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Volumn 36, Issue 2, 2014, Pages 211-226

JAM-related proteins in mucosal homeostasis and inflammation

Author keywords

Inflammatory bowel disease; JAMs; Leukocyte trafficking; Tight junction

Indexed keywords

CD11B ANTIGEN; CD18 ANTIGEN; CD47 ANTIGEN; COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR LIKE MEMBRANE PROTEIN; HEPATOCYTE NUCLEAR FACTOR 4ALPHA; JUNCTIONAL ADHESION MOLECULE; JUNCTIONAL ADHESION MOLECULE A; JUNCTIONAL ADHESION MOLECULE C; PROTEIN CAR; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; TIGHT JUNCTION PROTEIN; UNCLASSIFIED DRUG; CELL ADHESION MOLECULE;

EID: 84899982143     PISSN: 18632297     EISSN: 18632300     Source Type: Journal    
DOI: 10.1007/s00281-014-0421-0     Document Type: Review
Times cited : (95)

References (184)
  • 1
    • 0024149641 scopus 로고
    • The immunoglobulin superfamily - Domains for cell surface recognition
    • Williams AF, Barclay AN (1988) The immunoglobulin superfamily - domains for cell surface recognition. Annu Rev Immunol 6: 381-405 (Pubitemid 19141589)
    • (1988) Annual Review of Immunology , vol.6 , pp. 381-405
    • Williams, A.F.1    Barclay, A.N.2
  • 2
    • 0032446820 scopus 로고    scopus 로고
    • A novel immunoglobulin superfamily junctional molecule expressed by antigen presenting cells, endothelial cells and platelets
    • DOI 10.1016/S0161-5890(98)00102-3, PII S0161589098001023
    • Malergue F, Galland F, Martin F, Mansuelle P, Aurrand-Lions M et al (1998) A novel immunoglobulin superfamily junctional molecule expressed by antigen presenting cells, endothelial cells and platelets. Mol Immunol 35:1111-1119 (Pubitemid 29057150)
    • (1998) Molecular Immunology , vol.35 , Issue.17 , pp. 1111-1119
    • Malergue, F.1    Galland, F.2    Martin, F.3    Mansuelle, P.4    Aurrand-Lions, M.5    Naquet, P.6
  • 4
    • 0034602185 scopus 로고    scopus 로고
    • A novel protein with homology to the junctional adhesion molecule. Characterization of leukocyte interactions
    • Cunningham SA, Arrate MP, Rodriguez JM, Bjercke RJ, Vanderslice P et al (2000) A novel protein with homology to the junctional adhesion molecule. Characterization of leukocyte interactions. J Biol Chem 275:34750-34756
    • (2000) J Biol Chem , vol.275 , pp. 34750-34756
    • Cunningham, S.A.1    Arrate, M.P.2    Rodriguez, J.M.3    Bjercke, R.J.4    Vanderslice, P.5
  • 5
    • 0034705379 scopus 로고    scopus 로고
    • Vascular endothelial junction-associated molecule, a novel member of the immunoglobulin superfamily, is localized to intercellular boundaries of endothelial cells
    • DOI 10.1074/jbc.M003189200
    • Palmeri D, van Zante A, Huang CC, Hemmerich S, Rosen SD (2000) Vascular endothelial junction-associated molecule, a novel member of the immunoglobulin superfamily, is localized to intercellular boundaries of endothelial cells. J Biol Chem 275:19139-19145 (Pubitemid 30422883)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.25 , pp. 19139-19145
    • Palmeri, D.1    Van Zante, A.2    Huang, C.-C.3    Hemmerich, S.4    Rosen, S.D.5
  • 6
    • 0035824527 scopus 로고    scopus 로고
    • Cloning of human junctional adhesion molecule 3 (JAM3) and its identification as the JAM2 counter-receptor
    • Arrate MP, Rodriguez JM, Tran TM, Brock TA, Cunningham SA (2001) Cloning of human junctional adhesion molecule 3 (JAM3) and its identification as the JAM2 counter-receptor. J Biol Chem 276:45826-45832
    • (2001) J Biol Chem , vol.276 , pp. 45826-45832
    • Arrate, M.P.1    Rodriguez, J.M.2    Tran, T.M.3    Brock, T.A.4    Cunningham, S.A.5
  • 7
    • 0035951873 scopus 로고    scopus 로고
    • JAM-2, a novel immunoglobulin superfamily molecule, expressed by endothelial and lymphatic cells
    • Aurrand-Lions M, Duncan L, Ballestrem C, Imhof BA (2001) JAM-2, a novel immunoglobulin superfamily molecule, expressed by endothelial and lymphatic cells. J Biol Chem 276:2733-2741
    • (2001) J Biol Chem , vol.276 , pp. 2733-2741
    • Aurrand-Lions, M.1    Duncan, L.2    Ballestrem, C.3    Imhof, B.A.4
  • 8
    • 0346025727 scopus 로고    scopus 로고
    • Junctional adhesion molecules (JAMs): More molecules with dual functions?
    • DOI 10.1242/jcs.00930
    • Ebnet K, Suzuki A, Ohno S, Vestweber D (2004) Junctional adhesion molecules (JAMs): more molecules with dual functions? J Cell Sci 117:19-29 (Pubitemid 38072117)
    • (2004) Journal of Cell Science , vol.117 , Issue.1 , pp. 19-29
    • Ebnet, K.1    Suzuki, A.2    Ohno, S.3    Vestweber, D.4
  • 9
    • 0037641234 scopus 로고    scopus 로고
    • JAM4, a junctional cell adhesion molecule interacting with a tight junction protein, MAGI-1
    • DOI 10.1128/MCB.23.12.4267-4282.2003
    • Hirabayashi S, Tajima M, Yao I, Nishimura W, Mori H et al (2003) JAM4, a junctional cell adhesion molecule interacting with a tight junction protein, MAGI-1. Mol Cell Biol 23:4267-4282 (Pubitemid 36666429)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.12 , pp. 4267-4282
    • Hirabayashi, S.1    Tajima, M.2    Yao, I.3    Nishimura, W.4    Mori, H.5    Hata, Y.6
  • 10
    • 0142245587 scopus 로고    scopus 로고
    • JAML, a novel protein with characteristics of a junctional adhesion molecule, is induced during differentiation of myeloid leukemia cells
    • DOI 10.1182/blood-2002-11-3462
    • Moog-Lutz C, Cave-Riant F, Guibal FC, Breau MA, Di Gioia Y et al (2003) JAML, a novel protein with characteristics of a junctional adhesion molecule, is induced during differentiation of myeloid leukemia cells. Blood 102:3371-3378 (Pubitemid 37314780)
    • (2003) Blood , vol.102 , Issue.9 , pp. 3371-3378
    • Moog-Lutz, C.1    Cave-Riant, F.2    Guibal, F.C.3    Breau, M.A.4    Di, G.Y.5    Olivier, C.P.6    Cayre, Y.E.7    Bourdoulous, S.8    Lutz, P.G.9
  • 12
    • 0347052858 scopus 로고    scopus 로고
    • CLMP, a Novel Member of the CTX Family and a New Component of Epithelial Tight Junctions
    • DOI 10.1074/jbc.M308249200
    • Raschperger E, Engstrom U, Pettersson RF, Fuxe J (2004) CLMP, a novelmember of the CTX family and a new component of epithelial tight junctions. J Biol Chem 279:796-804 (Pubitemid 38044886)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.1 , pp. 796-804
    • Raschperger, E.1    Engstrom, U.2    Pettersson, R.F.3    Fuxe, J.4
  • 13
    • 0035844164 scopus 로고    scopus 로고
    • Cloning of an immunoglobulin family adhesion molecule selectively expressed by endothelial cells
    • Hirata K, Ishida T, Penta K, RezaeeM, Yang E et al (2001) Cloning of an immunoglobulin family adhesion molecule selectively expressed by endothelial cells. J Biol Chem 276:16223-16231
    • (2001) J Biol Chem , vol.276 , pp. 16223-16231
    • Hirata, K.1    Ishida, T.2    Penta, K.3    Rezaee, M.4    Yang, E.5
  • 15
    • 38449112244 scopus 로고    scopus 로고
    • Junctional adhesionmolecules in angiogenesis
    • Naik TU, Naik MU, Naik UP (2008) Junctional adhesionmolecules in angiogenesis. Front Biosci 13:258-262
    • (2008) Front Biosci , vol.13 , pp. 258-262
    • Naik, T.U.1    Naik, M.U.2    Naik, U.P.3
  • 16
    • 79960756426 scopus 로고    scopus 로고
    • Pathobiology of junctional adhesion molecules
    • Bazzoni G (2011) Pathobiology of junctional adhesion molecules. Antioxid Redox Signal 15:1221-1234
    • (2011) Antioxid Redox Signal , vol.15 , pp. 1221-1234
    • Bazzoni, G.1
  • 19
    • 33748445496 scopus 로고    scopus 로고
    • Claudins-key pieces in the tight junction puzzle
    • Koval M (2006) Claudins-key pieces in the tight junction puzzle. Cell Commun Adhes 13:127-138
    • (2006) Cell Commun Adhes , vol.13 , pp. 127-138
    • Koval, M.1
  • 20
    • 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
    • DOI 10.1083/jcb.147.6.1351
    • Itoh M, Furuse M, Morita K, Kubota K, Saitou M et al (1999) Direct binding of three tight junction-associated MAGUKs, ZO-1, ZO-2, and ZO-3, with the COOH termini of claudins. J Cell Biol 147:1351-1363 (Pubitemid 30012818)
    • (1999) Journal of Cell Biology , vol.147 , Issue.6 , pp. 1351-1363
    • Itoh, M.1    Furuse, M.2    Morita, K.3    Kubota, K.4    Saitou, M.5    Tsukita, S.6
  • 21
    • 0032491391 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton
    • DOI 10.1074/jbc.273.45.29745
    • Fanning AS, Jameson BJ, Jesaitis LA, Anderson JM (1998) The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton. J Biol Chem 273:29745-29753 (Pubitemid 28509986)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.45 , pp. 29745-29753
    • Fanning, A.S.1    Jameson, B.J.2    Jesaitis, L.A.3    Anderson, J.M.4
  • 22
    • 33645963995 scopus 로고    scopus 로고
    • Claudins and epithelial paracellular transport
    • Van Itallie CM, Anderson JM (2006) Claudins and epithelial paracellular transport. Annu Rev Physiol 68:403-429
    • (2006) Annu Rev Physiol , vol.68 , pp. 403-429
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 23
    • 0033635344 scopus 로고    scopus 로고
    • Complex phenotype of mice lacking occludin, a component of tight junction strands
    • SaitouM, FuruseM, Sasaki H, Schulzke JD, FrommMet al (2000) Complex phenotype of mice lacking occludin, a component of tight junction strands. Mol Biol Cell 11:4131-4142
    • (2000) Mol Biol Cell , vol.11 , pp. 4131-4142
    • Saitou, M.1    Furuse, M.2    Sasaki, H.3    Schulzke, J.D.F.A.4
  • 25
    • 21744433348 scopus 로고    scopus 로고
    • The second loop of occludin is required for suppression of Raf1-induced tumor growth
    • DOI 10.1038/sj.onc.1208634
    • Wang Z, Mandell KJ, Parkos CA, Mrsny RJ, Nusrat A (2005) The second loop of occludin is required for suppression of Raf1-induced tumor growth. Oncogene 24:4412-4420 (Pubitemid 40961764)
    • (2005) Oncogene , vol.24 , Issue.27 , pp. 4412-4420
    • Wang, Z.1    Mandell, K.J.2    Parkos, C.A.3    Mrsny, R.J.4    Nusrat, A.5
  • 26
    • 0031047483 scopus 로고    scopus 로고
    • Synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier
    • DOI 10.1083/jcb.136.2.399
    • Wong V, Gumbiner BM (1997) A synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier. J Cell Biol 136:399-409 (Pubitemid 27063089)
    • (1997) Journal of Cell Biology , vol.136 , Issue.2 , pp. 399-409
    • Wong, V.1    Gumbiner, B.M.2
  • 27
    • 69849104698 scopus 로고    scopus 로고
    • Evidence for cross-reactivity of JAM-C antibodies: Implications for cellular localization studies
    • Betanzos A, Schnoor M, Severson EA, Liang TW, Parkos CA (2009) Evidence for cross-reactivity of JAM-C antibodies: implications for cellular localization studies. Biol Cell 101:441-453
    • (2009) Biol Cell , vol.101 , pp. 441-453
    • Betanzos, A.1    Schnoor, M.2    Severson, E.A.3    Liang, T.W.4    Parkos, C.A.5
  • 29
    • 0035817623 scopus 로고    scopus 로고
    • Junctional adhesion molecule (JAM) binds to PAR-3: A possible mechanism for the recruitment of PAR-3 to tight junctions
    • DOI 10.1083/jcb.200103047
    • Itoh M, Sasaki H, Furuse M, Ozaki H, Kita T et al (2001) Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions. J Cell Biol 154:491-497 (Pubitemid 34286156)
    • (2001) Journal of Cell Biology , vol.154 , Issue.3 , pp. 491-497
    • Itoh, M.1    Sasaki, H.2    Furuse, M.3    Ozaki, H.4    Kita, T.5    Tsukita, S.6
  • 30
    • 0032547833 scopus 로고    scopus 로고
    • A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts
    • DOI 10.1083/jcb.143.2.391
    • Furuse M, Sasaki H, Fujimoto K, Tsukita S (1998) A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts. J Cell Biol 143:391-401 (Pubitemid 28487858)
    • (1998) Journal of Cell Biology , vol.143 , Issue.2 , pp. 391-401
    • Furuse, M.1    Sasaki, H.2    Fujimoto, K.3    Tsukita, S.4
  • 31
    • 37549038994 scopus 로고    scopus 로고
    • JAM-A regulates permeability and inflammation in the intestine in vivo
    • Laukoetter MG, Nava P, Lee WY, Severson EA, Capaldo CT et al (2007) JAM-A regulates permeability and inflammation in the intestine in vivo. J Exp Med 204:3067-3076
    • (2007) J Exp Med , vol.204 , pp. 3067-3076
    • Laukoetter, M.G.1    Nava, P.2    Lee, W.Y.3    Severson, E.A.4    Capaldo, C.T.5
  • 35
    • 1942501686 scopus 로고    scopus 로고
    • Involvement of the Junctional Adhesion Molecule-1 (JAM1) Homodimer Interface in Regulation of Epithelial Barrier Function
    • DOI 10.1074/jbc.M309483200
    • Mandell KJ, McCall IC, Parkos CA (2004) Involvement of the junctional adhesion molecule-1 (JAM1) homodimer interface in regulation of epithelial barrier function. J Biol Chem 279:16254-16262 (Pubitemid 38509319)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.16 , pp. 16254-16262
    • Mandell, K.J.1    McCall, I.C.2    Parkos, C.A.3
  • 36
    • 35148839457 scopus 로고    scopus 로고
    • Expression of JAM-A in the human corneal endothelium and retinal pigment epithelium: Localization and evidence for role in barrier function
    • DOI 10.1167/iovs.06-1536
    • Mandell KJ, Berglin L, Severson EA, Edelhauser HF, Parkos CA (2007) Expression of JAM-Ain the human corneal endotheliumand retinal pigment epithelium: localization and evidence for role in barrier function. Invest Ophthalmol Vis Sci 48:3928-3936 (Pubitemid 351261011)
    • (2007) Investigative Ophthalmology and Visual Science , vol.48 , Issue.9 , pp. 3928-3936
    • Mandell, K.J.1    Berglin, L.2    Severson, E.A.3    Edelhauser, H.F.4    Parkos, C.A.5
  • 37
    • 33748592841 scopus 로고    scopus 로고
    • Junctional adhesion molecule-A participates in the formation of apico-basal polarity through different domains
    • DOI 10.1016/j.yexcr.2006.07.004, PII S0014482706002825
    • Rehder D, Iden S, Nasdala I, Wegener J, Brickwedde MK et al (2006) Junctional adhesion molecule-a participates in the formation of apico-basal polarity through different domains. Exp Cell Res 312:3389-3403 (Pubitemid 44380238)
    • (2006) Experimental Cell Research , vol.312 , Issue.17 , pp. 3389-3403
    • Rehder, D.1    Iden, S.2    Nasdala, I.3    Wegener, J.4    Brickwedde, M.-K.M.Z.5    Vestweber, D.6    Ebnet, K.7
  • 38
    • 0035898658 scopus 로고    scopus 로고
    • The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM)
    • DOI 10.1093/emboj/20.14.3738
    • Ebnet K, Suzuki A, Horikoshi Y, Hirose T, Meyer Zu Brickwedde MK et al (2001) The cell polarity protein ASIP/PAR-3 directly associates with junctional adhesion molecule (JAM). EMBO J 20: 3738-3748 (Pubitemid 32691785)
    • (2001) EMBO Journal , vol.20 , Issue.14 , pp. 3738-3748
    • Ebnet, K.1    Suzuki, A.2    Horikoshi, Y.3    Hirose, T.4    Meyer, Z.B.M.-K.5    Ohno, S.6    Vestweber, D.7
  • 39
    • 0037106581 scopus 로고    scopus 로고
    • aPKC kinase activity is required for the asymmetric differentiation of the premature junctional complex during epithelial cell polarization
    • Suzuki A, Ishiyama C, Hashiba K, Shimizu M, Ebnet K et al (2002) aPKC kinase activity is required for the asymmetric differentiation of the premature junctional complex during epithelial cell polarization. J Cell Sci 115:3565-3573
    • (2002) J Cell Sci , vol.115 , pp. 3565-3573
    • Suzuki, A.1    Ishiyama, C.2    Hashiba, K.3    Shimizu, M.4    Ebnet, K.5
  • 40
    • 84859965733 scopus 로고    scopus 로고
    • aPKC phosphorylates JAM-A at Ser285 to promote cell contact maturation and tight junction formation
    • Iden S, Misselwitz S, Peddibhotla SS, Tuncay H, Rehder D et al (2012) aPKC phosphorylates JAM-A at Ser285 to promote cell contact maturation and tight junction formation. J Cell Biol 196: 623-639
    • (2012) J Cell Biol , vol.196 , pp. 623-639
    • Iden, S.1    Misselwitz, S.2    Peddibhotla, S.S.3    Tuncay, H.4    Rehder, D.5
  • 41
    • 0039027605 scopus 로고    scopus 로고
    • Interaction of junctional adhesion molecule with the tight junction components ZO-1, cingulin, and occludin
    • DOI 10.1074/jbc.M905251199
    • Bazzoni G, Martinez-Estrada OM, Orsenigo F, Cordenonsi M, Citi S et al (2000) Interaction of junctional adhesion molecule with the tight junction components ZO-1, cingulin, and occludin. J Biol Chem 275:20520-20526 (Pubitemid 30457633)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.27 , pp. 20520-20526
    • Bazzoni, G.1    Martinez-Estrada, O.M.2    Orsenigo, F.3    Cordenonsi, M.4    Citi, S.5    Dejana, E.6
  • 42
    • 84884469619 scopus 로고    scopus 로고
    • JAM-A associates with ZO-2, afadin, and PDZ-GEF1 to activate Rap2c and regulate epithelial barrier function
    • Monteiro AC, Sumagin R, Rankin CR, Leoni G, Mina MJ et al (2013) JAM-A associates with ZO-2, afadin, and PDZ-GEF1 to activate Rap2c and regulate epithelial barrier function. Mol Biol Cell 24:2849-2860
    • (2013) Mol Biol Cell , vol.24 , pp. 2849-2860
    • Monteiro, A.C.1    Sumagin, R.2    Rankin, C.R.3    Leoni, G.4    Mina, M.J.5
  • 43
    • 83355174042 scopus 로고    scopus 로고
    • The Src homology 3 domain is required for junctional adhesion molecule binding to the third PDZ domain of the scaffolding protein ZO-1
    • Nomme J, Fanning AS, Caffrey M, Lye MF, Anderson JM et al (2011) The Src homology 3 domain is required for junctional adhesion molecule binding to the third PDZ domain of the scaffolding protein ZO-1. J Biol Chem 286:43352-43360
    • (2011) J Biol Chem , vol.286 , pp. 43352-43360
    • Nomme, J.1    Fanning, A.S.2    Caffrey, M.3    Lye, M.F.4    Anderson, J.M.5
  • 44
    • 0034623082 scopus 로고    scopus 로고
    • Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1
    • Ebnet K, Schulz CU, Meyer Zu Brickwedde MK, Pendl GG, Vestweber D (2000) Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1. J Biol Chem 275:27979-27988
    • (2000) J Biol Chem , vol.275 , pp. 27979-27988
    • Ebnet, K.1    Schulz, C.U.2    Meyer Zu Brickwedde, M.K.3    Pendl, G.G.4    Vestweber, D.5
  • 45
    • 65249125248 scopus 로고    scopus 로고
    • Junctional adhesion molecule A interacts with Afadin and PDZGEF2 to activate Rap1A, regulate beta1 integrin levels, and enhance cell migration
    • Severson EA, Lee WY, Capaldo CT, Nusrat A, Parkos CA (2009) Junctional adhesion molecule A interacts with Afadin and PDZGEF2 to activate Rap1A, regulate beta1 integrin levels, and enhance cell migration. Mol Biol Cell 20:1916-1925
    • (2009) Mol Biol Cell , vol.20 , pp. 1916-1925
    • Severson, E.A.1    Lee, W.Y.2    Capaldo, C.T.3    Nusrat, A.4    Parkos, C.A.5
  • 46
    • 0037016668 scopus 로고    scopus 로고
    • Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule
    • DOI 10.1074/jbc.M109005200
    • Hamazaki Y, Itoh M, Sasaki H, Furuse M, Tsukita S (2002) Multi-PDZ domain protein 1 (MUPP1) is concentrated at tight junctions through its possible interaction with claudin-1 and junctional adhesion molecule. J Biol Chem 277:455-461 (Pubitemid 34952079)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.1 , pp. 455-461
    • Hamazaki, Y.1    Itoh, M.2    Sasaki, H.3    Furuse, M.4    Tsukita, S.5
  • 47
    • 0035937810 scopus 로고    scopus 로고
    • Association of junctional adhesion molecule with calcium/calmodulin- dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells
    • Martinez-Estrada OM, Villa A, Breviario F, Orsenigo F, Dejana E et al (2001) Association of junctional adhesion molecule with calcium/calmodulin- dependent serine protein kinase (CASK/LIN-2) in human epithelial caco-2 cells. J Biol Chem 276:9291-9296
    • (2001) J Biol Chem , vol.276 , pp. 9291-9296
    • Martinez-Estrada, O.M.1    Villa, A.2    Breviario, F.3    Orsenigo, F.4    Dejana, E.5
  • 48
    • 77957278004 scopus 로고    scopus 로고
    • Cytoskeletal regulation of epithelial barrier function during inflammation
    • Ivanov AI, Parkos CA, Nusrat A (2010) Cytoskeletal regulation of epithelial barrier function during inflammation. Am J Pathol 177: 512-524
    • (2010) Am J Pathol , vol.177 , pp. 512-524
    • Ivanov, A.I.1    Parkos, C.A.2    Nusrat, A.3
  • 49
    • 69949168324 scopus 로고    scopus 로고
    • Regulation by afadin of cyclical activation and inactivation of Rap1, Rac1, and RhoA small G proteins at leading edges of moving NIH3T3 cells
    • Miyata M, Rikitake Y, Takahashi M, Nagamatsu Y, Yamauchi Y et al (2009) Regulation by afadin of cyclical activation and inactivation of Rap1, Rac1, and RhoA small G proteins at leading edges of moving NIH3T3 cells. J Biol Chem 284:24595-24609
    • (2009) J Biol Chem , vol.284 , pp. 24595-24609
    • Miyata, M.1    Rikitake, Y.2    Takahashi, M.3    Nagamatsu, Y.4    Yamauchi, Y.5
  • 50
    • 79960329217 scopus 로고    scopus 로고
    • Involvement of afadin in barrier function and homeostasis of mouse intestinal epithelia
    • Tanaka-Okamoto M, Hori K, Ishizaki H, Itoh Y, Onishi S et al (2011) Involvement of afadin in barrier function and homeostasis of mouse intestinal epithelia. J Cell Sci 124:2231-2240
    • (2011) J Cell Sci , vol.124 , pp. 2231-2240
    • Tanaka-Okamoto, M.1    Hori, K.2    Ishizaki, H.3    Itoh, Y.4    Onishi, S.5
  • 52
    • 0037621983 scopus 로고    scopus 로고
    • Hepatocyte nuclear factor (HNF)-4alpha triggers formation of functional tight junctions and establishment of polarized epithelial morphology in F9 embryonal carcinoma cells
    • DOI 10.1016/S0014-4827(03)00116-2
    • Chiba H, Gotoh T, Kojima T, Satohisa S, Kikuchi K et al (2003) Hepatocyte nuclear factor (HNF)-4alpha triggers formation of functional tight junctions and establishment of polarized epithelial morphology in F9 embryonal carcinoma cells. Exp Cell Res 286:288-297 (Pubitemid 36566441)
    • (2003) Experimental Cell Research , vol.286 , Issue.2 , pp. 288-297
    • Chiba, H.1    Gotoh, T.2    Kojima, T.3    Satohisa, S.4    Kikuchi, K.5    Osanai, M.6    Sawada, N.7
  • 53
    • 70449585192 scopus 로고    scopus 로고
    • Loss of hepatocyte-nuclear-factor-4alpha affects colonic ion transport and causes chronic inflammation resembling inflammatory bowel disease in mice
    • Darsigny M, Babeu JP, Dupuis AA, Furth EE, Seidman EG et al (2009) Loss of hepatocyte-nuclear-factor-4alpha affects colonic ion transport and causes chronic inflammation resembling inflammatory bowel disease in mice. PLoS One 4:e7609
    • (2009) PLoS One , vol.4
    • Darsigny, M.1    Babeu, J.P.2    Dupuis, A.A.3    Furth, E.E.4    Seidman, E.G.5
  • 54
    • 25844464135 scopus 로고    scopus 로고
    • Behavior of tight-junction, adherens-junction and cell polarity proteins during HNF-4alpha-induced epithelial polarization
    • DOI 10.1016/j.yexcr.2005.06.025, PII S0014482705003253
    • Satohisa S, Chiba H, Osanai M, Ohno S, Kojima T et al (2005) Behavior of tight-junction, adherens-junction and cell polarity proteins during HNF-4alpha-induced epithelial polarization. Exp Cell Res 310:66-78 (Pubitemid 41393688)
    • (2005) Experimental Cell Research , vol.310 , Issue.1 , pp. 66-78
    • Satohisa, S.1    Chiba, H.2    Osanai, M.3    Ohno, S.4    Kojima, T.5    Saito, T.6    Sawada, N.7
  • 55
    • 0141635242 scopus 로고    scopus 로고
    • Roles of immunoglobulin-like loops of junctional cell adhesion molecule 4; involvement in the subcellular localization and the cell adhesion
    • DOI 10.1046/j.1365-2443.2003.00673.x
    • TajimaM, Hirabayashi S, Yao I, Shirasawa M, Osuga J et al (2003) Roles of immunoglobulin-like loops of junctional cell adhesion molecule 4; involvement in the subcellular localization and the cell adhesion. Genes Cells 8:759-768 (Pubitemid 37121564)
    • (2003) Genes to Cells , vol.8 , Issue.9 , pp. 759-768
    • Tajima, M.1    Hirabayashi, S.2    Yao, I.3    Shirasawa, M.4    Osuga, J.5    Ishibashi, S.6    Fujita, T.7    Hata, Y.8
  • 59
    • 9144243706 scopus 로고    scopus 로고
    • The coxsackievirus and adenovirus receptor interacts with the multi-PDZ domain protein-1 (MUPP-1) within the tight junction
    • DOI 10.1074/jbc.M409061200
    • Coyne CB, Voelker T, Pichla SL, Bergelson JM (2004) The Coxsackievirus and adenovirus receptor interacts with the multi-PDZ domain protein-1 (MUPP-1) within the tight junction. J Biol Chem 279:48079-48084 (Pubitemid 39540961)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.46 , pp. 48079-48084
    • Coyne, C.B.1    Voelker, T.2    Pichla, S.L.3    Bergelson, J.M.4
  • 60
    • 33646153988 scopus 로고    scopus 로고
    • The coxsackie- and adenovirus receptor (CAR) is an in vivo marker for epithelial tight junctions, with a potential role in regulating permeability and tissue homeostasis
    • Raschperger E, Thyberg J, Pettersson S, Philipson L, Fuxe J et al (2006) The coxsackie- and adenovirus receptor (CAR) is an in vivo marker for epithelial tight junctions, with a potential role in regulating permeability and tissue homeostasis. Exp Cell Res 312:1566-1580
    • (2006) Exp Cell Res , vol.312 , pp. 1566-1580
    • Raschperger, E.1    Thyberg, J.2    Pettersson, S.3    Philipson, L.4    Fuxe, J.5
  • 61
  • 62
    • 77649108637 scopus 로고    scopus 로고
    • The Coxsackievirus - adenovirus receptor reveals complex homophilic and heterophilic interactions on neural cells
    • Patzke C, Max KE, Behlke J, Schreiber J, Schmidt H et al (2010) The Coxsackievirus - adenovirus receptor reveals complex homophilic and heterophilic interactions on neural cells. J Neurosci 30:2897-2910
    • (2010) J Neurosci , vol.30 , pp. 2897-2910
    • Patzke, C.1    Max, K.E.2    Behlke, J.3    Schreiber, J.4    Schmidt, H.5
  • 63
    • 0034435587 scopus 로고    scopus 로고
    • Dimeric structure of the coxsackievirus and adenovirus receptor D1 domain at 1.7 A resolution
    • DOI 10.1016/S0969-2126(00)00528-1, PII S0969212600005281
    • van Raaij MJ, Chouin E, van der Zandt H, Bergelson JM, Cusack S (2000) Dimeric structure of the Coxsackievirus and adenovirus receptor D1 domain at 1.7 A resolution. Structure 8:1147-1155 (Pubitemid 32667480)
    • (2000) Structure , vol.8 , Issue.11 , pp. 1147-1155
    • Van Raaij, M.J.1    Chouin, E.2    Van Der, Z.H.3    Bergelson, J.M.4    Cusack, S.5
  • 64
    • 79961139374 scopus 로고    scopus 로고
    • CAR modulates E-cadherin dynamics in the presence of adenovirus type 5
    • Hussain F, Morton PE, Snippe M, Sullivan J, Farmer C et al (2011) CAR modulates E-cadherin dynamics in the presence of adenovirus type 5. PLoS One 6:e23056
    • (2011) PLoS One , vol.6
    • Hussain, F.1    Morton, P.E.2    Snippe, M.3    Sullivan, J.4    Farmer, C.5
  • 65
    • 84885369037 scopus 로고    scopus 로고
    • CAR regulates epithelial cell junction stability through control of Ecadherin trafficking
    • Morton PE, Hicks A, Nastos T, Santis G, Parsons M (2013) CAR regulates epithelial cell junction stability through control of Ecadherin trafficking. Sci Rep 3:2889
    • (2013) Sci Rep , vol.3 , pp. 2889
    • Morton, P.E.1    Hicks, A.2    Nastos, T.3    Santis, G.4    Parsons, M.5
  • 66
    • 79958063088 scopus 로고    scopus 로고
    • Multiple phenotypes in adult mice following inactivation of the Coxsackievirus and adenovirus receptor (Car) gene
    • Pazirandeh A, Sultana T, Mirza M, Rozell B, Hultenby K et al (2011) Multiple phenotypes in adult mice following inactivation of the Coxsackievirus and adenovirus receptor (Car) gene. PLoS One 6:1-6
    • (2011) PLoS One , vol.6 , pp. 1-6
    • Pazirandeh, A.1    Sultana, T.2    Mirza, M.3    Rozell, B.4    Hultenby, K.5
  • 67
    • 84857636412 scopus 로고    scopus 로고
    • CLMP is required for intestinal development, and loss-of-function mutations cause congenital short-bowel syndrome
    • Van Der Werf CS, Wabbersen TD, Hsiao NH, Paredes J, Etchevers HC et al (2012) CLMP is required for intestinal development, and loss-of-function mutations cause congenital short-bowel syndrome. Gastroenterology 142(453-462):e453
    • (2012) Gastroenterology , vol.142 , Issue.453-462
    • Van Der Werf, C.S.1    Wabbersen, T.D.2    Hsiao, N.H.3    Paredes, J.4    Etchevers, H.C.5
  • 68
    • 44349132270 scopus 로고    scopus 로고
    • Epithelial-cell recognition of commensal bacteria and maintenance of immune homeostasis in the gut
    • Artis D (2008) Epithelial-cell recognition of commensal bacteria and maintenance of immune homeostasis in the gut. Nat Rev Immunol 8:411-420
    • (2008) Nat Rev Immunol , vol.8 , pp. 411-420
    • Artis, D.1
  • 69
    • 77649086402 scopus 로고    scopus 로고
    • Immune adaptations that maintain homeostasis with the intestinal microbiota
    • Hooper LV, Macpherson AJ (2010) Immune adaptations that maintain homeostasis with the intestinal microbiota. Nat Rev Immunol 10:159-169
    • (2010) Nat Rev Immunol , vol.10 , pp. 159-169
    • Hooper, L.V.1    Macpherson, A.J.2
  • 70
    • 34548230927 scopus 로고    scopus 로고
    • Getting to the site of inflammation: The leukocyte adhesion cascade updated
    • DOI 10.1038/nri2156, PII NRI2156
    • Ley K, Laudanna C, Cybulsky MI, Nourshargh S (2007) Getting to the site of inflammation: the leukocyte adhesion cascade updated. Nat Rev Immunol 7:678-689 (Pubitemid 47327397)
    • (2007) Nature Reviews Immunology , vol.7 , Issue.9 , pp. 678-689
    • Ley, K.1    Laudanna, C.2    Cybulsky, M.I.3    Nourshargh, S.4
  • 71
    • 0035895050 scopus 로고    scopus 로고
    • Heterogeneity of endothelial junctions is reflected by differential expression and specific subcellular localization of the three JAM family members
    • Aurrand-Lions M, Johnson-Leger C, Wong C, Du Pasquier L, Imhof BA (2001) Heterogeneity of endothelial junctions is reflected by differential expression and specific subcellular localization of the three JAM family members. Blood 98:3699-3707
    • (2001) Blood , vol.98 , pp. 3699-3707
    • Aurrand-Lions, M.1    Johnson-Leger, C.2    Wong, C.3    Du Pasquier, L.4    Imhof, B.A.5
  • 72
    • 0032813563 scopus 로고    scopus 로고
    • Expression of the coxsackievirus and adenovirus receptor in cultured human umbilical vein endothelial cells: Regulation in response to cell density
    • Carson SD, Hobbs JT, Tracy SM, Chapman NM(1999) Expression of the Coxsackievirus and adenovirus receptor in cultured human umbilical vein endothelial cells: regulation in response to cell density. J Virol 73:7077-7079 (Pubitemid 29327898)
    • (1999) Journal of Virology , vol.73 , Issue.8 , pp. 7077-7079
    • Carson, S.D.1    Hobbs, J.T.2    Tracy, S.M.3    Chapman, N.M.4
  • 73
    • 1842632667 scopus 로고    scopus 로고
    • Endothelial cell-cell junctions: Happy together
    • Dejana E (2004) Endothelial cell-cell junctions: happy together. Nat Rev Mol Cell Biol 5:261-270
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 261-270
    • Dejana, E.1
  • 75
    • 4644245292 scopus 로고    scopus 로고
    • Endothelial adhesion molecule ESAM binds directly to the multidomain adaptor MAGI-1 and recruits it to cell contacts
    • DOI 10.1016/j.yexcr.2004.07.010, PII S0014482704003908
    • Wegmann F, Ebnet K, Du Pasquier L, Vestweber D, Butz S (2004) Endothelial adhesion molecule ESAM binds directly to the multidomain adaptor MAGI-1 and recruits it to cell contacts. Exp Cell Res 300:121-133 (Pubitemid 39286222)
    • (2004) Experimental Cell Research , vol.300 , Issue.1 , pp. 121-133
    • Wegmann, F.1    Ebnet, K.2    Du, P.L.3    Vestweber, D.4    Butz, S.5
  • 76
    • 0033565947 scopus 로고    scopus 로고
    • Cutting edge: Combined treatment of TNF-alpha and IFN-gamma causes redistribution of junctional adhesion molecule in human endothelial cells
    • Ozaki H, Ishii K, Horiuchi H, Arai H, Kawamoto T et al (1999) Cutting edge: combined treatment of TNF-alpha and IFN-gamma causes redistribution of junctional adhesion molecule in human endothelial cells. J Immunol 163:553-557 (Pubitemid 29328054)
    • (1999) Journal of Immunology , vol.163 , Issue.2 , pp. 553-557
    • Ozaki, H.1    Ishii, K.2    Horiuchi, H.3    Arai, H.4    Kawamoto, T.5    Okawa, K.6    Iwamatsu, A.7    Kita, T.8
  • 77
    • 8444229240 scopus 로고    scopus 로고
    • 2 integrin lymphocyte function-associated antigen-1 with junctional adhesion molecule-A is mediated by the I domain
    • Fraemohs L, Koenen RR, Ostermann G, Heinemann B, Weber C (2004) The functional interaction of the beta 2 integrin lymphocyte function-associated antigen-1 with junctional adhesion molecule-A is mediated by the I domain. J Immunol 173:6259-6264 (Pubitemid 39487784)
    • (2004) Journal of Immunology , vol.173 , Issue.10 , pp. 6259-6264
    • Fraemohs, L.1    Koenen, R.R.2    Ostermann, G.3    Heinemann, B.4    Weber, C.5
  • 78
    • 0036008013 scopus 로고    scopus 로고
    • 2 integrin LFA-I involved in transendothelial migration of leukocytes
    • DOI 10.1038/ni755
    • Ostermann G,Weber KS, Zernecke A, Schroder A,Weber C (2002) JAM-1 is a ligand of the beta(2) integrin LFA-1 involved in transendothelial migration of leukocytes. Nat Immunol 3:151-158 (Pubitemid 34141445)
    • (2002) Nature Immunology , vol.3 , Issue.2 , pp. 151-158
    • Ostermann, G.1    Weber, K.S.C.2    Zernecke, A.3    Schroder, A.4    Weber, C.5
  • 79
    • 58849161367 scopus 로고    scopus 로고
    • LFA-1 binding destabilizes the JAM-A homophilic interaction during leukocyte transmigration
    • Wojcikiewicz EP, Koenen RR, Fraemohs L, Minkiewicz J, Azad H et al (2009) LFA-1 binding destabilizes the JAM-A homophilic interaction during leukocyte transmigration. Biophys J 96:285-293
    • (2009) Biophys J , vol.96 , pp. 285-293
    • Wojcikiewicz, E.P.1    Koenen, R.R.2    Fraemohs, L.3    Minkiewicz, J.4    Azad, H.5
  • 82
    • 22144433384 scopus 로고    scopus 로고
    • Junctional adhesion molecule-A deficiency increases hepatic ischemia-reperfusion injury despite reduction of neutrophil transendothelial migration
    • DOI 10.1182/blood-2004-11-4416
    • Khandoga A, Kessler JS, Meissner H, Hanschen M, CoradaM et al (2005) Junctional adhesion molecule-A deficiency increases hepatic ischemia - reperfusion injury despite reduction of neutrophil transendothelial migration. Blood 106:725-733 (Pubitemid 40981273)
    • (2005) Blood , vol.106 , Issue.2 , pp. 725-733
    • Khandoga, A.1    Kessler, J.S.2    Meissner, H.3    Hanschen, M.4    Corada, M.5    Motoike, T.6    Enders, G.7    Dejana, E.8    Krombach, F.9
  • 83
    • 34548825638 scopus 로고    scopus 로고
    • JAM-A mediates neutrophil transmigration in a stimulus-specific manner in vivo: Evidence for sequential roles for JAM-A and PECAM-1 in neutrophil transmigration
    • DOI 10.1182/blood-2006-09-047431
    • Woodfin A, Reichel CA, Khandoga A, Corada M, Voisin MB et al (2007) JAM-A mediates neutrophil transmigration in a stimulusspecific manner in vivo: evidence for sequential roles for JAM-A and PECAM-1 in neutrophil transmigration. Blood 110:1848-1856 (Pubitemid 47443896)
    • (2007) Blood , vol.110 , Issue.6 , pp. 1848-1856
    • Woodfin, A.1    Reichel, C.A.2    Khandoga, A.3    Corada, M.4    Voisin, M.-B.5    Scheiermann, C.6    Haskard, D.O.7    Dejana, E.8    Krombach, F.9    Nourshargh, S.10
  • 84
    • 67650413623 scopus 로고    scopus 로고
    • Endothelial cell activation leads to neutrophil transmigration as supported by the sequential roles of ICAM-2, JAM-A, and PECAM-1
    • Woodfin A, Voisin MB, Imhof BA, Dejana E, Engelhardt B et al (2009) Endothelial cell activation leads to neutrophil transmigration as supported by the sequential roles of ICAM-2, JAM-A, and PECAM-1. Blood 113:6246-6257
    • (2009) Blood , vol.113 , pp. 6246-6257
    • Woodfin, A.1    Voisin, M.B.2    Imhof, B.A.3    Dejana, E.4    Engelhardt, B.5
  • 85
    • 61949276292 scopus 로고    scopus 로고
    • JAM-A promotes neutrophil chemotaxis by controlling integrin internalization and recycling
    • Cera MR, Fabbri M, Molendini C, Corada M, Orsenigo F et al (2009) JAM-A promotes neutrophil chemotaxis by controlling integrin internalization and recycling. J Cell Sci 122:268-277
    • (2009) J Cell Sci , vol.122 , pp. 268-277
    • Cera, M.R.1    Fabbri, M.2    Molendini, C.3    Corada, M.4    Orsenigo, F.5
  • 90
    • 33644795491 scopus 로고    scopus 로고
    • Junctional adhesion molecules (JAM)-B and -C contribute to leukocyte extravasation to the skin and mediate cutaneous inflammation
    • Ludwig RJ, Zollner TM, Santoso S, Hardt K, Gille J et al (2005) Junctional adhesion molecules (JAM)-B and -C contribute to leukocyte extravasation to the skin and mediate cutaneous inflammation. J Invest Dermatol 125:969-976
    • (2005) J Invest Dermatol , vol.125 , pp. 969-976
    • Ludwig, R.J.1    Zollner, T.M.2    Santoso, S.3    Hardt, K.4    Gille, J.5
  • 91
    • 69949112052 scopus 로고    scopus 로고
    • Junctional adhesion molecule (JAM)-B supports lymphocyte rolling and adhesion through interaction with alpha4beta1 integrin
    • Ludwig RJ, Hardt K, Hatting M, Bistrian R, Diehl S et al (2009) Junctional adhesion molecule (JAM)-B supports lymphocyte rolling and adhesion through interaction with alpha4beta1 integrin. Immunology 128:196-205
    • (2009) Immunology , vol.128 , pp. 196-205
    • Ludwig, R.J.1    Hardt, K.2    Hatting, M.3    Bistrian, R.4    Diehl, S.5
  • 96
    • 0036785376 scopus 로고    scopus 로고
    • Junctional adhesion molecule-2 (JAM-2) promotes lymphocyte transendothelial migration
    • Johnson-Leger CA, Aurrand-Lions M, Beltraminelli N, Fasel N, Imhof BA (2002) Junctional adhesion molecule-2 (JAM-2) promotes lymphocyte transendothelial migration. Blood 100:2479-2486
    • (2002) Blood , vol.100 , pp. 2479-2486
    • Johnson-Leger, C.A.1    Aurrand-Lions, M.2    Beltraminelli, N.3    Fasel, N.4    Imhof, B.A.5
  • 97
    • 70349567942 scopus 로고    scopus 로고
    • Junctional adhesion molecule-C mediates leukocyte infiltration in response to ischemia reperfusion injury
    • Scheiermann C, Colom B, Meda P, Patel NS, Voisin MB et al (2009) Junctional adhesion molecule-C mediates leukocyte infiltration in response to ischemia reperfusion injury. Arterioscler Thromb Vasc Biol 29:1509-1515
    • (2009) Arterioscler Thromb Vasc Biol , vol.29 , pp. 1509-1515
    • Scheiermann, C.1    Colom, B.2    Meda, P.3    Patel, N.S.4    Voisin, M.B.5
  • 100
    • 80052026271 scopus 로고    scopus 로고
    • The junctional adhesion molecule JAM-C regulates polarized transendothelial migration of neutrophils in vivo
    • Woodfin A, Voisin MB, Beyrau M, Colom B, Caille D et al (2011) The junctional adhesion molecule JAM-C regulates polarized transendothelial migration of neutrophils in vivo. Nat Immunol 12:761-769
    • (2011) Nat Immunol , vol.12 , pp. 761-769
    • Woodfin, A.1    Voisin, M.B.2    Beyrau, M.3    Colom, B.4    Caille, D.5
  • 101
    • 33751546663 scopus 로고    scopus 로고
    • Junctional adhesion molecule-C regulates vascular endothelial permeability by modulating VE-cadherin-mediated cell-cell contacts
    • DOI 10.1084/jem.20051730
    • Orlova VV, Economopoulou M, Lupu F, Santoso S, Chavakis T (2006) Junctional adhesion molecule-C regulates vascular endothelial permeability by modulating VE-cadherin-mediated cell-cell contacts. J Exp Med 203:2703-2714 (Pubitemid 44833346)
    • (2006) Journal of Experimental Medicine , vol.203 , Issue.12 , pp. 2703-2714
    • Orlova, V.V.1    Economopoulou, M.2    Lupu, F.3    Santoso, S.4    Chavakis, T.5
  • 102
    • 61749083594 scopus 로고    scopus 로고
    • Leukocyte transmigration in inflamed liver: A role for endothelial cell-selective adhesion molecule
    • Khandoga A, Huettinger S, Khandoga AG, Li H, Butz S et al (2009) Leukocyte transmigration in inflamed liver: a role for endothelial cell-selective adhesion molecule. J Hepatol 50:755-765
    • (2009) J Hepatol , vol.50 , pp. 755-765
    • Khandoga, A.1    Huettinger, S.2    Khandoga, A.G.3    Li, H.4    Butz, S.5
  • 104
    • 77955430489 scopus 로고    scopus 로고
    • Endothelial cell-selective adhesion molecule modulates atherosclerosis through plaque angiogenesis and monocyte-endothelial interaction
    • Inoue M, Ishida T, Yasuda T, Toh R, Hara Tet al (2010) Endothelial cell-selective adhesion molecule modulates atherosclerosis through plaque angiogenesis and monocyte-endothelial interaction. Microvasc Res 80:179-187
    • (2010) Microvasc Res , vol.80 , pp. 179-187
    • Inoue, M.1    Ishida, T.2    Yasuda, T.3    Toh, R.4    Hara, T.5
  • 105
    • 64049085727 scopus 로고    scopus 로고
    • Endothelial cell-selective adhesion molecule regulates albuminuria in diabetic nephropathy
    • Hara T, Ishida T, Cangara HM, Hirata K (2009) Endothelial cell-selective adhesion molecule regulates albuminuria in diabetic nephropathy. Microvasc Res 77:348-355
    • (2009) Microvasc Res , vol.77 , pp. 348-355
    • Hara, T.1    Ishida, T.2    Cangara, H.M.3    Hirata, K.4
  • 106
    • 58249090536 scopus 로고    scopus 로고
    • JAM-L-mediated leukocyte adhesion to endothelial cells is regulated in cis by alpha4beta1 integrin activation
    • Luissint AC, Lutz PG, Calderwood DA, Couraud PO, Bourdoulous S (2008) JAM-L-mediated leukocyte adhesion to endothelial cells is regulated in cis by alpha4beta1 integrin activation. J Cell Biol 183: 1159-1173
    • (2008) J Cell Biol , vol.183 , pp. 1159-1173
    • Luissint, A.C.1    Lutz, P.G.2    Calderwood, D.A.3    Couraud, P.O.4    Bourdoulous, S.5
  • 107
    • 3242656311 scopus 로고    scopus 로고
    • Cytokine-mediated downregulation of coxsackievirus-adenovirus receptor in endothelial cells
    • DOI 10.1128/JVI.78.15.8047-8058.2004
    • Vincent T, Pettersson RF, Crystal RG, Leopold PL (2004) Cytokine-mediated downregulation of Coxsackievirus-adenovirus receptor in endothelial cells. J Virol 78:8047-8058 (Pubitemid 38944289)
    • (2004) Journal of Virology , vol.78 , Issue.15 , pp. 8047-8058
    • Vincent, T.1    Pettersson, R.F.2    Crystal, R.G.3    Leopold, P.L.4
  • 108
    • 58849114504 scopus 로고    scopus 로고
    • Role of junctional adhesion molecule-like protein in mediating monocyte transendothelial migration
    • Guo YL, Bai R, Chen CX, Liu DQ, Liu Y et al (2009) Role of junctional adhesion molecule-like protein in mediating monocyte transendothelial migration. Arterioscler Thromb Vasc Biol 29:75-83
    • (2009) Arterioscler Thromb Vasc Biol , vol.29 , pp. 75-83
    • Guo, Y.L.1    Bai, R.2    Chen, C.X.3    Liu, D.Q.4    Liu, Y.5
  • 109
    • 33644895026 scopus 로고    scopus 로고
    • Coxsackievirus and adenovirus receptor (CAR) is expressed inmale germ cells and forms a complex with the differentiation factor JAMC in mouse testis
    • Mirza M, Hreinsson J, Strand ML, Hovatta O, Soder O et al (2006) Coxsackievirus and adenovirus receptor (CAR) is expressed inmale germ cells and forms a complex with the differentiation factor JAMC in mouse testis. Exp Cell Res 312:817-830
    • (2006) Exp Cell Res , vol.312 , pp. 817-830
    • Mirza, M.1    Hreinsson, J.2    Strand, M.L.3    Hovatta, O.4    Soder, O.5
  • 110
    • 84862097767 scopus 로고    scopus 로고
    • Essential role of the coxsackie- and adenovirus receptor (CAR) in development of the lymphatic system in mice
    • Mirza M, Pang MF, Zaini MA, Haiko P, Tammela T et al (2012) Essential role of the coxsackie- and adenovirus receptor (CAR) in development of the lymphatic system in mice. PLoS One 7:e37523
    • (2012) PLoS One , vol.7
    • Mirza, M.1    Pang, M.F.2    Zaini, M.A.3    Haiko, P.4    Tammela, T.5
  • 111
    • 0025723465 scopus 로고
    • Neutrophil migration across a cultured intestinal epithelium. Dependence on a CD11b/CD18-mediated event and enhanced efficiency in physiological direction
    • Parkos CA, Delp C, Arnaout MA, Madara JL (1991) Neutrophil migration across a cultured intestinal epithelium. Dependence on a CD11b/CD18-mediated event and enhanced efficiency in physiological direction. J Clin Invest 88:1605-1612
    • (1991) J Clin Invest , vol.88 , pp. 1605-1612
    • Parkos, C.A.1    Delp, C.2    Arnaout, M.A.3    Madara, J.L.4
  • 112
    • 0036839560 scopus 로고    scopus 로고
    • CD11b/CD18-dependent interactions of neutrophils with intestinal epithelium are mediated by fucosylated proteoglycans
    • Zen K, Liu Y, Cairo D, Parkos CA (2002) CD11b/CD18-dependent interactions of neutrophils with intestinal epithelium are mediated by fucosylated proteoglycans. J Immunol 169:5270-5278 (Pubitemid 35217199)
    • (2002) Journal of Immunology , vol.169 , Issue.9 , pp. 5270-5278
    • Zen, K.1    Liu, Y.2    Cairo, D.3    Parkos, C.A.4
  • 113
    • 0037078334 scopus 로고    scopus 로고
    • An intracellular signaling hierarchy determines direction of migration in opposing chemotactic gradients
    • DOI 10.1083/jcb.200202114
    • Heit B, Tavener S, Raharjo E, Kubes P (2002) An intracellular signaling hierarchy determines direction of migration in opposing chemotactic gradients. J Cell Biol 159:91-102 (Pubitemid 35191521)
    • (2002) Journal of Cell Biology , vol.159 , Issue.1 , pp. 91-102
    • Heit, B.1    Tavener, S.2    Raharjo, E.3    Kubes, P.4
  • 114
  • 115
    • 0026520089 scopus 로고
    • Leukocyte adhesion deficiency: Clinical and postmortem observations
    • Hawkins HK, Heffelfinger SC, Anderson DC (1992) Leukocyte adhesion deficiency: clinical and postmortem observations. Pediatr Pathol 12:119-130
    • (1992) Pediatr Pathol , vol.12 , pp. 119-130
    • Hawkins, H.K.1    Heffelfinger, S.C.2    Anderson, D.C.3
  • 116
    • 78649684951 scopus 로고    scopus 로고
    • The role of cis dimerization of signal regulatory protein alpha (SIRPalpha) in binding to CD47
    • Lee WY, Weber DA, Laur O, Stowell SR, McCall I et al (2010) The role of cis dimerization of signal regulatory protein alpha (SIRPalpha) in binding to CD47. J Biol Chem 285:37953-37963
    • (2010) J Biol Chem , vol.285 , pp. 37953-37963
    • Lee, W.Y.1    Weber, D.A.2    Laur, O.3    Stowell, S.R.4    McCall, I.5
  • 117
    • 0035955676 scopus 로고    scopus 로고
    • The role of CD47 in neutrophil transmigration. Increased rate of migration correlates with increased cell surface expression of CD47
    • Liu Y, Merlin D, Burst SL, Pochet M, Madara JL et al (2001) The role of CD47 in neutrophil transmigration. Increased rate of migration correlates with increased cell surface expression of CD47. J Biol Chem 276:40156-40166
    • (2001) J Biol Chem , vol.276 , pp. 40156-40166
    • Liu, Y.1    Merlin, D.2    Burst, S.L.3    Pochet, M.4    Madara, J.L.5
  • 120
    • 51649122800 scopus 로고    scopus 로고
    • Endothelial CD47 interaction with SIRPgamma is required for human T-cell transendothelial migration under shear flow conditions in vitro
    • Stefanidakis M, Newton G, Lee WY, Parkos CA, Luscinskas FW (2008) Endothelial CD47 interaction with SIRPgamma is required for human T-cell transendothelial migration under shear flow conditions in vitro. Blood 112:1280-1289
    • (2008) Blood , vol.112 , pp. 1280-1289
    • Stefanidakis, M.1    Newton, G.2    Lee, W.Y.3    Parkos, C.A.4    Luscinskas, F.W.5
  • 122
    • 19644367752 scopus 로고    scopus 로고
    • Neutrophil migration across tight junctions is mediated by adhesive interactions between epithelial coxsackie and adenovirus receptor and a junctional adhesion molecule-like protein on neutrophils
    • DOI 10.1091/mbc.E05-01-0036
    • Zen K, Liu Y, McCall IC, Wu T, Lee W et al (2005) Neutrophil migration across tight junctions ismediated by adhesive interactions between epithelial coxsackie and adenovirus receptor and a junctional adhesion molecule-like protein on neutrophils. Mol Biol Cell 16:2694-2703 (Pubitemid 40741217)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.6 , pp. 2694-2703
    • Zen, K.1    Liu, Y.2    McCall, I.C.3    Wu, T.4    Lee, W.5    Babbin, B.A.6    Nusrat, A.7    Parkos, C.A.8
  • 123
    • 33947416079 scopus 로고    scopus 로고
    • Pathobiology of neutrophil transepithelial migration: Implications in mediating epithelial injury
    • DOI 10.1146/annurev.pathol.2.010506.091944, Annual Review of Pathology: Mechanisms of Disease
    • Chin AC, Parkos CA (2007) Pathobiology of neutrophil transepithelial migration: implications in mediating epithelial injury. Annu Rev Pathol 2:111-143 (Pubitemid 46448062)
    • (2007) Annual Review of Pathology , vol.2 , pp. 111-143
    • Chin, A.C.1    Parkos, C.A.2
  • 124
    • 0023546355 scopus 로고
    • Effects of polymorphonuclear leukocyte transmigration on the barrier function of cultured intestinal epithelial monolayers
    • Nash S, Stafford J,Madara JL (1987) Effects of polymorphonuclear leukocyte transmigration on the barrier function of cultured intestinal epithelial monolayers. J Clin Invest 80:1104-1113 (Pubitemid 18075649)
    • (1987) Journal of Clinical Investigation , vol.80 , Issue.4 , pp. 1104-1113
    • Nash, S.1    Stafford, J.2    Madara, J.L.3
  • 125
    • 0030812622 scopus 로고    scopus 로고
    • Neutrophil migration across model intestinal epithelia: Monolayer disruption and subsequent events in epithelial repair
    • DOI 10.1053/gast.1997.v113.pm9352851
    • Nusrat A, Parkos CA, Liang TW, Carnes DK, Madara JL (1997) Neutrophil migration across model intestinal epithelia: monolayer disruption and subsequent events in epithelial repair. Gastroenterology 113:1489-1500 (Pubitemid 27461235)
    • (1997) Gastroenterology , vol.113 , Issue.5 , pp. 1489-1500
    • Nusrat, A.1    Parkos, C.A.2    Liang, T.W.3    Carnes, D.K.4    Madara, J.L.5
  • 126
    • 0030017256 scopus 로고    scopus 로고
    • Infection of human intestinal epithelial cells with invasive bacteria upregulates apical intercellular adhesion molecule-1 (ICAM-1) expression and neutrophil adhesion
    • Huang GT, Eckmann L, Savidge TC, Kagnoff MF (1996) Infection of human intestinal epithelial cells with invasive bacteria upregulates apical intercellular adhesion molecule-1 (ICAM)-1) expression and neutrophil adhesion. J Clin Invest 98:572-583 (Pubitemid 26255759)
    • (1996) Journal of Clinical Investigation , vol.98 , Issue.2 , pp. 572-583
    • Huang, G.T.-J.1    Eckmann, L.2    Savidge, T.C.3    Kagnoff, M.F.4
  • 127
    • 0029764610 scopus 로고    scopus 로고
    • Expression and polarization of intercellular adhesion molecule-1 on human intestinal epithelia: Consequences for CD11b/CD18-mediated interactions with neutrophils
    • Parkos CA, Colgan SP, Diamond MS, Nusrat A, Liang TW et al (1996) Expression and polarization of intercellular adhesion molecule-1 on human intestinal epithelia: consequences for CD11b/ CD18-mediated interactions with neutrophils. Mol Med 2:489-505 (Pubitemid 26271703)
    • (1996) Molecular Medicine , vol.2 , Issue.4 , pp. 489-505
    • Parkos, C.A.1    Colgan, S.P.2    Diamond, M.S.3    Nusrat, A.4    Liang, T.W.5    Springer, T.A.6    Madara, J.L.7
  • 128
    • 84898646992 scopus 로고    scopus 로고
    • Transmigrated neutrophils in the intestinal lumen engage ICAM-1 to regulate the epithelial barrier and neutrophil recruitment
    • Sumagin R, Robin AZ, Nusrat A, Parkos CA (2013) Transmigrated neutrophils in the intestinal lumen engage ICAM-1 to regulate the epithelial barrier and neutrophil recruitment. Mucosal Immunol.
    • (2013) Mucosal Immunol
    • Sumagin, R.1    Robin, A.Z.2    Nusrat, A.3    Parkos, C.A.4
  • 129
    • 78650656116 scopus 로고    scopus 로고
    • Neutrophil migration across intestinal epithelium: Evidence for a role of CD44 in regulating detachment of migrating cells from the luminal surface
    • Brazil JC, Lee WY, Kolegraff KN, Nusrat A, Parkos CA et al (2010) Neutrophil migration across intestinal epithelium: evidence for a role of CD44 in regulating detachment of migrating cells from the luminal surface. J Immunol 185:7026-7036
    • (2010) J Immunol , vol.185 , pp. 7026-7036
    • Brazil, J.C.1    Lee, W.Y.2    Kolegraff, K.N.3    Nusrat, A.4    Parkos, C.A.5
  • 132
    • 84864861276 scopus 로고    scopus 로고
    • The role of neutrophils during intestinal inflammation
    • Fournier BM, Parkos CA (2012) The role of neutrophils during intestinal inflammation. Mucosal Immunol 5:354-366
    • (2012) Mucosal Immunol , vol.5 , pp. 354-366
    • Fournier, B.M.1    Parkos, C.A.2
  • 133
    • 79955670124 scopus 로고    scopus 로고
    • Resolvins and protectins in inflammation resolution
    • Serhan CN, Petasis NA (2011) Resolvins and protectins in inflammation resolution. Chem Rev 111:5922-5943
    • (2011) Chem Rev , vol.111 , pp. 5922-5943
    • Serhan, C.N.1    Petasis, N.A.2
  • 134
    • 1642347836 scopus 로고    scopus 로고
    • Intestinal Intraepithelial Lymphocyte gammadelta-T Cell-Derived Keratinocyte Growth Factor Modulates Epithelial Growth in the Mouse
    • Yang H, Antony PA, Wildhaber BE, Teitelbaum DH (2004) Intestinal intraepithelial lymphocyte gamma delta-T cell-derived keratinocyte growth factor modulates epithelial growth in the mouse. J Immunol 172:4151-4158 (Pubitemid 38375227)
    • (2004) Journal of Immunology , vol.172 , Issue.7 , pp. 4151-4158
    • Yang, H.1    Antony, P.A.2    Wildhaber, B.E.3    Teitelbaum, D.H.4
  • 136
    • 77956273963 scopus 로고    scopus 로고
    • The junctional adhesion molecule JAML is a costimulatory receptor for epithelial gammadelta T cell activation
    • Witherden DA, Verdino P, Rieder SE, Garijo O, Mills RE et al (2010) The junctional adhesion molecule JAML is a costimulatory receptor for epithelial gammadelta T cell activation. Science 329: 1205-1210
    • (2010) Science , vol.329 , pp. 1205-1210
    • Witherden, D.A.1    Verdino, P.2    Rieder, S.E.3    Garijo, O.4    Mills, R.E.5
  • 139
    • 0034182004 scopus 로고    scopus 로고
    • Neutrophil apoptosis is delayed in patients with inflammatory bowel disease
    • Brannigan AE, O'Connell PR, Hurley H, O'Neill A, Brady HR et al (2000) Neutrophil apoptosis is delayed in patients with inflammatory bowel disease. Shock 13:361-366
    • (2000) Shock , vol.13 , pp. 361-366
    • Brannigan, A.E.1    O'Connell, P.R.2    Hurley, H.3    O'Neill, A.4    Brady, H.R.5
  • 140
    • 84879068635 scopus 로고    scopus 로고
    • The role of polymorphonuclear leukocyte trafficking in the perpetuation of inflammation during inflammatory bowel disease
    • Brazil JC, Louis NA, Parkos CA (2013) The role of polymorphonuclear leukocyte trafficking in the perpetuation of inflammation during inflammatory bowel disease. Inflamm Bowel Dis 19:1556-1565
    • (2013) Inflamm Bowel Dis , vol.19 , pp. 1556-1565
    • Brazil, J.C.1    Louis, N.A.2    Parkos, C.A.3
  • 141
    • 66549086638 scopus 로고    scopus 로고
    • Regulated release and functional modulation of junctional adhesion molecule A by disintegrin metalloproteinases
    • Koenen RR, Pruessmeyer J, Soehnlein O, Fraemohs L, Zernecke A et al (2009) Regulated release and functional modulation of junctional adhesion molecule A by disintegrin metalloproteinases. Blood 113:4799-4809
    • (2009) Blood , vol.113 , pp. 4799-4809
    • Koenen, R.R.1    Pruessmeyer, J.2    Soehnlein, O.3    Fraemohs, L.4    Zernecke, A.5
  • 142
    • 77956419867 scopus 로고    scopus 로고
    • Junctional adhesion molecule-C is a soluble mediator of angiogenesis
    • Rabquer BJ, Amin MA, Teegala N, Shaheen MK, Tsou PS et al (2010) Junctional adhesion molecule-C is a soluble mediator of angiogenesis. J Immunol 185:1777-1785
    • (2010) J Immunol , vol.185 , pp. 1777-1785
    • Rabquer, B.J.1    Amin, M.A.2    Teegala, N.3    Shaheen, M.K.4    Tsou, P.S.5
  • 144
    • 79953312227 scopus 로고    scopus 로고
    • JAM-A regulates epithelial proliferation through Akt/beta-catenin signalling
    • Nava P, Capaldo CT, Koch S, Kolegraff K, Rankin CR et al (2011) JAM-A regulates epithelial proliferation through Akt/beta-catenin signalling. EMBO Rep 12:314-320
    • (2011) EMBO Rep , vol.12 , pp. 314-320
    • Nava, P.1    Capaldo, C.T.2    Koch, S.3    Kolegraff, K.4    Rankin, C.R.5
  • 145
    • 20444481707 scopus 로고    scopus 로고
    • Interferon-gamma induces internalization of epithelial tight junction proteins via a macropinocytosis-like process
    • DOI 10.1096/fj.04-3260com
    • Bruewer M, Utech M, Ivanov AI, Hopkins AM, Parkos CA et al (2005) Interferon-gamma induces internalization of epithelial tight junction proteins via a macropinocytosis-like process. FASEB J 19: 923-933 (Pubitemid 40827713)
    • (2005) FASEB Journal , vol.19 , Issue.8 , pp. 923-933
    • Bruewer, M.1    Utech, M.2    Ivanov, A.I.3    Hopkins, A.M.4    Parkos, C.A.5    Nusrat, A.6
  • 146
    • 0035185891 scopus 로고    scopus 로고
    • Neutrophil transmigration in inflammatory bowel disease is associated with differential expression of epithelial intercellular junction proteins
    • Kucharzik T, Walsh SV, Chen J, Parkos CA, Nusrat A (2001) Neutrophil transmigration in inflammatory bowel disease is associated with differential expression of epithelial intercellular junction proteins. Am J Pathol 159:2001-2009 (Pubitemid 33104255)
    • (2001) American Journal of Pathology , vol.159 , Issue.6 , pp. 2001-2009
    • Kucharzik, T.1    Walsh, S.V.2    Chen, J.3    Parkos, C.A.4    Nusrat, A.5
  • 148
    • 63249123919 scopus 로고    scopus 로고
    • Cytokine regulation of tight junctions
    • Capaldo CT, Nusrat A (2009) Cytokine regulation of tight junctions. Biochim Biophys Acta 1788:864-871
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 864-871
    • Capaldo, C.T.1    Nusrat, A.2
  • 150
    • 17844396691 scopus 로고    scopus 로고
    • Quantitative measurement of cytokine mRNA in inflammatory bowel disease: Relation to clinical and endoscopic activity and outcome
    • DOI 10.1097/00042737-200505000-00012
    • Raddatz D, Bockemuhl M, Ramadori G (2005) Quantitative measurement of cytokine mRNA in inflammatory bowel disease: relation to clinical and endoscopic activity and outcome. Eur J Gastroenterol Hepatol 17:547-557 (Pubitemid 40592713)
    • (2005) European Journal of Gastroenterology and Hepatology , vol.17 , Issue.5 , pp. 547-557
    • Raddatz, D.1    Bockemuhl, M.2    Ramadori, G.3
  • 152
    • 0028576989 scopus 로고
    • Interferon expression in Crohn's disease patients: Increased interferon-gamma and -alphamRNA in the intestinal lamina propria mononuclear cells
    • Fais S, Capobianchi MR, Silvestri M, Mercuri F, Pallone F et al (1994) Interferon expression in Crohn's disease patients: increased interferon-gamma and -alphamRNA in the intestinal lamina propria mononuclear cells. J Interferon Res 14:235-238
    • (1994) J Interferon Res , vol.14 , pp. 235-238
    • Fais, S.1    Capobianchi, M.R.2    Silvestri, M.3    Mercuri, F.4    Pallone, F.5
  • 153
    • 0025333699 scopus 로고
    • Tumour necrosis factor-alpha and interferon-gamma production measured at the single cell level in normal and inflamed human intestine
    • MacDonald TT, Hutchings P, Choy MY, Murch S, Cooke A (1990) Tumour necrosis factor-alpha and interferon-gamma production measured at the single cell level in normal and inflamed human intestine. Clin Exp Immunol 81:301-305 (Pubitemid 20242538)
    • (1990) Clinical and Experimental Immunology , vol.81 , Issue.2 , pp. 301-305
    • MacDonald, T.T.1    Hutchings, P.2    Choy, M.-Y.3    Murch, S.4    Cooke, A.5
  • 154
    • 0027486125 scopus 로고
    • Location of tumour necrosis factor alpha by immunohistochemistry in chronic inflammatory bowel disease
    • Murch SH, Braegger CP, Walker-Smith JA, MacDonald TT (1993) Location of tumour necrosis factor alpha by immunohistochemistry in chronic inflammatory bowel disease. Gut 34:1705-1709 (Pubitemid 23353163)
    • (1993) Gut , vol.34 , Issue.12 , pp. 1705-1709
    • Murch, S.H.1    Braegger, C.P.2    Walker-Smith, J.A.3    MacDonald, T.T.4
  • 157
    • 26244442836 scopus 로고    scopus 로고
    • Mechanism of IFN-gamma-induced endocytosis of tight junction proteins: Myosin II-dependent vacuolarization of the apical plasma membrane
    • DOI 10.1091/mbc.E05-03-0193
    • Utech M, Ivanov AI, Samarin SN, Bruewer M, Turner JR et al (2005) Mechanism of IFN-gamma-induced endocytosis of tight junction proteins: myosin II-dependent vacuolarization of the apical plasma membrane. Mol Biol Cell 16:5040-5052 (Pubitemid 41416480)
    • (2005) Molecular Biology of the Cell , vol.16 , Issue.10 , pp. 5040-5052
    • Utech, M.1    Ivanov, A.I.2    Samarin, S.N.3    Bruewer, M.4    Turner, J.R.5    Mrsny, R.J.6    Parkos, C.A.7    Nusrat, A.8
  • 158
    • 13244298599 scopus 로고    scopus 로고
    • Interferon-gamma and tumor necrosis factor-alpha synergize to induce intestinal epithelial barrier dysfunction by up-regulating myosin light chain kinase expression
    • Wang F, Graham WV, Wang Y, Witkowski ED, Schwarz BT et al (2005) Interferon-gamma and tumor necrosis factoralpha synergize to induce intestinal epithelial barrier dysfunction by up-regulating myosin light chain kinase expression. Am J Pathol 166:409-419 (Pubitemid 40189038)
    • (2005) American Journal of Pathology , vol.166 , Issue.2 , pp. 409-419
    • Wang, F.1    Graham, W.V.2    Wang, Y.3    Witkowski, E.D.4    Schwarz, B.T.5    Turner, J.R.6
  • 159
    • 33746266715 scopus 로고    scopus 로고
    • Expression of the coxsackievirus- and adenovirus receptor in gastrointestinal cancer correlates with tumor differentiation
    • DOI 10.1038/sj.cgt.7700947, PII 7700947
    • Korn WM, Macal M, Christian C, Lacher MD, McMillan A et al (2006) Expression of the Coxsackievirus- and adenovirus receptor in gastrointestinal cancer correlates with tumor differentiation. Cancer Gene Ther 13:792-797 (Pubitemid 44100492)
    • (2006) Cancer Gene Therapy , vol.13 , Issue.8 , pp. 792-797
    • Korn, W.M.1    Macal, M.2    Christian, C.3    Lacher, M.D.4    McMillan, A.5    Rauen, K.A.6    Warren, R.S.7    Ferrell, L.8
  • 160
    • 0035420192 scopus 로고    scopus 로고
    • The mechanism of the growth-inhibitory effect of coxsackie and adenovirus receptor (CAR) on human bladder cancer: A functional analysis of car protein structure
    • Okegawa T, Pong RC, Li Y, Bergelson JM, Sagalowsky AI et al (2001) The mechanism of the growth-inhibitory effect of coxsackie and adenovirus receptor (CAR) on human bladder cancer: a functional analysis of car protein structure. Cancer Res 61:6592-6600 (Pubitemid 32783269)
    • (2001) Cancer Research , vol.61 , Issue.17 , pp. 6592-6600
    • Okegawa, T.1    Pong, R.-C.2    Li, Y.3    Bergelson, J.M.4    Sagalowsky, A.I.5    Hsieh, J.-T.6
  • 161
    • 70350626887 scopus 로고    scopus 로고
    • Loss of Coxsackie and adenovirus receptor downregulates alpha-catenin expression
    • Stecker K, Koschel A, Wiedenmann B, Anders M (2009) Loss of Coxsackie and adenovirus receptor downregulates alpha-catenin expression. Br J Cancer 101:1574-1579
    • (2009) Br J Cancer , vol.101 , pp. 1574-1579
    • Stecker, K.1    Koschel, A.2    Wiedenmann, B.3    Anders, M.4
  • 162
    • 33847315194 scopus 로고    scopus 로고
    • JAM-C regulates tight junctions and integrin-mediated cell adhesion and migration
    • DOI 10.1074/jbc.M605666200
    • Mandicourt G, Iden S, Ebnet K, Aurrand-Lions M, Imhof BA (2007) JAM-C regulates tight junctions and integrin-mediated cell adhesion and migration. J Biol Chem 282:1830-1837 (Pubitemid 47076730)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.3 , pp. 1830-1837
    • Mandicourt, G.1    Iden, S.2    Ebnet, K.3    Aurrand-Lions, M.4    Imhof, B.A.5
  • 163
    • 0141679018 scopus 로고    scopus 로고
    • 3 complex
    • DOI 10.1182/blood-2003-04-1114
    • Naik MU, Mousa SA, Parkos CA, Naik UP (2003) Signaling through JAM-1 and alphavbeta3 is required for the angiogenic action of bFGF: dissociation of the JAM-1 and alphavbeta3 complex. Blood 102:2108-2114 (Pubitemid 37122387)
    • (2003) Blood , vol.102 , Issue.6 , pp. 2108-2114
    • Naik, M.U.1    Mousa, S.A.2    Parkos, C.A.3    Naik, U.P.4
  • 164
    • 33644967620 scopus 로고    scopus 로고
    • Junctional adhesion molecule-A induced endothelial cell migration on vitronectin is integrin alpha v beta 3 specific
    • Naik MU, Naik UP (2006) Junctional adhesion molecule-A induced endothelial cell migration on vitronectin is integrin alpha v beta 3 specific. J Cell Sci 119:490-499
    • (2006) J Cell Sci , vol.119 , pp. 490-499
    • Naik, M.U.1    Naik, U.P.2
  • 165
    • 68249147448 scopus 로고    scopus 로고
    • JAM-A expression positively correlates with poor prognosis in breast cancer patients
    • McSherry EA, McGee SF, Jirstrom K, Doyle EM, Brennan DJ et al (2009) JAM-A expression positively correlates with poor prognosis in breast cancer patients. Int J Cancer 125:1343-1351
    • (2009) Int J Cancer , vol.125 , pp. 1343-1351
    • McSherry, E.A.1    McGee, S.F.2    Jirstrom, K.3    Doyle, E.M.4    Brennan, D.J.5
  • 166
    • 15744362477 scopus 로고    scopus 로고
    • Junctional adhesion molecule 1 regulates epithelial cell morphology through effects on beta1 integrins and Rap1 activity
    • DOI 10.1074/jbc.M412650200
    • Mandell KJ, Babbin BA, Nusrat A, Parkos CA (2005) Junctional adhesion molecule 1 regulates epithelial cell morphology through effects on beta1 integrins and Rap1 activity. J Biol Chem 280: 11665-11674 (Pubitemid 40418481)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.12 , pp. 11665-11674
    • Mandell, K.J.1    Babbin, B.A.2    Nusrat, A.3    Parkos, C.A.4
  • 168
    • 84866523733 scopus 로고    scopus 로고
    • Compromised intestinal epithelial barrier induces adaptive immune compensation that protects from colitis
    • Khounlotham M, KimW, Peatman E, Nava P, Medina-Contreras O et al (2012) Compromised intestinal epithelial barrier induces adaptive immune compensation that protects from colitis. Immunity 37: 563-573
    • (2012) Immunity , vol.37 , pp. 563-573
    • Khounlotham, M.1    Kim, W.2    Peatman, E.3    Nava, P.4    Medina-Contreras, O.5
  • 169
    • 42049113615 scopus 로고    scopus 로고
    • Attenuation of junctional adhesion molecule-A is a contributing factor for breast cancer cell invasion
    • DOI 10.1158/0008-5472.CAN-07-3057
    • Naik MU, Naik TU, Suckow AT, Duncan MK, Naik UP (2008) Attenuation of junctional adhesion molecule-A is a contributing factor for breast cancer cell invasion. Cancer Res 68:2194-2203 (Pubitemid 351521792)
    • (2008) Cancer Research , vol.68 , Issue.7 , pp. 2194-2203
    • Naik, M.U.1    Naik, T.U.2    Suckow, A.T.3    Duncan, M.K.4    Naik, U.P.5
  • 170
    • 34247276545 scopus 로고    scopus 로고
    • Junctional adhesion molecule-C promotes metastatic potential of HT1080 human fibrosarcoma
    • DOI 10.1074/jbc.M608836200
    • Fuse C, Ishida Y, Hikita T, Asai T, Oku N (2007) Junctional adhesion molecule-C promotes metastatic potential of HT1080 human fibrosarcoma. J Biol Chem 282:8276-8283 (Pubitemid 47093624)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.11 , pp. 8276-8283
    • Fuse, C.1    Ishida, Y.2    Hikita, T.3    Asai, T.4    Oku, N.5
  • 171
    • 0033639244 scopus 로고    scopus 로고
    • Characterization of huJAM: Evidence for involvement in cell-cell contact and tight junction regulation
    • Liang TW, DeMarco RA,Mrsny RJ, Gurney A, Gray A et al (2000) Characterization of huJAM: evidence for involvement in cell-cell contact and tight junction regulation. Am J Physiol Cell Physiol 279:C1733-C1743
    • (2000) Am J Physiol Cell Physiol , vol.279
    • Liang, T.W.1    DeMarco, R.A.2    Mrsny, R.J.3    Gurney, A.4    Gray, A.5
  • 172
    • 4644307425 scopus 로고    scopus 로고
    • Spermatid differentiation requires the assembly of a cell polarity complex downstream of junctional adhesion molecule-C
    • DOI 10.1038/nature02877
    • Gliki G, Ebnet K, Aurrand-LionsM, Imhof BA, Adams RH (2004) Spermatid differentiation requires the assembly of a cell polarity complex downstream of junctional adhesion molecule-C. Nature 431:320-324 (Pubitemid 39265668)
    • (2004) Nature , vol.431 , Issue.7006 , pp. 320-324
    • Gliki, G.1    Ebnet, K.2    Aurrand-Lions, M.3    Imhof, B.A.4    Adams, R.H.5
  • 173
    • 37349001073 scopus 로고    scopus 로고
    • JAM-A is present in mammalian spermatozoa where it is essential for normal motility
    • DOI 10.1016/j.ydbio.2007.10.013, PII S001216060701456X
    • Shao M, Ghosh A, Cooke VG, Naik UP, Martin-DeLeon PA (2008) JAM-A is present in mammalian spermatozoa where it is essential for normal motility. Dev Biol 313:246-255 (Pubitemid 350298312)
    • (2008) Developmental Biology , vol.313 , Issue.1 , pp. 246-255
    • Shao, M.1    Ghosh, A.2    Cooke, V.G.3    Naik, U.P.4    Martin-DeLeon, P.A.5
  • 174
    • 38949151579 scopus 로고    scopus 로고
    • Junctional adhesion molecule-A, JAM-A, is a novel cell-surface marker for long-term repopulating hematopoietic stem cells
    • DOI 10.1182/blood-2007-03-081554
    • Sugano Y, Takeuchi M, Hirata A, Matsushita H, Kitamura T et al (2008) Junctional adhesion molecule-A, JAM-A, is a novel cellsurface marker for long-term repopulating hematopoietic stem cells. Blood 111:1167-1172 (Pubitemid 351213397)
    • (2008) Blood , vol.111 , Issue.3 , pp. 1167-1172
    • Sugano, Y.1    Takeuchi, M.2    Hirata, A.3    Matsushita, H.4    Kitamura, T.5    Tanaka, M.6    Miyajima, A.7
  • 176
    • 61849125758 scopus 로고    scopus 로고
    • Genetic deletion of JAM-C reveals a role in myeloid progenitor generation
    • Praetor A, McBride JM, Chiu H, Rangell L, Cabote L et al (2009) Genetic deletion of JAM-C reveals a role in myeloid progenitor generation. Blood 113:1919-1928
    • (2009) Blood , vol.113 , pp. 1919-1928
    • Praetor, A.1    McBride, J.M.2    Chiu, H.3    Rangell, L.4    Cabote, L.5
  • 177
    • 84863229734 scopus 로고    scopus 로고
    • Schwann cell-specific JAM-C-deficient mice reveal novel expression and functions for JAM-C in peripheral nerves
    • Colom B, Poitelon Y, Huang W, Woodfin A, Averill S et al (2012) Schwann cell-specific JAM-C-deficient mice reveal novel expression and functions for JAM-C in peripheral nerves. FASEB J 26:1064-1076
    • (2012) FASEB J , vol.26 , pp. 1064-1076
    • Colom, B.1    Poitelon, Y.2    Huang, W.3    Woodfin, A.4    Averill, S.5
  • 179
    • 33747495972 scopus 로고    scopus 로고
    • Junctional adhesion molecules (JAMs) are differentially expressed in fibroblasts and co-localize with ZO-1 to adherens-like junctions
    • DOI 10.1080/15419060600877978, PII MJ6X608Q31831676
    • Morris AP, Tawil A, Berkova Z, Wible L, Smith CWet al (2006) Junctional Adhesion Molecules (JAMs) are differentially expressed in fibroblasts and co-localize with ZO-1 to adherens-like junctions. Cell Commun Adhes 13:233-247 (Pubitemid 44256252)
    • (2006) Cell Communication and Adhesion , vol.13 , Issue.4 , pp. 233-247
    • Morris, A.P.1    Tawil, A.2    Berkova, Z.3    Wible, L.4    Smith, C.W.5    Cunningham, S.A.6
  • 180
    • 33751012712 scopus 로고    scopus 로고
    • A CTX family cell adhesion molecule, JAM4, is expressed in stem cell and progenitor cell populations of both male germ cell and hematopoietic cell lineages
    • DOI 10.1128/MCB.01502-06
    • Nagamatsu G, Ohmura M, Mizukami T, Hamaguchi I, Hirabayashi S et al (2006) ACTX family cell adhesionmolecule, JAM4, is expressed in stem cell and progenitor cell populations of both male germ cell and hematopoietic cell lineages. Mol Cell Biol 26:8498-8506 (Pubitemid 44748582)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.22 , pp. 8498-8506
    • Nagamatsu, G.1    Ohmura, M.2    Mizukami, T.3    Hamaguchi, I.4    Hirabayashi, S.5    Yoshida, S.6    Hata, Y.7    Suda, T.8    Ohbo, K.9
  • 181
    • 57749178164 scopus 로고    scopus 로고
    • Coxsackie- and adenovirus receptor (CAR) is expressed in lymphatic vessels in human skin and affects lymphatic endothelial cell function in vitro
    • Vigl B, Zgraggen C, Rehman N, Banziger-Tobler NE, Detmar M et al (2009) Coxsackie- and adenovirus receptor (CAR) is expressed in lymphatic vessels in human skin and affects lymphatic endothelial cell function in vitro. Exp Cell Res 315:336-347
    • (2009) Exp Cell Res , vol.315 , pp. 336-347
    • Vigl, B.1    Zgraggen, C.2    Rehman, N.3    Banziger-Tobler, N.E.4    Detmar, M.5
  • 182
    • 20244369880 scopus 로고    scopus 로고
    • Identification of adipocyte adhesion molecule (ACAM), a novel CTX gene family, implicated in adipocyte maturation and development of obesity
    • DOI 10.1042/BJ20041709
    • Eguchi J, Wada J, Hida K, Zhang H, Matsuoka T et al (2005) Identification of adipocyte adhesion molecule (ACAM), a novel CTX gene family, implicated in adipocyte maturation and development of obesity. Biochem J 387:343-353 (Pubitemid 40571220)
    • (2005) Biochemical Journal , vol.387 , Issue.2 , pp. 343-353
    • Eguchi, J.1    Wada, J.2    Hida, K.3    Zhang, H.4    Matsuoka, T.5    Baba, M.6    Hashimoto, I.7    Shikata, K.8    Ogawa, N.9    Makino, H.10
  • 183
    • 0141594945 scopus 로고    scopus 로고
    • Targeted Disruption of Endothelial Cell-selective Adhesion Molecule Inhibits Angiogenic Processes in Vitro and in Vivo
    • DOI 10.1074/jbc.M304890200
    • Ishida T, Kundu RK, Yang E, Hirata K, Ho YD et al (2003) Targeted disruption of endothelial cell-selective adhesion molecule inhibits angiogenic processes in vitro and in vivo. J Biol Chem 278:34598-34604 (Pubitemid 37553309)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.36 , pp. 34598-34604
    • Ishida, T.1    Kundu, R.K.2    Yang, E.3    Hirata, K.-I.4    Ho, Y.-D.5    Quertermous, T.6
  • 184
    • 63849111505 scopus 로고    scopus 로고
    • The endothelial antigen ESAM marks primitive hematopoietic progenitors throughout life in mice
    • Yokota T, Oritani K, Butz S, Kokame K, Kincade PW et al (2009) The endothelial antigen ESAM marks primitive hematopoietic progenitors throughout life in mice. Blood 113:2914-2923
    • (2009) Blood , vol.113 , pp. 2914-2923
    • Yokota, T.1    Oritani, K.2    Butz, S.3    Kokame, K.4    Kincade, P.W.5


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