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

作者信息

Yang S, Boroughs K L, McDermott M J

机构信息

Heska Corporation, Fort Collins, CO 80525, USA.

出版信息

J Interferon Cytokine Res. 2000 Sep;20(9):779-85. doi: 10.1089/10799900050151049.

Abstract

Interleukin-13 (IL-13) regulates immune responses mediated by type 2 T helper 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 canine IL-13 (CaIL-13) precursor polypeptide of 131 amino acids. CaIL-13 shares 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 human IL-13 (HuIL-13) (61.8%). The predicted CaIL-13 mature polypeptide of 111 residues was expressed in bacteria, and recombinant CaIL-13 (rCaIL-13) was isolated from inclusion bodies and refolded. rCaIL-13 stimulated the proliferation 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 cytokines. CaIL-13 mRNA was readily detectable by reverse transcriptase-polymerase 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.

摘要

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