain tight and adherens junction proteins in spatial proximity
    • Rüffer C, Strey A, Janning A, Kim KS, Gerke V. Cell-cell junctions of dermal microvascular endothelial cells contain tight and adherens junction proteins in spatial proximity. Biochemistry. 2004;43:5360-5369.
    • (2004) Biochemistry , vol.43 , pp. 5360-5369
    • Rüffer, C.1    Strey, A.2    Janning, A.3    Kim, K.S.4    Gerke, V.5
  • 42
    • 0031568002 scopus 로고    scopus 로고
    • Mechanism of sustained E-selectin expression in cultured human dermal microvascular endothelial cells
    • Kluger MS, Johnson DR, Pober JS. Mechanism of sustained E-selectin expression in cultured human dermal microvascular endothelial cells. J Immunol. 1997;158:887-896.
    • (1997) J Immunol , vol.158 , pp. 887-896
    • Kluger, M.S.1    Johnson, D.R.2    Pober, J.S.3
  • 43
    • 0036498903 scopus 로고    scopus 로고
    • Cutting edge: Internalization of transduced E-selectin by cultured human endothelial cells: Comparison of dermal microvascular and umbilical vein cells and identification of a phosphoserine-type di-leucine motif
    • Kluger MS, Shiao SL, Bothwell AL, Pober JS. Cutting edge: internalization of transduced E-selectin by cultured human endothelial cells: comparison of dermal microvascular and umbilical vein cells and identification of a phosphoserine-type di-leucine motif. J Immunol. 2002;168:2091-2095.
    • (2002) J Immunol , vol.168 , pp. 2091-2095
    • Kluger, M.S.1    Shiao, S.L.2    Bothwell, A.L.3    Pober, J.S.4
  • 45
    • 3543024486 scopus 로고    scopus 로고
    • The C-terminal cytoplasmic tail of claudins 1 and 5 but not its PDZ-binding motif is required for apical localization at epithelial and endothelial tight junctions
    • Rüffer C, Gerke V. The C-terminal cytoplasmic tail of claudins 1 and 5 but not its PDZ-binding motif is required for apical localization at epithelial and endothelial tight junctions. Eur J Cell Biol. 2004;83:135-144.
    • (2004) Eur J Cell Biol , vol.83 , pp. 135-144
    • Rüffer, C.1    Gerke, V.2
  • 46
    • 0025916059 scopus 로고
    • Micromotion of mammalian cells measured electrically
    • Giaever I, Keese CR. Micromotion of mammalian cells measured electrically. Proc Natl Acad Sci USA. 1991;88:7896-7900.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7896-7900
    • Giaever, I.1    Keese, C.R.2
  • 47
    • 0017236553 scopus 로고
    • Ultrastructure of the human dermal microcirculation: The horizontal plexus of the papillary dermis
    • Yen A, Braverman IM. Ultrastructure of the human dermal microcirculation: the horizontal plexus of the papillary dermis. J Invest Dermatol. 1976;66:131-142.
    • (1976) J Invest Dermatol , vol.66 , pp. 131-142
    • Yen, A.1    Braverman, I.M.2
  • 48
    • 0028081567 scopus 로고
    • Inducibility and expression of microvascular endothelial adhesion molecules in lesional, perilesional, and uninvolved skin of psoriatic patients
    • Petzelbauer P, Pober JS, Keh A, Braverman IM. Inducibility and expression of microvascular endothelial adhesion molecules in lesional, perilesional, and uninvolved skin of psoriatic patients. J Invest Dermatol. 1994;103:300-305.
    • (1994) J Invest Dermatol , vol.103 , pp. 300-305
    • Petzelbauer, P.1    Pober, J.S.2    Keh, A.3    Braverman, I.M.4
  • 49
    • 0017581866 scopus 로고
    • Ultrastructure of the human dermal microcirculation. II. The capillary loops of the dermal papillae
    • Braverman IM, Yen A. Ultrastructure of the human dermal microcirculation. II. The capillary loops of the dermal papillae. J Invest Dermatol. 1977;68:44-52.
    • (1977) J Invest Dermatol , vol.68 , pp. 44-52
    • Braverman, I.M.1    Yen, A.2
  • 50
    • 0024371028 scopus 로고
    • Ultrastructure and organization of the cutaneous microvasculature in normal and pathologic states
    • Braverman IM. Ultrastructure and organization of the cutaneous microvasculature in normal and pathologic states. J Invest Dermatol. 1989;93:2S-9S.
    • (1989) J Invest Dermatol , vol.93
    • Braverman, I.M.1
  • 52
    • 0022642049 scopus 로고
    • Quantitation of the relationship between aortic endothelial intercellular cleft morphology and permeability to albumin
    • Zimmerman M, McGeachie J. Quantitation of the relationship between aortic endothelial intercellular cleft morphology and permeability to albumin. Atherosclerosis. 1986;59:277-282.
    • (1986) Atherosclerosis , vol.59 , pp. 277-282
    • Zimmerman, M.1    McGeachie, J.2
  • 54
    • 25444486668 scopus 로고    scopus 로고
    • The Rac activator Tiam1 controls tight junction biogenesis in keratinocytes through binding to and activation of the Par polarity complex
    • Mertens AE, Rygiel TP, Olivo C, van der Kammen R, Collard JG. The Rac activator Tiam1 controls tight junction biogenesis in keratinocytes through binding to and activation of the Par polarity complex. J Cell Biol. 2005;170:1029-1037.
    • (2005) J Cell Biol , vol.170 , pp. 1029-1037
    • Mertens, A.E.1    Rygiel, T.P.2    Olivo, C.3    Van Der Kammen, R.4    Collard, J.G.5
  • 55
    • 34247842900 scopus 로고    scopus 로고
    • Hypoxia disrupts the barrier function of neural blood vessels through changes in the expression of claudin-5 in endothelial cells
    • Koto T, Takubo K, Ishida S, Shinoda H, Inoue M, Tsubota K, Okada Y, Ikeda E. Hypoxia disrupts the barrier function of neural blood vessels through changes in the expression of claudin-5 in endothelial cells. Am J Pathol. 2007;170:1389-1397.
    • (2007) Am J Pathol , vol.170 , pp. 1389-1397
    • Koto, T.1    Takubo, K.2    Ishida, S.3    Shinoda, H.4    Inoue, M.5    Tsubota, K.6    Okada, Y.7    Ikeda, E.8
  • 57
    • 3042590902 scopus 로고    scopus 로고
    • Endothelial cell-to-cell junctions: Molecular organization and role in vascular homeostasis
    • Bazzoni G, Dejana E. Endothelial cell-to-cell junctions: molecular organization and role in vascular homeostasis. Physiol Rev. 2004;84:869-901.
    • (2004) Physiol Rev , vol.84 , pp. 869-901
    • Bazzoni, G.1    Dejana, E.2
  • 60
    • 33749516287 scopus 로고    scopus 로고
    • Limited contribution of claudin-5-dependent tight junction strands to endothelial barrier function
    • Fontijn RD, Rohlena J, van Marle J, Pannekoek H, Horrevoets AJ. Limited contribution of claudin-5-dependent tight junction strands to endothelial barrier function. Eur J Cell Biol. 2006;85:1131-1144.
    • (2006) Eur J Cell Biol , vol.85 , pp. 1131-1144
    • Fontijn, R.D.1    Rohlena, J.2    Van Marle, J.3    Pannekoek, H.4    Horrevoets, A.J.5
  • 62
    • 33846798106 scopus 로고    scopus 로고
    • Phenotypic heterogeneity of the endothelium I. Structure, function, and mechanisms
    • Aird WC. Phenotypic heterogeneity of the endothelium: I. Structure, function, and mechanisms. Circ Res. 2007;100:158-173.
    • (2007) Circ Res , vol.100 , pp. 158-173
    • Aird, W.C.1
  • 63
  • 65
    • 72449202243 scopus 로고    scopus 로고
    • Immortalized human brain endothelial cell line HCMEC/D3 as a model of the blood-brain barrier facilitates in vitro studies of central nervous system infection by Cryptococcus neoformans
    • Vu K, Weksler B, Romero I, Couraud PO, Gelli A. Immortalized human brain endothelial cell line HCMEC/D3 as a model of the blood-brain barrier facilitates in vitro studies of central nervous system infection by Cryptococcus neoformans. Eukaryotic Cell. 2009;8: 1803-1807.
    • (2009) Eukaryotic Cell , vol.8 , pp. 1803-1807
    • Vu, K.1    Weksler, B.2    Romero, I.3    Couraud, P.O.4    Gelli, A.5
  • 66
    • 34748815589 scopus 로고    scopus 로고
    • Pericytes from brain microvessels strengthen the barrier integrity in primary cultures of rat brain endothelial cells
    • Nakagawa S, Deli MA, Nakao S, Honda M, Hayashi K, Nakaoke R, Kataoka Y, Niwa M. Pericytes from brain microvessels strengthen the barrier integrity in primary cultures of rat brain endothelial cells. Cell Mol Neurobiol. 2007;27:687-694.
    • (2007) Cell Mol Neurobiol , vol.27 , pp. 687-694
    • Nakagawa, S.1    Deli, M.A.2    Nakao, S.3    Honda, M.4    Hayashi, K.5    Nakaoke, R.6    Kataoka, Y.7    Niwa, M.8
  • 67
    • 84856373406 scopus 로고    scopus 로고
    • Pericyte-derived glial cell line-derived neurotrophic factor increase the expression of claudin-5 in the blood-brain barrier and the blood-nerve barrier
    • Shimizu F, Sano Y, Saito K, Abe MA, Maeda T, Haruki H, Kanda T. Pericyte-derived glial cell line-derived neurotrophic factor increase the expression of claudin-5 in the blood-brain barrier and the blood-nerve barrier. Neurochem Res. 2012;37:401-409.
    • (2012) Neurochem Res , vol.37 , pp. 401-409
    • Shimizu, F.1    Sano, Y.2    Saito, K.3    Abe, M.A.4    Maeda, T.5    Haruki, H.6    Kanda, T.7
  • 69
    • 51149089536 scopus 로고    scopus 로고
    • Distinct molecular composition of blood and lymphatic vascular endothelial cell junctions establishes specific functional barriers within the peripheral lymph node
    • Pfeiffer F, Kumar V, Butz S, Vestweber D, Imhof BA, Stein JV, Engelhardt B. Distinct molecular composition of blood and lymphatic vascular endothelial cell junctions establishes specific functional barriers within the peripheral lymph node. Eur J Immunol. 2008;38:2142-2155.
    • (2008) Eur J Immunol , vol.38 , pp. 2142-2155
    • Pfeiffer, F.1    Kumar, V.2    Butz, S.3    Vestweber, D.4    Imhof, B.A.5    Stein, J.V.6    Engelhardt, B.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.