Expression of a Soluble Functional Form of the Integrin α₄β₁ in Mammalian Cells

References

• Argraves W. S., Suzuki S., Arai H., Thompson K., Pierschbacher M. D., Ruoslahti E. Amino acid sequence of the human fibronectin receptor. Journal of Cell Biology 1987; 105: 1183–1190
   PubMed Web of Science ®Google Scholar
• Baneres J. L., Roquet F., Green M., LeCalvcz H., Parello J. The cation-binding domain from the alpha subunit of integrin alpha5 betal is a minimal domain for fibronectin recognition. Journal of Biological Chemistry. 1998; 273: 24744–24753
   PubMed Web of Science ®Google Scholar
• Bebbington C. Use of vectors based on gene amplification for the expression of cloned genes in mammalian cells. DNA Cloning 4, D. M. Glover, B. D. Hames. 1 RL Press. 1995; 85–110
   Google Scholar
• Bebbington C. R., Renner G., Thomson S., King D., Abrams D., Yarranton G. T. High-level expression of a recombinant antibody from myeloma cells using a glutamine synthetase gene as an amplifiable selectable marker. Bio/Technology 1992; 10: 169–175
   PubMed Web of Science ®Google Scholar
• Bednarczyk J. L., Szabo M. C., McLntyre B. W. Post-translational processing of the leukocyte integrin alpha 4 beta I. Journal of Biological Chemistry. 1992; 267: 25274–25281
   PubMed Web of Science ®Google Scholar
• Blue M. L., Davis G., Conrad P., Kelley K. Specific cleavage of the alpha 4 integrin associated with activation of peripheral T lymphocytes. Immunology. 1993; 78: 80–85
   PubMed Web of Science ®Google Scholar
• Briesewitz R., Kern A., Marcantonio E. E. Ligand-dependent and -independent integrin focal contact localization: the role of the alpha chain cytoplasmic domain. Molecular Biology of the Cell. 1993; 4: 593–604
   PubMed Web of Science ®Google Scholar
• Cierniewski C. S., Byzova T., Papierak M., Haas T. A., Niewiarowska J., Zhang L., Cieslak M., Plow E. F. Peptide ligands can bind to distinct sites in integrin alpha 1 lb/beta3 and elicit different functional responses. Journal of Biological Chemistry. 1999; 274: 16 923–16932
   Web of Science ®Google Scholar
• Cockett M. I., Bebbington C. R, Yarranton G. T. The use of engineered El A genes to transactivate the hCMV-MIE promoter in permanent CHO cell lines. Nucleic Acids Research. 1991; 19: 319–325
   PubMed Web of Science ®Google Scholar
• Cox D., Aoki T., Seki J., Motoyama Y., Yoshida K. The pharmacology of the integrins. [Review] [356 refs]. Medicinal Research Reyiens. 1994; 14: 195”–228
   PubMed Web of Science ®Google Scholar
• Denda S., Muller U., Crossin K. L., Erickson H. P., Reichardt L. F. Utilization of a soluble integrin-alkaline phosphatase chimera to characterize integrin alpha 8 beta 1 receptor interactions with tenascin: murine alpha 8 beta 1 binds to the RGD site in tenascin-C fragments, but not to native tenascin-C. Biochemistry 1998; 37: 5464–5474
   PubMed Web of Science ®Google Scholar
• De Melker A. A., Sonnenberg A. The role of the cytoplasmic domain of alpha 6 integrin in the assembly and function of alpha 6 beta I and alpha 6 beta 4. European Journal of Biochemistry. 1996; 241: 254–264
   PubMedGoogle Scholar
• Eble J. A., Wucherpfennig K. W., Gauthier L., Dersch P., Krukonis E., Isberg R. R., Hemler M. E. Recombinant soluble human alpha 3 beta 1 integrin: purification, processing, regulation, and specific binding to laminin-5 and invasin in a mutually exclusive manner. Biochemistry 1998; 37: 10945–10955
   PubMed Web of Science ®Google Scholar
• Gazdar A. F., Carney D. N., Bunn P. A., Russell E. K., Jaffe E. S., Schechter G. P., Guccion J. G. Mitogen requirements for the in vitro propagation of cutaneous T-cell lymphomas. Blood. 1980; 55: 409–417
   PubMed Web of Science ®Google Scholar
• Gulino D., Boudignon C., Zhang L. Y., Concord E., Rabiet M. J., Marguenc G. Ca(2+)-binding properties of the platelet glycoprotein lib ligand-interacting domain. Journal of Biological Chemistry 1992; 267: 1001–1007
   PubMed Web of Science ®Google Scholar
• Gulino D., Martinez P., Delachanal E., Concord E., Duperray A., Alemany M., Marguerie G. Expression and purification of a soluble functional form of the platelet alpha lib beta 3 integrin. European Journal of Biochemistry 1995; 227: 108–115
   PubMedGoogle Scholar
• Huang C., Lu C., Springer T. A. Folding of the conserved domain but not of flanking regions in the integrin beta2 subunit requires association with the alpha subunit. Proceedings of the National Academy of Sciences of the United States of A meriea 1997; 94: 3156–3161
   PubMed Web of Science ®Google Scholar
• Kabat E. A., Wu T. T., Reid-Miller M., Perry H. M., Gottesman K. S. Sequences of Proteins of Immunological Interest. United States Department of Health and Human Services., Washington, DC 1987
   Google Scholar
• Kassner P. D., Kawaguchi S., Hemler M. E. Minimum alpha chain cytoplasmic tail sequence needed to support integrin-mediated adhesion. Journal of Biological Chemistry 1994; 269: 19 859–19 867
   Web of Science ®Google Scholar
• Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680
   PubMed Web of Science ®Google Scholar
• LaFlamme S. E., Akiyama S. K., Yamada K. M. Regulation of fibronectin receptor distribution [published erratum in J. Cell Biol. 1992 118(2), 491]. Journal of Cell Biology. 1992; 117: 437–447
   PubMed Web of Science ®Google Scholar
• Lobb R. R., Antognelti G., Pepinsky R. B., Burkly L. C., Leone D. R., Whitty A. A direct binding assay for the vascular cell adhesion molecule-1 (VCAM1) interaction with alpha 4 integrins. Cell Adhesion & Communication 1995; 3: 385–397
   PubMed Web of Science ®Google Scholar
• Lobb R. R., Abraham W. M., Burkly L. C., Gill A., Ma W., Knight J. A., Leone D. R., Antognetti G., Pepinsky R. B. Pathophysiologic role of alpha 4 integrins in the lung. [Review] [47 refs]. Annals of the New York Academy of Sciences 1996; 796: 113–123
   PubMed Web of Science ®Google Scholar
• Lu C. F., Springer T. A. The alpha subunit cytoplasmic domain regulates the assembly and adhesiveness of integrin lymphocyte function-associated antigen-1. Journal of Immunology 1997; 159: 268–278
   PubMed Web of Science ®Google Scholar
• McKay B. S., Annis D. S., Honda S., Christie D., Kunicki T. J. Molecular requirements for assembly and function of a minimized human integrin alphallbbeta3. Journal of Biological Chemistry 1996; 271: 30 544–30 547
   PubMed Web of Science ®Google Scholar
• Mehta R. J., Diefenbach B., Brown A., Cullen E., Jonczyk A., Gussow D., Luckenbach G. A., Goodman S. L. Transmembrane-truncated alphavbeta3 integrin retains high affinity for ligand binding: evidence for an ‘inside-out‘ suppressor?. Biochemical Journal 1998; 330: 861–869
   PubMed Web of Science ®Google Scholar
• Metzger W. J. Therapeutic approaches to asthma based on VLA-4 integrin and its counter receptors. [Review] [65 refs]. Springer Seminars in Immunopathologv 1995; 16: 467–478
   PubMed Web of Science ®Google Scholar
• Mould A. P., Akiyama S. K., Humphries M. J. Regulation of integrin alpha 5 beta 1 -fibronectin interactions by divalent cations. Evidence for distinct classes of binding sites for Mn2+, Mg24 and Ca2. Journal of Biological Chemistry 1995; 270: 26270–26277
   PubMed Web of Science ®Google Scholar
• Ortlepp S., Stephens P. E., Hogg N., Figdor C. G., Robinson M. K. Antibodies that activate beta 2 integrins can generate different ligand binding states. European Journal of Immunology 1995; 25: 637–643
   PubMed Web of Science ®Google Scholar
• Osborn L., Hession C, Tizard R., Vassallo C., Luhowskyj S., Chi-Rosso G., Lobb R. Direct expression cloning of vascular cell adhesion molecule 1, a cytokine-induced endothelial protein that bind to lymphocytes. Cell 1989; 59: 1203–1211
   PubMed Web of Science ®Google Scholar
• Pardi R., Bossi G., Inverardi L., Rovida E., Bender J. R. Conserved regions in the cytoplasmic domains of the leukocyte integrin alpha L beta 2 are involved in endoplasmic reticulum retention, dimerization, and cytoskeletal association. Journal of Immunology 1995; 155: 1252–1263
   PubMed Web of Science ®Google Scholar
• Peterson J. A., Visentin G. P., Newman P. J., Aster R. H. A recombinant soluble form of the integrin alpha lib beta 3 (GPIIb-IIIa) assumes an active, ligand-binding conformation and is recognized by GPIIb-IIIa-specific monoclonal, alio-, auto-, and drug-dependent platelet antibodies. Blood 1998; 92: 2053–2063
   PubMed Web of Science ®Google Scholar
• Ridgway J. B., Presta L. G., Carter P. ‘Knobs-into-holes’ engineering of antibody CH3 domains for heavy chain heterodimerization. Protein Engineering 1996; 9: 617–621
   PubMedGoogle Scholar
• Sonnenberg A. Integrins and their ligands. [Review] [241 refs]. Current Topics in Microbiology & Immunology 1993; 184: 7–35
   PubMedGoogle Scholar
• Stephens P. E., Cockett M. I. The construction of a highly efficient and versatile set of mammalian expression vectors. Nucleic Acids Research 1989; 17: 7110
   PubMed Web of Science ®Google Scholar
• Szabo M. C., McLntyre B. W. Identification of two variants of the human Integrin alpha-4 subunit. Molecular Immunology 1995; 32: 1453–1454
   PubMed Web of Science ®Google Scholar
• Takada O., Elices M., Crouse C., Hemler M. The primary structure of the a4 subunit of VLA-4: homology of other integrins and a possible cell-cell adhesion function. EMBO journal 1989; 8: 1361–1368
   PubMed Web of Science ®Google Scholar
• Takahashi N., Ueda S., Obata M., Nikaido T., Nakai S., Honjo T. Structure of human immunoglobulin gamma genes: implications for evolution of a gene family. Cell 1982; 29: 671–679
   PubMed Web of Science ®Google Scholar
• Teixido J., Parker C M., Kassner P. D., Hemler M. E. Functional and structural analysis of VLA-4 integrin alpha 4 subunit cleavage. Journal of Biological Chemistry 1992; 267: 1786–1791
   PubMed Web of Science ®Google Scholar
• Tominaga Y., Kita Y., Uchiyama T., Sato K., Takashi T., Horiuchi T. Expression of a soluble form of LFA-1 and demonstration of its binding activity with 1CAM-1. Journal of Immunological Methods 1998; 212: 61–68
   PubMed Web of Science ®Google Scholar
• Tomonaga M., Gasson J. C., Quan S. G., Golde D. W. Establishment of eosinophillic sublines from human promyelocytic leukemia (HL60) cells: demonstration of mulitpotentiality and single-lineage commitment of HL-60 stem cells. Blood 1986; 67: 1433–1441
   PubMed Web of Science ®Google Scholar
• Whittle N., Adair J., Lloyd C., Jenkins E., Devine J., Schlom J., Raubitschek A., Colcher D., Bodmer M. Expression in COS cells of a mouse-human chimacric B72.3 antibody. Protein Engineering 1987; 1: 499–505
   PubMedGoogle Scholar
• Yauch R. L., Felsenfeld D. P., Kraeft S. K., Chen L. B., Sheetz M. P., Hemler M. E. Mutational evidence for control of cell adhesion through integrin diffusion/ clustering, independent of ligand binding. Journal of Experimental Medicine 1997; 186: 1347–1355
   PubMed Web of Science ®Google Scholar