11
Views
4
CrossRef citations to date
0
Altmetric
Original Article

Cloning and sequencing of an ovine interleukin-5 cDNA

, , , &
Pages 331-335 | Published online: 11 Jul 2009

References

  • Azuma C., Tanabe T., Konishi M., Kinashi T., Noma T., Matsuda F., Yaoita Y., Takatsu K., Hammarstroem L., et al. “Cloning of cDNA for human T-cell replacing factor (interleukin-5) and comparison with the murine homologue”. Nucl. Acid. Res. 1986; 14: 9149–9158
  • Campbell H. D., Tucker W. Q.J., Hort Y., Martinson M. E., Mayo G., Clutterbuck E. J., Sanderson C. J., Young I. G. “Molecular cloning, nucleotide sequence, and expression of the gene encoding human eosinophil differentation factor (inter-leukin 5)”. Proc. Natl. Acad. Sci. USA 1987; 84: 6629–6633
  • Campbell H. D., Sanderson C. J., Wang Y., Hort Y., Martinson M. E., Tucker W. Q., Stellwagen A., Strath M., Young I. G. “Isolation, structure and expression of cDNA and genomic clones for murine eosinophil differentiation factor. Comparison with other eosinophilopoietic lymphokines and identity with interleukin-5”. Eur. Biochem J. 1988; 174: 345–352
  • Coffman R. L., Seymour B. W.P., Hudak S., Jackson J., Rennick D. “Antibody to interleukin-5 inhibits helminth-induced eosinophilia in mice”. Science 1989; 245: 308–310
  • Comelis S., Plaetinck G., Devos R., Vahderheyden J., Tavernier J., Sanderson C. J., Guisez Y., Fiers W. “Detailed analysis of the IL-5-IL-5R-alpha interaction-characterisation of crucial residues on the ligand and the receptor”. Embo J. 1995; 14: 3395–3402
  • Dent L. A., Strath M., Mellor A. L., Sanderson C. J. “Eosinophilia in transgenic mice expressing interleukin 5”. Exp. J. Med. 1990; 172: 1425–1431
  • Devos R., Plaetinck G., Van-Der-Heyden J., Comelis S., Van-Dekerckhove J., Fiers W., Tavernier J. “Molecular basis of a high affinity murine interleukin-5”. Embo J. 1991a; 10: 2133–2137
  • Devos R., Vandekerckhove J., Rolink A., Plaetinck G., Van-Der-Heyden J., Fiers W., Tavernier J. “Amino acid sequence analysis of a mouse interleukin 5 receptor protein reveals homology with a mouse interleukin 3 receptor protein”. Eur. Immunol J. 1991b; 21: 1315–1318
  • Graber P., Proudfoot A. E.I., Talabot F., Bernard A., McKinnon M., Banks M., Fattah D., Solari R., Peitsch M. C., Wells T. N.C. “Identification of key charged residues of human interleukin-5 in receptor binding and cellular activation”. Biol J. Chem. 1995; 270: 15762–15769
  • Jones D. G. “The Eosinophil”. J. Comp. Path. 1993; 108: 317–335
  • Kinashi T., Harada N., Severinson E., Tanabe T., Sideras P., Konishi M., Azuma C., Tominaga A., Bergstedt-Lindqvist S., et al. “Cloning of complementary DNA encoding T-cell replacing factor and identity with B-cell growth factor II”. Nature 1986; 234: 70–72
  • Koyama N., Harada N., Takahashi T., Mita S., Okamura H., Tominaga A., Takatsu K. “Role of recombinant inter-leukin-1 compared to recombinant T-cell replacing factor/inter-leukin-5 in B-cell differentiation”. Immunology 1988; 63: 277–283
  • Lopez A. F., Vadas A., Woodcock J. M., Milton S. E., Lewis A., Elliott M. J., Gillis D., Ireland R., Olwell E., Park L. S. “Interleukin-5, interIeukin-3 and granulocyte-macrophage colony-stimulating factor cross-compete for binding to cell surface respectors on human eosinophils”. J. Biol. Chem. 1991; 266: 24741–24747
  • McKenzie A. N.J., Ely B., Sanderson C. J. “Mutated interleukin-5 monomers are biologically inactive”. Mol. Immunol. 1991a; 28: 155–158
  • McKenzie A. N.J., Barry S. C., Strath M., Sanderson C. J. “Structure-function analysis of interleukin-5 utilising mouse/human chimeric molecules”. Embo J. 1991b; 10: 1193–1199
  • Milburn M. V., Hassell A. M., Lambert M. H., Jordan S. R., Proudfoot A. E.I., Graber P., Wells T. N.C. “A novel dimer configuration revealed by the crystal structure at 2.4 Angstroms resolution of human interleukin-5”. Nature 1993; 363: 172–176
  • Minamitake Y., Kodama S., Katayama T., Adachi H., Tanaka S., Tsujimoto M. “Structure of recombinant human interleukin 5 produced by Chinese hamster ovary cells”. J. Biochem. 1990; 107: 292–297
  • Mizuta T. R., Tanabe T., Nakakubo H., Noma T., Honjo T. “Molecular cloning and structure of the mouse intereleukin-5 gene”. Growth Factors 1989; 1: 51–57
  • Murata Y., Takaki S., Migita M., Kikuchi Y., Tominaga A., Takatsu K. “Molecular cloning and expression of the human interleukin 5 receptor”. J. Exp. Med. 1992; 175: 341–351
  • Sanderson C. D., Warren D. J., Strath M. “Identification of a lymphokine that stimulates eosinophil differentation in vitro”. J. Exp. Med. 1985; 162: 60–74
  • Sanderson C. J., Campbell H. D., Young I. G. “Molecular and cellular biology of eosinophil differentiation factor (interleukin-5) and its effects on human and mouse B cells”. Immunol. Rev. 1988; 102: 29–50
  • Sonda E., Hitoshi Y., Yamaguchi N., Ishi T., Tominaga A., Araki S., Takatsu K. “Differential Regulation of IgA production by TCF-β and IL-5, TGF-β induces surface IgA-positive cells bearing IL-5 receptor, whereas IL-5 promotes their survival and maturation into IgA-secreting cells”. Cell. Immunol. 1992; 140: 158–172
  • Stevenson L. M., Jones D. G. “Cross-reactivity amongst recombinant haematopoietic cytokines from different species for sheep bone-marrow eosinophils”. J. Comp. Path. 1994; 111: 99–106
  • Tavernier J., Devos R., Cornelis S., Tuypens T., Van-Der-Heyden J., Fiers W., Plaetinck G. “A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific alpha chain and a beta chain shared with the receptor for GM-CS”. Cell 1991; 66: 1175–1184
  • Tavernier J., Tuypens T., Verhee A., Plaetinck G., Devos R., Vanderheyden J., Guisez Y., Oefner C. “Identification of receptor-binding domains on human interleukin 5 and design of an interleukin 5-derived receptor antagonist”. Proc. Natl. Acad. Sci. USA 1995; 92: 5194–5198
  • Ueberla K., Li W., Qin Z., Richter G., Raabe T., Diamantstein T., Blankenstein T. “The rat interleukin-5 gene: Characterisation and expression by retroviral gene transfer and polymerase chain reaction”. Cytokine 1991; 3: 72–81

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.