REFERENCES
- El Nemer W., Gane P., Colin Y., Bony V., Rahuel C., Galacteros F., Cartron J. P., Le Van Kim C. The Lutheran blood group glycoproteins, the erythroid receptors for laminin, are adhesion molecules. J. Biol. Chem. 1998; 273: 16686–16693, [PUBMED], [INFOTRIEVE], [CSA]
- Udani M., Zen Q., Cottman M., Leonard N., Jefferson S., Daymont C., Truskey G., Telen M. J. Basal cell adhesion molecule/lutheran protein. The receptor critical for sickle cell adhesion to laminin. J. Clin. Invest. 1998; 101: 2550–2558, [PUBMED], [INFOTRIEVE], [CSA]
- Burgeson R. E., Chiquet M., Deutzmann R., Ekblom P., Engel J., Kleinman H., Martin G. R., Meneguzzi G., Paulsson M., Sanes J., Timpl R., Tryggvason K., Yamada Y., Yurchenco P. D. A new nomenclature for the laminins. Matrix Biol. 1994; 14: 209–211, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Miner J. H., Patton B. L., Lentz S. I., Gilbert D. J., Snider W. D., Jenkins N. A., Copeland N. G., Sanes J. R. The laminin α chains: expression, developmental transitions, and chromosomal locations of α 1–5, identification of heterotrimeric laminins 8–11, and cloning of a novel α3 isoform. J. Cell Biol. 1997; 137: 685–701, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Koch M., Olson P. F., Albus A., Jin W., Hunter D. D., Brunken W. J., Burgeson R. E., Champliaud M. F. Characterization and expression of the laminin γ3 chain: a novel, non-basement membrane-associated, laminin chain. J. Cell Biol. 1999; 145: 605–618, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Libby R. T., Champliaud M. F., Claudepierre T., Xu Y., Gibbons E. P., Koch M., Burgeson R. E., Hunter D. D., Brunken W. J. Laminin expression in adult and developing retinae: evidence of two novel CNS laminins. J. Neurosci. 2000; 20: 6517–6528, [PUBMED], [INFOTRIEVE], [CSA]
- Champliaud M. F., Virtanen I., Tiger C. F., Korhonen M., Burgeson R., Gullberg D. Posttranslational modifications and β/γ chain associations of human laminin α 1 and laminin α 5 chains: purification of laminin-3 from placenta. Exp. Cell Res. 2000; 259: 326–335, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Aumailley M., Smyth N. The role of laminins in basement membrane function. J. Anat. 1998; 193: 1–21, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Colognato H., Yurchenco P. D. Form and function: the laminin family of heterotrimers. Dev. Dyn. 2000; 218: 213–234, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Belkin A. M., Stepp M. A. Integrins as receptors for laminins. Microsc. Res. Tech. 2000; 51: 280–301, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Henry M. D., Campbell K. P. Dystroglycan inside and out. Curr. Opin. Cell Biol. 1999; 11: 602–607, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Salmivirta M., Mali M., Heino J., Hermonen J., Jalkanen M. A novel laminin-binding form of syndecan-1 (cell surface proteoglycan) produced by syndecan-1 cDNA-transfected NIH-3T3 cells. Exp. Cell. Res. 1994; 215: 180–188, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Hoffman M. P., Nomizu M., Roque E., Lee S., Jung D. W., Yamada Y., Kleinman H. K. Laminin-1 and laminin-2 G-domain synthetic peptides bind syndecan-1 and are involved in acinar formation of a human submandibular gland cell line. J. Biol. Chem. 1998; 273: 28633–28641, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- van der Flier A., Sonnenberg A. Function and interactions of integrins. Cell Tissue Res. 2001; 305: 285–298, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Kikkawa Y., Moulson C. L., Virtanen I., Miner J. H. Identification of the binding site for the Lutheran blood group glycoprotein on laminin α 5 through expression of chimeric laminin chains in vivo. J. Biol. Chem. 2002; 277: 44864–44869, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Miner J. H., Cunningham J., Sanes J. R. Roles for laminin in embryogenesis: exencephaly, syndactyly, and placentopathy in mice lacking the laminin α 5 chain. J. Cell Biol. 1998; 143: 1713–1723, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Miner J. H., Li C. Defective glomerulogenesis in the absence of laminin α 5 demonstrates a developmental role for the kidney glomerular basement membrane. Dev. Biol. 2000; 217: 278–289, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Nguyen N. M., Miner J. H., Pierce R. A., Senior R. M. Laminin α 5 is required for lobar septation and visceral pleural basement membrane formation in the developing mouse lung. Dev. Biol. 2002; 246: 231–244, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Bolcato-Bellemin A. L., Lefebvre O., Arnold C., Sorokin L., Miner J. H., Kedinger M., Simon-Assmann P. Laminin α 5 chain is required for intestinal smooth muscle development. Dev. Biol. 2003; 260: 376–390, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Kikkawa Y., Virtanen I., Miner J. H. Mesangial cells organize the glomerular capillaries by adhering to the G domain of laminin α 5 in the glomerular basement membrane. J. Cell Biol. 2003; 161: 187–196, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Li J., Tzu J., Chen Y., Zhang Y. P., Nguyen N. T., Gao J., Bradley M., Keene D. R., Oro A. E., Miner J. H., Marinkovich M. P. Laminin-10 is crucial for hair morphogenesis. EMBO J. 2003; 22: 2400–2410, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Kikkawa Y., Sanzen N., Sekiguchi K. Isolation and characterization of laminin-10/11 secreted by human lung carcinoma cells: laminin-10/11 mediates cell adhesion through integrin α 3β 1. J. Biol. Chem. 1998; 273: 15854–15859, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Kikkawa Y., Sanzen N., Fujiwara H., Sonnenberg A., Sekiguchi K. Integrin binding specificity of laminin-10/11: laminin-10/11 are recognized by α 3β 1, α 6β 1 and α 6β 4 integrins. J. Cell Sci. 2000; 113: 869–876, [PUBMED], [INFOTRIEVE], [CSA]
- Shimizu H., Hosokawa H., Ninomiya H., Miner J. H., Masaki T. Adhesion of cultured bovine aortic endothelial cells to laminin-1 mediated by dystroglycan. J. Biol. Chem. 1999; 274: 11995–12000, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Campbell I. G., Foulkes W. D., Senger G., Trowsdale J., Garin-Chesa P., Rettig W. J. Molecular cloning of the B-CAM cell surface glycoprotein of epithelial cancers: a novel member of the immunoglobulin superfamily. Cancer Res. 1994; 54: 5761–5765, [PUBMED], [INFOTRIEVE], [CSA]
- Parsons S. F., Mallinson G., Holmes C. H., Houlihan J. M., Simpson K. L., Mawby W. J., Spurr N. K., Warne D., Barclay A. N., Anstee D. J. 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 1995; 92: 5496–5500, [PUBMED], [INFOTRIEVE], [CSA]
- Rahuel C., Le Van Kim C., Mattei M. G., Cartron J. P., Colin Y. A unique gene encodes spliceoforms of the B-cell adhesion molecule cell surface glycoprotein of epithelial cancer and of the Lutheran blood group glycoprotein. Blood 1996; 88: 1865–1872, [PUBMED], [INFOTRIEVE], [CSA]
- Rahuel C., Colin Y., Goossens D., Gane P., El Nemer W., Cartron J. P., Le Van Kim C. Characterization of a mouse liminin receptor gene homologous to the human blood group Lutheran gene. Immunogenetics 1999; 50: 271–277, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Parsons S. F., Lee G., Spring F. A., Willig T. N., Peters L. L., Gimm J. A., Tanner M. J., Mohandas N., Anstee D. J., Chasis J. A. Lutheran blood group glycoprotein and its newly characterized mouse homologue specifically bind α 5 chain-containing human laminin with high affinity. Blood 2001; 97: 312–320, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Shih I. M. The role of CD146 (Mel-CAM) in biology and pathology. J. Pathol. 1999; 189: 4–11, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Bowen M. A., Patel D. D., Li X., Modrell B., Malacko A. R., Wang W. C., Marquardt H., Neubauer M., Pesando J. M., Francke U., Haynes B. F., Aruffo A. Cloning, mapping, and characterization of activated leukocyte-cell adhesion molecule (ALCAM), a CD6 ligand. J. Exp. Med. 1995; 181: 2213–2220, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Pourquie O., Corbel C., Le Caer J. P., Rossier J., Le Douarin N. M. BEN, a surface glycoprotein of the immunoglobulin superfamily, is expressed in a variety of developing systems. Proc. Natl. Acad. Sci. USA 1992; 89: 5261–5265, [PUBMED], [INFOTRIEVE], [CSA]
- Burns F. R., von Kannen S., Guy L., Raper J. A., Kamholz J., Chang S. DM-GRASP, a novel immunoglobulin superfamily axonal surface protein that supports neurite extension. Neuron 1991; 7: 209–220, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Tanaka H., Matsui T., Agata A., Tomura M., Kubota I., McFarland K. C., Kohr B., Lee A., Phillips H. S., Shelton D. L. Molecular cloning and expression of a novel adhesion molecule, SC1. Neuron 1991; 7: 535–545, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Peduzzi J. D., Irwin M. H., Geisert E. E., Jr. Distribution and characteristics of a 90 kDa protein, KG-CAM, in the rat CNS. Brain Res. 1994; 640: 296–307, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Paschke K. A., Lottspeich F., Stuermer C. A. Neurolin, a cell surface glycoprotein on growing retinal axons in the goldfish visual system, is reexpressed during retinal axonal regeneration. J. Cell Biol. 1992; 117: 863–875, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- El Nemer W., Rahuel C., Colin Y., Gane P., Cartron J. P., Le Van Kim C. Organization of the human LU gene and molecular basis of the Lu(a)/Lu(b) blood group polymorphism. Blood 1997; 89: 4608–4616, [PUBMED], [INFOTRIEVE], [CSA]
- Parsons S. F., Mallinson G., Daniels G. L., Green C. A., Smythe J. S., Anstee D. J. Use of domain-deletion mutants to locate Lutheran blood group antigens to each of the five immunoglobulin superfamily domains of the Lutheran glycoprotein: elucidation of the molecular basis of the Lu(a)/Lu(b) and the Au(a)/Au(b) polymorphisms. Blood 1997; 89: 4219–4225, [PUBMED], [INFOTRIEVE], [CSA]
- Daniels G. Human Blood Groups. Blackwell Scientific Publications, Oxford 2002; 275–294
- Crew V. K., Green C., Daniels G. Molecular bases of the antigens of the Lutheran blood group system. Transfusion 2003; 43: 1729–1737, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Moulson C. L., Li C., Miner J. H. Localization of Lutheran, a novel laminin receptor, in normal, knockout, and transgenic mice suggests an interaction with laminin α 5 in vivo. Dev. Dyn. 2001; 222: 101–114, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Rettig W. J., Dracopoli N. C., Goetzger T. A., Spengler B. A., Biedler J. L., Oettgen H. F., Old L. J. Somatic cell genetic analysis of human cell surface antigens: chromosomal assignments and regulation of expression in rodent-human hybrid cells. Proc. Natl. Acad. Sci. USA 1984; 81: 6437–6441, [PUBMED], [INFOTRIEVE], [CSA]
- Rettig W. J., Chesa P. G., Beresford H. R., Feickert H. J., Jennings M. T., Cohen J., Oettgen H. F., Old L. J. Differential expression of cell surface antigens and glial fibrillary acidic protein in human astrocytoma subsets. Cancer Res. 1986; 46: 6406–6412, [PUBMED], [INFOTRIEVE], [CSA]
- Bernemann T. M., Podda M., Wolter M., Boehncke W. H. Expression of the basal cell adhesion molecule (B-CAM) in normal and diseased human skin. J. Cutan. Pathol. 2000; 27: 108–111, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Drewniok C., Wienrich B. G., Schon M., Ulrich J., Zen Q., Telen M. J., Hartig R. J., Wieland I., Gollnick H., Schon M. P. Molecular interactions of B-CAM (basal-cell adhesion molecule) and laminin in epithelial skin cancer. Arch. Dermatol. Res. 2004; 296: 59–66, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Schon M., Klein C. E., Hogenkamp V., Kaufmann R., Wienrich B. G., Schon M. P. Basal-cell adhesion molecule (B-CAM) is induced in epithelial skin tumors and inflammatory epidermis, and is expressed at cell-cell and cell-substrate contact sites. J. Invest. Dermatol. 2000; 115: 1047–1053, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Judson P. A., Spring F. A., Parsons S. F., Anstee D. J., Mallinson G. Report on group 8 (Lutheran) antibodies. Rev. Fr. Transfus. Immunohematol. 1988; 31: 433–440, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Southcott M. J., Tanner M. J., Anstee D. J. The expression of human blood group antigens during erythropoiesis in a cell culture system. Blood 1999; 93: 4425–4435, [PUBMED], [INFOTRIEVE], [CSA]
- Bony V., Gane P., Bailly P., Cartron J. P. Time-course expression of polypeptides carrying blood group antigens during human erythroid differentiation. Br. J. Haematol. 1999; 107: 263–274, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Gu Y., Sorokin L., Durbeej M., Hjalt T., Jonsson J. I., Ekblom M. Characterization of bone marrow laminins and identification of α 5-containing laminins as adhesive proteins for multipotent hematopoietic FDCP-Mix cells. Blood 1999; 93: 2533–2542, [PUBMED], [INFOTRIEVE], [CSA]
- Ferletta M., Ekblom P. Identification of laminin-10/11 as a strong cell adhesive complex for a normal and a malignant human epithelial cell line. J. Cell Sci. 1999; 112: 1–10, [PUBMED], [INFOTRIEVE], [CSA]
- El Nemer W., Gane P., Colin Y., D'Ambrosio A. M., Callebaut I., Cartron J. P., Van Kim C. L. Characterization of the laminin binding domains of the Lutheran blood group glycoprotein. J. Biol. Chem. 2001; 276: 23757–23762, [PUBMED], [INFOTRIEVE], [CSA]
- Zen Q., Cottman M., Truskey G., Fraser R., Telen M. J. Critical factors in basal cell adhesion molecule/lutheran-mediated adhesion to laminin. J. Biol. Chem. 1999; 274: 728–734, [PUBMED], [INFOTRIEVE], [CSA]
- Timpl R., Tisi D., Talts J. F., Andac Z., Sasaki T., Hohenester E. Structure and function of laminin LG modules. Matrix Biol. 2000; 19: 309–317, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Ido H., Harada K., Futaki S., Hayashi Y., Nishiuchi R., Natsuka Y., Li S., Wada Y., Combs A. C., Ervasti J. M., Sekiguchi K. Molecular dissection of the α-dystroglycan- and integrin-binding sites within the globular domain of human laminin-10. J. Biol. Chem. 2004; 279: 10946–10954, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Yu H., Chen J. K., Feng S., Dalgarno D. C., Brauer A. W., Schreiber S. L. Structural basis for the binding of proline-rich peptides to SH3 domains. Cell 1994; 76: 933–945, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Kroviarski Y., El Nemer W., Gane P., Rahuel C., Gauthier E., Lecomte M. C., Cartron J. P., Colin Y., Le Van Kim C. Direct interaction between the Lu/B-CAM adhesion glycoproteins and erythroid spectrin. Br. J. Haematol. 2004; 126: 255–264, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- El Nemer W., Colin Y., Bauvy C., Codogno P., Fraser R. H., Cartron J. P., Le Van Kim C. L. 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. 1999; 274: 31903–31908, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Hines P. C., Zen Q., Burney S. N., Shea D. A., Ataga K. I., Orringer E. P., Telen M. J., Parise L. V. Novel epinephrine and cyclic AMP-mediated activation of BCAM/Lu-dependent sickle (SS) RBC adhesion. Blood 2003; 101: 3281–3287, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Hillery C. A., Du M. C., Montgomery R. R., Scott J. P. Increased adhesion of erythrocytes to components of the extracellular matrix: isolation and characterization of a red blood cell lipid that binds thrombospondin and laminin. Blood 1996; 87: 4879–4886, [PUBMED], [INFOTRIEVE], [CSA]
- Lee S. P., Cunningham M. L., Hines P. C., Joneckis C. C., Orringer E. P., Parise L. V. Sickle cell adhesion to laminin: potential role for the α 5 chain. Blood 1998; 92: 2951–2958, [PUBMED], [INFOTRIEVE], [CSA]
- Zen Q., Batchvarova M., Twyman C. A., Eyler C. E., Qiu H., De Castro L. M., Telen M. J. B-CAM/LU expression and the role of B-CAM/LU activation in binding of low- and high-density red cells to laminin in sickle cell disease. Am. J. Hematol. 2004; 75: 63–72, [PUBMED], [INFOTRIEVE], [CSA], [CROSSREF]
- Garin-Chesa P., Sanz-Moncasi M. -P., Campbell I. G., Rettig W. J. Non-polarized expression of basal cell adhesion molecule B-CAM in epithelial ovarian cancers. Int. J. Oncol. 1994; 5: 1261–1266, [CSA]
- Rettig W. J., Garin-Chesa P., Beresford H. R., Oettgen H. F., Melamed M. R., Old L. J. Cell-surface glycoproteins of human sarcomas: differential expression in normal and malignant tissues and cultured cells. Proc. Natl. Acad. Sci. USA 1988; 85: 3110–3114, [PUBMED], [INFOTRIEVE], [CSA]
- Harlan J. M. Introduction: anti-adhesion therapy in sickle cell disease. Blood 2000; 95: 365–367, [PUBMED], [INFOTRIEVE], [CSA]