Canine interleukin-13: Molecular cloning of full-length cDNA and expression of biologically active recombinant protein

Citation
Sm. Yang et al., Canine interleukin-13: Molecular cloning of full-length cDNA and expression of biologically active recombinant protein, J INTERF CY, 20(9), 2000, pp. 779-785
Citations number
30
Categorie Soggetti
Immunology
Journal title
JOURNAL OF INTERFERON AND CYTOKINE RESEARCH
ISSN journal
10799907 → ACNP
Volume
20
Issue
9
Year of publication
2000
Pages
779 - 785
Database
ISI
SICI code
1079-9907(200009)20:9<779:CIMCOF>2.0.ZU;2-9
Abstract
Interleukin-13 (IL-13) regulates immune responses mediated by type 2 T help er lymphocytes (Th2) in the human and mouse. To study the function of this cytokine in the dog, we have isolated a cDNA that encodes the full-length c anine IL-13 (CaIL-13) precursor polypeptide of 131 amino acids. CaIL-13 sha res significant homology with the IL-13 amino acid sequences of cattle (54. 1%), mouse (39.6%), and rat (36.6%) but shares the highest identity with hu man IL-13 (HuIL-13) (61.8%), The predicted CaIL-13 mature polypeptide of 11 1 residues was expressed in bacteria, and recombinant CaIL-13 (rCaIL-13) wa s isolated from inclusion bodies and refolded. rCaIL-13 stimulated the prol iferation of TF-1 cells, which are derived from human erythroleukemia cells and respond to IL-13 as well as to a number of other human and murine cyto kines, CaIL-13 mRNA was readily detectable by reverse transcriptase-polymer ase chain reaction (RT-PCR) in cells from lymph nodes and peripheral blood. The gene sequence and biologically active recombinant protein for CaIL-13 will be useful reagents to determine the role of IL-13 in the regulation of canine immune responses.