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Volumn 15, Issue 1-2, 2008, Pages 29-33

Role of Lu/BCAM in abnormal adhesion of sickle red blood cells to vascular endothelium

Author keywords

Adhesion; Alpha 4 integrin; Lutheran BCAM; Sickle cell anemia

Indexed keywords

ADRENALIN; BASAL CELL ADHESION MOLECULE; CASEIN KINASE II; CELL ADHESION MOLECULE; CYCLIC AMP DEPENDENT PROTEIN KINASE; GLYCOGEN SYNTHASE KINASE 3BETA; LAMININ 10;

EID: 49949151974     PISSN: 12467820     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tracli.2008.05.002     Document Type: Article
Times cited : (20)

References (33)
  • 1
    • 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., Galacteros F., et al. The Lutheran blood group glycoproteins, the erythroid receptors for laminin, are adhesion molecules. J Biol Chem 273 (1998) 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    Galacteros, F.6
  • 2
    • 0035161468 scopus 로고    scopus 로고
    • Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity
    • Parsons S.F., Lee G., Spring F.A., Willig T.N., Peters L.L., Gimm J.A., et al. Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind alpha5 chain-containing human laminin with high affinity. Blood 97 (2001) 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    Gimm, J.A.6
  • 3
    • 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., Daymont C., et al. Basal cell adhesion molecule/lutheran protein. The receptor critical for sickle cell adhesion to laminin. J Clin Invest 101 (1998) 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    Daymont, C.6
  • 4
    • 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 C.L., Li C., and Miner J.H. Localization of Lutheran, a novel laminin receptor, in normal, knockout, and transgenic mice suggests an interaction with laminin alpha5 in vivo. Dev Dyn 222 (2001) 101-114
    • (2001) Dev Dyn , vol.222 , pp. 101-114
    • Moulson, C.L.1    Li, C.2    Miner, J.H.3
  • 7
    • 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 C.L., Virtanen I., and Miner J.H. 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 (2002) 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
  • 8
    • 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 A.M., Callebaut I., Cartron J.P., et al. Characterization of the laminin binding domains of the Lutheran blood group glycoprotein. J Biol Chem 276 (2001) 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    Cartron, J.P.6
  • 9
    • 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 M.P., El Nemer W., Gane P., Wautier J.L., et al. Protein kinase A-dependent phosphorylation of Lutheran/basal cell adhesion molecule glycoprotein regulates cell adhesion to laminin alpha5. J Biol Chem 280 (2005) 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    Wautier, J.L.6
  • 10
    • 0023164977 scopus 로고
    • Evidence that the Lub blood group antigen is located on red cell membrane glycoproteins of 85 and 78 kd
    • Parsons S.F., Mallinson G., Judson P.A., Anstee D.J., Tanner M.J., and Daniels G.L. Evidence that the Lub blood group antigen is located on red cell membrane glycoproteins of 85 and 78 kd. Transfusion 27 (1987) 61-63
    • (1987) Transfusion , vol.27 , pp. 61-63
    • Parsons, S.F.1    Mallinson, G.2    Judson, P.A.3    Anstee, D.J.4    Tanner, M.J.5    Daniels, G.L.6
  • 11
    • 0024338544 scopus 로고
    • Identification, by immunoblotting, of the structures carrying Lutheran and para-Lutheran blood group antigens
    • Daniels G., and Khalid G. Identification, by immunoblotting, of the structures carrying Lutheran and para-Lutheran blood group antigens. Vox Sang 57 (1989) 137-141
    • (1989) Vox Sang , vol.57 , pp. 137-141
    • Daniels, G.1    Khalid, G.2
  • 12
    • 0027944580 scopus 로고
    • Molecular cloning of the B-CAM cell surface glycoprotein of epithelial cancers: a novel member of the immunoglobulin superfamily
    • Campbell I.G., Foulkes W.D., Senger G., Trowsdale J., Garin-Chesa P., and Rettig W.J. Molecular cloning of the B-CAM cell surface glycoprotein of epithelial cancers: a novel member of the immunoglobulin superfamily. Cancer Res 54 (1994) 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    Rettig, W.J.6
  • 13
    • 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 S.F., Mallinson G., Holmes C.H., Houlihan J.M., Simpson K.L., Mawby W.J., et al. 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 (1995) 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    Mawby, W.J.6
  • 14
    • 0021679055 scopus 로고
    • Somatic cell genetic analysis of human cell surface antigens: chromosomal assignments and regulation of expression in rodent-human hybrid cells
    • Rettig W.J., Dracopoli N.C., Goetzger T.A., Spengler B.A., Biedler J.L., Oettgen H.F., et al. Somatic cell genetic analysis of human cell surface antigens: chromosomal assignments and regulation of expression in rodent-human hybrid cells. Proc Natl Acad Sci U S A 81 (1984) 6437-6441
    • (1984) Proc Natl Acad Sci U S A , vol.81 , pp. 6437-6441
    • Rettig, W.J.1    Dracopoli, N.C.2    Goetzger, T.A.3    Spengler, B.A.4    Biedler, J.L.5    Oettgen, H.F.6
  • 15
    • 0005429990 scopus 로고
    • Cell-surface glycoproteins of human sarcomas: differential expression in normal and malignant tissues and cultured cells
    • Rettig W.J., Garin-Chesa P., Beresford H.R., Oettgen H.F., Melamed M.R., and Old L.J. Cell-surface glycoproteins of human sarcomas: differential expression in normal and malignant tissues and cultured cells. Proc Natl Acad Sci U S A 85 (1988) 3110-3114
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 3110-3114
    • Rettig, W.J.1    Garin-Chesa, P.2    Beresford, H.R.3    Oettgen, H.F.4    Melamed, M.R.5    Old, L.J.6
  • 16
    • 0018924116 scopus 로고
    • Abnormal adherence of sickle erythrocytes to cultured vascular endothelium: possible mechanism for microvascular occlusion in sickle cell disease
    • Hebbel R.P., Yamada O., Moldow C.F., Jacob H.S., White J.G., and Eaton J.W. Abnormal adherence of sickle erythrocytes to cultured vascular endothelium: possible mechanism for microvascular occlusion in sickle cell disease. J Clin Invest 65 (1980) 154-160
    • (1980) J Clin Invest , vol.65 , pp. 154-160
    • Hebbel, R.P.1    Yamada, O.2    Moldow, C.F.3    Jacob, H.S.4    White, J.G.5    Eaton, J.W.6
  • 17
    • 0018885938 scopus 로고
    • Erythrocyte adherence to endothelium in sickle-cell anemia. A possible determinant of disease severity
    • Hebbel R.P., Boogaerts M.A., Eaton J.W., and Steinberg M.H. Erythrocyte adherence to endothelium in sickle-cell anemia. A possible determinant of disease severity. N Engl J Med 302 (1980) 992-995
    • (1980) N Engl J Med , vol.302 , pp. 992-995
    • Hebbel, R.P.1    Boogaerts, M.A.2    Eaton, J.W.3    Steinberg, M.H.4
  • 18
    • 0141990755 scopus 로고    scopus 로고
    • Erythrocyte adhesion in sickle cell disease
    • Parise L.V., and Telen M.J. Erythrocyte adhesion in sickle cell disease. Curr Hematol Rep 2 (2003) 102-108
    • (2003) Curr Hematol Rep , vol.2 , pp. 102-108
    • Parise, L.V.1    Telen, M.J.2
  • 20
    • 0037606006 scopus 로고    scopus 로고
    • Novel epinephrine and cyclic AMP-mediated activation of BCAM/Lu-dependent sickle (SS) RBC adhesion
    • Hines P.C., Zen Q., Burney S.N., Shea D.A., Ataga K.I., Orringer E.P., et al. Novel epinephrine and cyclic AMP-mediated activation of BCAM/Lu-dependent sickle (SS) RBC adhesion. Blood 101 (2003) 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    Orringer, E.P.6
  • 21
    • 0344812230 scopus 로고
    • Microvascular sites and characteristics of sickle cell adhesion to vascular endothelium in shear flow conditions: pathophysiological implications
    • Kaul D.K., Fabry M.E., and Nagel R.L. Microvascular sites and characteristics of sickle cell adhesion to vascular endothelium in shear flow conditions: pathophysiological implications. Proc Natl Acad Sci U S A 86 (1989) 3356-3360
    • (1989) Proc Natl Acad Sci U S A , vol.86 , pp. 3356-3360
    • Kaul, D.K.1    Fabry, M.E.2    Nagel, R.L.3
  • 22
    • 33751092291 scopus 로고    scopus 로고
    • Peptides based on alphaV-binding domains of erythrocyte ICAM-4 inhibit sickle red cell-endothelial interactions and vaso-occlusion in the microcirculation
    • Kaul D.K., Liu X.D., Zhang X., Mankelow T., Parsons S., Spring F., et al. Peptides based on alphaV-binding domains of erythrocyte ICAM-4 inhibit sickle red cell-endothelial interactions and vaso-occlusion in the microcirculation. Am J Physiol Cell Physiol 291 (2006) C922-C930
    • (2006) Am J Physiol Cell Physiol , vol.291
    • Kaul, D.K.1    Liu, X.D.2    Zhang, X.3    Mankelow, T.4    Parsons, S.5    Spring, F.6
  • 23
    • 0028108393 scopus 로고
    • Structural motifs for recognition and adhesion in members of the immunoglobulin superfamily
    • Holness C.L., and Simmons D.L. Structural motifs for recognition and adhesion in members of the immunoglobulin superfamily. J Cell Sci 107 Pt 8 (1994) 2065-2070
    • (1994) J Cell Sci , vol.107 , Issue.PART 8 , pp. 2065-2070
    • Holness, C.L.1    Simmons, D.L.2
  • 24
    • 0026073690 scopus 로고
    • Coexpression of two fibronectin receptors, VLA-4 and VLA-5, by immature human erythroblastic precursor cells
    • Rosemblatt M., Vuillet-Gaugler M.H., Leroy C., and Coulombel L. Coexpression of two fibronectin receptors, VLA-4 and VLA-5, by immature human erythroblastic precursor cells. J Clin Invest 87 (1991) 6-11
    • (1991) J Clin Invest , vol.87 , pp. 6-11
    • Rosemblatt, M.1    Vuillet-Gaugler, M.H.2    Leroy, C.3    Coulombel, L.4
  • 25
    • 0025851410 scopus 로고
    • Fibronectin and VLA-4 in haematopoietic stem cell-microenvironment interactions
    • Williams D.A., Rios M., Stephens C., and Patel V.P. Fibronectin and VLA-4 in haematopoietic stem cell-microenvironment interactions. Nature 352 (1991) 438-441
    • (1991) Nature , vol.352 , pp. 438-441
    • Williams, D.A.1    Rios, M.2    Stephens, C.3    Patel, V.P.4
  • 26
    • 0022575635 scopus 로고
    • The fibronectin receptor on mammalian erythroid precursor cells: characterization and developmental regulation
    • Patel V.P., and Lodish H.F. The fibronectin receptor on mammalian erythroid precursor cells: characterization and developmental regulation. J Cell Biol 102 (1986) 449-456
    • (1986) J Cell Biol , vol.102 , pp. 449-456
    • Patel, V.P.1    Lodish, H.F.2
  • 27
    • 0023546121 scopus 로고
    • A fibronectin matrix is required for differentiation of murine erythroleukemia cells into reticulocytes
    • Patel V.P., and Lodish H.F. A fibronectin matrix is required for differentiation of murine erythroleukemia cells into reticulocytes. J Cell Biol 105 (1987) 3105-3118
    • (1987) J Cell Biol , vol.105 , pp. 3105-3118
    • Patel, V.P.1    Lodish, H.F.2
  • 28
    • 0023180454 scopus 로고
    • Differential binding of erythroid and myeloid progenitors to fibroblasts and fibronectin
    • Tsai S., Patel V., Beaumont E., Lodish H.F., Nathan D.G., and Sieff C.A. Differential binding of erythroid and myeloid progenitors to fibroblasts and fibronectin. Blood 69 (1987) 1587-1594
    • (1987) Blood , vol.69 , pp. 1587-1594
    • Tsai, S.1    Patel, V.2    Beaumont, E.3    Lodish, H.F.4    Nathan, D.G.5    Sieff, C.A.6
  • 29
    • 14444272787 scopus 로고    scopus 로고
    • Expression and function of integrins on hematopoietic progenitor cells
    • Coulombel L., Auffray I., Gaugler M.H., and Rosemblatt M. Expression and function of integrins on hematopoietic progenitor cells. Acta Haematol 97 (1997) 13-21
    • (1997) Acta Haematol , vol.97 , pp. 13-21
    • Coulombel, L.1    Auffray, I.2    Gaugler, M.H.3    Rosemblatt, M.4
  • 30
    • 0027131853 scopus 로고
    • Integrin alpha 4 beta 1 and glycoprotein IV (CD36) are expressed on circulating reticulocytes in sickle cell anemia
    • Joneckis C.C., Ackley R.L., Orringer E.P., Wayner E.A., and Parise L.V. Integrin alpha 4 beta 1 and glycoprotein IV (CD36) are expressed on circulating reticulocytes in sickle cell anemia. Blood 82 (1993) 3548-3555
    • (1993) Blood , vol.82 , pp. 3548-3555
    • Joneckis, C.C.1    Ackley, R.L.2    Orringer, E.P.3    Wayner, E.A.4    Parise, L.V.5
  • 31
    • 0027184968 scopus 로고
    • Alpha 4 beta 1-integrin expression on sickle reticulocytes: vascular cell adhesion molecule-1-dependent binding to endothelium
    • Swerlick R.A., Eckman J.R., Kumar A., Jeitler M., and Wick T.M. Alpha 4 beta 1-integrin expression on sickle reticulocytes: vascular cell adhesion molecule-1-dependent binding to endothelium. Blood 82 (1993) 1891-1899
    • (1993) Blood , vol.82 , pp. 1891-1899
    • Swerlick, R.A.1    Eckman, J.R.2    Kumar, A.3    Jeitler, M.4    Wick, T.M.5
  • 32
    • 0029957666 scopus 로고    scopus 로고
    • Phorbol ester stimulation increases sickle erythrocyte adherence to endothelium: a novel pathway involving alpha 4 beta 1 integrin receptors on sickle reticulocytes and fibronectin
    • Kumar A., Eckmam J.R., Swerlick R.A., and Wick T.M. Phorbol ester stimulation increases sickle erythrocyte adherence to endothelium: a novel pathway involving alpha 4 beta 1 integrin receptors on sickle reticulocytes and fibronectin. Blood 88 (1996) 4348-4358
    • (1996) Blood , vol.88 , pp. 4348-4358
    • Kumar, A.1    Eckmam, J.R.2    Swerlick, R.A.3    Wick, T.M.4
  • 33
    • 5644298408 scopus 로고    scopus 로고
    • Mechanism of CD47-induced alpha4beta1 integrin activation and adhesion in sickle reticulocytes
    • Brittain J.E., Han J., Ataga K.I., Orringer E.P., and Parise L.V. Mechanism of CD47-induced alpha4beta1 integrin activation and adhesion in sickle reticulocytes. J Biol Chem 279 (2004) 42393-42402
    • (2004) J Biol Chem , vol.279 , pp. 42393-42402
    • Brittain, J.E.1    Han, J.2    Ataga, K.I.3    Orringer, E.P.4    Parise, L.V.5


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