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Volumn 6, Issue 8, 2011, Pages

An antibody to the Lutheran glycoprotein (Lu) recognizing the LU4 blood type variant inhibits cell adhesion to laminin α5

Author keywords

[No Author keywords available]

Indexed keywords

LAMININ; LAMININ ALPHA5; LUTHERAN GLYCOPROTEIN; MEMBRANE PROTEIN; MONOCLONAL ANTIBODY; UNCLASSIFIED DRUG; BCAM PROTEIN, HUMAN; CELL ADHESION MOLECULE; EPITOPE; VERY LATE ACTIVATION ANTIGEN 1; VERY LATE ACTIVATION ANTIGEN 3; VERY LATE ACTIVATION ANTIGEN 6;

EID: 80051625896     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0023329     Document Type: Article
Times cited : (8)

References (33)
  • 1
    • 0029078165 scopus 로고
    • The Lutheran blood group glycoprotein, another member of the immunoglobulin superfamily, is widely expressed in human tissues and is developmentally regulated in human liver
    • Parsons SF, Mallinson G, Holmes CH, Houlihan JM, Simpson KL, et al. (1995) The Lutheran blood group glycoprotein, another member of the immunoglobulin superfamily, is widely expressed in human tissues and is developmentally regulated in human liver. Proc Natl Acad Sci U S A 92: 5496-5500.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 5496-5500
    • Parsons, S.F.1    Mallinson, G.2    Holmes, C.H.3    Houlihan, J.M.4    Simpson, K.L.5
  • 2
    • 36148955798 scopus 로고    scopus 로고
    • The Laminin 511/521-binding site on the Lutheran blood group glycoprotein is located at the flexible junction of Ig domains 2 and 3
    • Mankelow TJ, Burton N, Stefansdottir FO, Spring FA, Parsons SF, et al. (2007) The Laminin 511/521-binding site on the Lutheran blood group glycoprotein is located at the flexible junction of Ig domains 2 and 3. Blood 110: 3398-3406.
    • (2007) Blood , vol.110 , pp. 3398-3406
    • Mankelow, T.J.1    Burton, N.2    Stefansdottir, F.O.3    Spring, F.A.4    Parsons, S.F.5
  • 3
    • 41949140173 scopus 로고    scopus 로고
    • Molecular structure of the extracellular region of Lutheran blood group glycoprotein and location of the laminin binding site
    • Burton NM, Brady RL, (2008) Molecular structure of the extracellular region of Lutheran blood group glycoprotein and location of the laminin binding site. Blood Cells Mol Dis 40: 446-448.
    • (2008) Blood Cells Mol Dis , vol.40 , pp. 446-448
    • Burton, N.M.1    Brady, R.L.2
  • 4
    • 0027944580 scopus 로고
    • Molecular cloning of the B-CAM cell surface glycoprotein of epithelial cancers: a novel member of the immunoglobulin superfamily
    • Campbell IG, Foulkes WD, Senger G, Trowsdale J, Garin-Chesa P, et al. (1994) Molecular cloning of the B-CAM cell surface glycoprotein of epithelial cancers: a novel member of the immunoglobulin superfamily. Cancer Res 54: 5761-5765.
    • (1994) Cancer Res , vol.54 , pp. 5761-5765
    • Campbell, I.G.1    Foulkes, W.D.2    Senger, G.3    Trowsdale, J.4    Garin-Chesa, P.5
  • 5
    • 0033527534 scopus 로고    scopus 로고
    • Isoforms of the Lutheran/basal cell adhesion molecule glycoprotein are differentially delivered in polarized epithelial cells. Mapping of the basolateral sorting signal to a cytoplasmic di-leucine motif
    • El Nemer W, Colin Y, Bauvy C, Codogno P, Fraser RH, et al. (1999) Isoforms of the Lutheran/basal cell adhesion molecule glycoprotein are differentially delivered in polarized epithelial cells. Mapping of the basolateral sorting signal to a cytoplasmic di-leucine motif. J Biol Chem 274: 31903-31908.
    • (1999) J Biol Chem , vol.274 , pp. 31903-31908
    • El Nemer, W.1    Colin, Y.2    Bauvy, C.3    Codogno, P.4    Fraser, R.H.5
  • 6
    • 24044477554 scopus 로고    scopus 로고
    • Protein kinase A-dependent phosphorylation of Lutheran/basal cell adhesion molecule glycoprotein regulates cell adhesion to laminin alpha5
    • Gauthier E, Rahuel C, Wautier MP, El Nemer W, Gane P, et al. (2005) Protein kinase A-dependent phosphorylation of Lutheran/basal cell adhesion molecule glycoprotein regulates cell adhesion to laminin alpha5. J Biol Chem 280: 30055-30062.
    • (2005) J Biol Chem , vol.280 , pp. 30055-30062
    • Gauthier, E.1    Rahuel, C.2    Wautier, M.P.3    El Nemer, W.4    Gane, P.5
  • 7
    • 3242701301 scopus 로고    scopus 로고
    • Direct interaction between the Lu/B-CAM adhesion glycoproteins and erythroid spectrin
    • Kroviarski Y, El Nemer W, Gane P, Rahuel C, Gauthier E, et al. (2004) Direct interaction between the Lu/B-CAM adhesion glycoproteins and erythroid spectrin. Br J Haematol 126: 255-264.
    • (2004) Br J Haematol , vol.126 , pp. 255-264
    • Kroviarski, Y.1    El Nemer, W.2    Gane, P.3    Rahuel, C.4    Gauthier, E.5
  • 8
    • 58149398627 scopus 로고    scopus 로고
    • Adhesive activity of Lu glycoproteins is regulated by interaction with spectrin
    • An X, Gauthier E, Zhang X, Guo X, Anstee DJ, et al. (2008) Adhesive activity of Lu glycoproteins is regulated by interaction with spectrin. Blood 112: 5212-5218.
    • (2008) Blood , vol.112 , pp. 5212-5218
    • An, X.1    Gauthier, E.2    Zhang, X.3    Guo, X.4    Anstee, D.J.5
  • 9
    • 0037606006 scopus 로고    scopus 로고
    • Novel epinephrine and cyclic AMP-mediated activation of BCAM/Lu-dependent sickle (SS) RBC adhesion
    • Hines PC, Zen Q, Burney SN, Shea DA, Ataga KI, et al. (2003) Novel epinephrine and cyclic AMP-mediated activation of BCAM/Lu-dependent sickle (SS) RBC adhesion. Blood 101: 3281-3287.
    • (2003) Blood , vol.101 , pp. 3281-3287
    • Hines, P.C.1    Zen, Q.2    Burney, S.N.3    Shea, D.A.4    Ataga, K.I.5
  • 10
    • 17044386676 scopus 로고    scopus 로고
    • Role of Rap1 in promoting sickle red blood cell adhesion to laminin via BCAM/LU
    • Murphy MM, Zayed MA, Evans A, Parker CE, Ataga KI, et al. (2005) Role of Rap1 in promoting sickle red blood cell adhesion to laminin via BCAM/LU. Blood 105: 3322-3329.
    • (2005) Blood , vol.105 , pp. 3322-3329
    • Murphy, M.M.1    Zayed, M.A.2    Evans, A.3    Parker, C.E.4    Ataga, K.I.5
  • 11
    • 0032479420 scopus 로고    scopus 로고
    • The Lutheran blood group glycoproteins, the erythroid receptors for laminin, are adhesion molecules
    • El Nemer W, Gane P, Colin Y, Bony V, Rahuel C, et al. (1998) The Lutheran blood group glycoproteins, the erythroid receptors for laminin, are adhesion molecules. J Biol Chem 273: 16686-16693.
    • (1998) J Biol Chem , vol.273 , pp. 16686-16693
    • El Nemer, W.1    Gane, P.2    Colin, Y.3    Bony, V.4    Rahuel, C.5
  • 12
    • 0032103286 scopus 로고    scopus 로고
    • Basal cell adhesion molecule/lutheran protein. The receptor critical for sickle cell adhesion to laminin
    • Udani M, Zen Q, Cottman M, Leonard N, Jefferson S, et al. (1998) Basal cell adhesion molecule/lutheran protein. The receptor critical for sickle cell adhesion to laminin. J Clin Invest 101: 2550-2558.
    • (1998) J Clin Invest , vol.101 , pp. 2550-2558
    • Udani, M.1    Zen, Q.2    Cottman, M.3    Leonard, N.4    Jefferson, S.5
  • 13
    • 0035161468 scopus 로고    scopus 로고
    • Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha 5 chain-containing human laminin with high affinity
    • Parsons SF, Lee G, Spring FA, Willig TN, Peters LL, et al. (2001) Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha 5 chain-containing human laminin with high affinity. Blood 97: 312-320.
    • (2001) Blood , vol.97 , pp. 312-320
    • Parsons, S.F.1    Lee, G.2    Spring, F.A.3    Willig, T.N.4    Peters, L.L.5
  • 14
    • 0034858369 scopus 로고    scopus 로고
    • Localization of Lutheran, a novel laminin receptor, in normal, knockout, and transgenic mice suggests an interaction with laminin alpha5 in vivo
    • Moulson CL, Li C, Miner JH, (2001) Localization of Lutheran, a novel laminin receptor, in normal, knockout, and transgenic mice suggests an interaction with laminin alpha5 in vivo. Dev Dyn 222: 101-114.
    • (2001) Dev Dyn , vol.222 , pp. 101-114
    • Moulson, C.L.1    Li, C.2    Miner, J.H.3
  • 15
    • 0037160080 scopus 로고    scopus 로고
    • Identification of the binding site for the Lutheran blood group glycoprotein on laminin alpha 5 through expression of chimeric laminin chains in vivo
    • Kikkawa Y, Moulson CL, Virtanen I, Miner JH, (2002) Identification of the binding site for the Lutheran blood group glycoprotein on laminin alpha 5 through expression of chimeric laminin chains in vivo. J Biol Chem 277: 44864-44869.
    • (2002) J Biol Chem , vol.277 , pp. 44864-44869
    • Kikkawa, Y.1    Moulson, C.L.2    Virtanen, I.3    Miner, J.H.4
  • 16
    • 0030919488 scopus 로고    scopus 로고
    • The laminin a chains: expression, developmental transitions, and chromosomal locations of alpha 1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel alpha 3 isoform
    • Miner JH, Patton BL, Lentz SI, Gilbert DJ, Snider WD, et al. (1997) The laminin a chains: expression, developmental transitions, and chromosomal locations of alpha 1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel alpha 3 isoform. J Cell Biol 137: 685-701.
    • (1997) J Cell Biol , vol.137 , pp. 685-701
    • Miner, J.H.1    Patton, B.L.2    Lentz, S.I.3    Gilbert, D.J.4    Snider, W.D.5
  • 17
    • 0034025635 scopus 로고    scopus 로고
    • Integrin binding specificity of laminin-10/11: laminin-10/11 are recognized by alpha 3 beta 1, alpha 6 beta 1 and alpha 6 beta 4 integrins
    • Kikkawa Y, Sanzen N, Fujiwara H, Sonnenberg A, Sekiguchi K, (2000) Integrin binding specificity of laminin-10/11: laminin-10/11 are recognized by alpha 3 beta 1, alpha 6 beta 1 and alpha 6 beta 4 integrins. J Cell Sci 113 (Pt 5): 869-876.
    • (2000) J Cell Sci , vol.113 , Issue.Pt 5 , pp. 869-876
    • Kikkawa, Y.1    Sanzen, N.2    Fujiwara, H.3    Sonnenberg, A.4    Sekiguchi, K.5
  • 18
    • 0032546780 scopus 로고    scopus 로고
    • Isolation and characterization of laminin-10/11 secreted by human lung carcinoma cells. laminin-10/11 mediates cell adhesion through integrin alpha3 beta1
    • Kikkawa Y, Sanzen N, Sekiguchi K, (1998) Isolation and characterization of laminin-10/11 secreted by human lung carcinoma cells. laminin-10/11 mediates cell adhesion through integrin alpha3 beta1. J Biol Chem 273: 15854-15859.
    • (1998) J Biol Chem , vol.273 , pp. 15854-15859
    • Kikkawa, Y.1    Sanzen, N.2    Sekiguchi, K.3
  • 19
    • 0033597343 scopus 로고    scopus 로고
    • Adhesion of cultured bovine aortic endothelial cells to laminin-1 mediated by dystroglycan
    • Shimizu H, Hosokawa H, Ninomiya H, Miner JH, Masaki T, (1999) Adhesion of cultured bovine aortic endothelial cells to laminin-1 mediated by dystroglycan. J Biol Chem 274: 11995-12000.
    • (1999) J Biol Chem , vol.274 , pp. 11995-12000
    • Shimizu, H.1    Hosokawa, H.2    Ninomiya, H.3    Miner, J.H.4    Masaki, T.5
  • 20
    • 34447536949 scopus 로고    scopus 로고
    • The LG1-3 tandem of laminin alpha5 harbors the binding sites of Lutheran/basal cell adhesion molecule and alpha3beta1/alpha6beta1 integrins
    • Kikkawa Y, Sasaki T, Nguyen MT, Nomizu M, Mitaka T, et al. (2007) The LG1-3 tandem of laminin alpha5 harbors the binding sites of Lutheran/basal cell adhesion molecule and alpha3beta1/alpha6beta1 integrins. J Biol Chem 282: 14853-14860.
    • (2007) J Biol Chem , vol.282 , pp. 14853-14860
    • Kikkawa, Y.1    Sasaki, T.2    Nguyen, M.T.3    Nomizu, M.4    Mitaka, T.5
  • 21
    • 0038414615 scopus 로고    scopus 로고
    • Beta1 integrin and alpha-dystroglycan binding sites are localized to different laminin-G-domain-like (LG) modules within the laminin alpha5 chain G domain
    • Yu H, Talts JF, (2003) Beta1 integrin and alpha-dystroglycan binding sites are localized to different laminin-G-domain-like (LG) modules within the laminin alpha5 chain G domain. Biochem J 371: 289-299.
    • (2003) Biochem J , vol.371 , pp. 289-299
    • Yu, H.1    Talts, J.F.2
  • 22
    • 12144286984 scopus 로고    scopus 로고
    • Molecular dissection of the alpha-dystroglycan- and integrin-binding sites within the globular domain of human laminin-10
    • Ido H, Harada K, Futaki S, Hayashi Y, Nishiuchi R, et al. (2004) Molecular dissection of the alpha-dystroglycan- and integrin-binding sites within the globular domain of human laminin-10. J Biol Chem 279: 10946-10954.
    • (2004) J Biol Chem , vol.279 , pp. 10946-10954
    • Ido, H.1    Harada, K.2    Futaki, S.3    Hayashi, Y.4    Nishiuchi, R.5
  • 23
    • 0033534462 scopus 로고    scopus 로고
    • Critical factors in basal cell adhesion molecule/lutheran-mediated adhesion to laminin
    • Zen Q, Cottman M, Truskey G, Fraser R, Telen MJ, (1999) Critical factors in basal cell adhesion molecule/lutheran-mediated adhesion to laminin. J Biol Chem 274: 728-734.
    • (1999) J Biol Chem , vol.274 , pp. 728-734
    • Zen, Q.1    Cottman, M.2    Truskey, G.3    Fraser, R.4    Telen, M.J.5
  • 24
    • 0035968260 scopus 로고    scopus 로고
    • Characterization of the laminin binding domains of the Lutheran blood group glycoprotein
    • El Nemer W, Gane P, Colin Y, D'Ambrosio AM, Callebaut I, et al. (2001) Characterization of the laminin binding domains of the Lutheran blood group glycoprotein. J Biol Chem 276: 23757-23762.
    • (2001) J Biol Chem , vol.276 , pp. 23757-23762
    • El Nemer, W.1    Gane, P.2    Colin, Y.3    D'Ambrosio, A.M.4    Callebaut, I.5
  • 25
    • 0029892514 scopus 로고    scopus 로고
    • Molecular basis of sickle cell-endothelial cell interactions
    • Wick TM, Eckman JR, (1996) Molecular basis of sickle cell-endothelial cell interactions. Curr Opin Hematol 3: 118-124.
    • (1996) Curr Opin Hematol , vol.3 , pp. 118-124
    • Wick, T.M.1    Eckman, J.R.2
  • 26
    • 0031157083 scopus 로고    scopus 로고
    • Perspectives series: cell adhesion in vascular biology. Adhesive interactions of sickle erythrocytes with endothelium
    • Hebbel RP, (1997) Perspectives series: cell adhesion in vascular biology. Adhesive interactions of sickle erythrocytes with endothelium. J Clin Invest 99: 2561-2564.
    • (1997) J Clin Invest , vol.99 , pp. 2561-2564
    • Hebbel, R.P.1
  • 27
    • 33645285018 scopus 로고    scopus 로고
    • The Lutheran glycoprotein: a multifunctional adhesion receptor
    • Eyler CE, Telen MJ, (2006) The Lutheran glycoprotein: a multifunctional adhesion receptor. Transfusion 46: 668-677.
    • (2006) Transfusion , vol.46 , pp. 668-677
    • Eyler, C.E.1    Telen, M.J.2
  • 28
    • 77957204379 scopus 로고    scopus 로고
    • Decreased sickle red blood cell adhesion to laminin by hydroxyurea is associated with inhibition of Lu/BCAM protein phosphorylation
    • Bartolucci P, Chaar V, Picot J, Bachir D, Habibi A, et al. (2010) Decreased sickle red blood cell adhesion to laminin by hydroxyurea is associated with inhibition of Lu/BCAM protein phosphorylation. Blood 116: 2152-2159.
    • (2010) Blood , vol.116 , pp. 2152-2159
    • Bartolucci, P.1    Chaar, V.2    Picot, J.3    Bachir, D.4    Habibi, A.5
  • 29
  • 30
    • 48849092900 scopus 로고    scopus 로고
    • Laminin alpha 5 mediates ectopic adhesion of hepatocellular carcinoma through integrins and/or Lutheran/basal cell adhesion molecule
    • Kikkawa Y, Sudo R, Kon J, Mizuguchi T, Nomizu M, et al. (2008) Laminin alpha 5 mediates ectopic adhesion of hepatocellular carcinoma through integrins and/or Lutheran/basal cell adhesion molecule. Exp Cell Res 314: 2579-2590.
    • (2008) Exp Cell Res , vol.314 , pp. 2579-2590
    • Kikkawa, Y.1    Sudo, R.2    Kon, J.3    Mizuguchi, T.4    Nomizu, M.5
  • 31
    • 0031456144 scopus 로고    scopus 로고
    • Distribution and function of laminins in the neuromuscular system of developing, adult, and mutant mice
    • Patton BL, Miner JH, Chiu AY, Sanes JR, (1997) Distribution and function of laminins in the neuromuscular system of developing, adult, and mutant mice. J Cell Biol 139: 1507-1521.
    • (1997) J Cell Biol , vol.139 , pp. 1507-1521
    • Patton, B.L.1    Miner, J.H.2    Chiu, A.Y.3    Sanes, J.R.4
  • 32
    • 0030614865 scopus 로고    scopus 로고
    • Integrin alpha8beta1 is critically important for epithelial-mesenchymal interactions during kidney morphogenesis
    • Muller U, Wang D, Denda S, Meneses JJ, Pedersen RA, et al. (1997) Integrin alpha8beta1 is critically important for epithelial-mesenchymal interactions during kidney morphogenesis. Cell 88: 603-613.
    • (1997) Cell , vol.88 , pp. 603-613
    • Muller, U.1    Wang, D.2    Denda, S.3    Meneses, J.J.4    Pedersen, R.A.5
  • 33
    • 33645113450 scopus 로고    scopus 로고
    • Review: Lutheran/B-CAM: a laminin receptor on red blood cells and in various tissues
    • Kikkawa Y, Miner JH, (2005) Review: Lutheran/B-CAM: a laminin receptor on red blood cells and in various tissues. Connect Tissue Res 46: 193-199.
    • (2005) Connect Tissue Res , vol.46 , pp. 193-199
    • Kikkawa, Y.1    Miner, J.H.2


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