Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9110807 | Cytokine | 2005 | 9 Pages |
Abstract
To direct the synthesis and secretion of recombinant human interleukin-11 (rhIL-11) in chicken HD11 cells, a plasmid targeting the c-lysozyme gene has been constructed which contains the mature cytokine cDNA in frame with the lysozyme leader sequence. The upregulation of rhIL-11 mediated by LPS proves the knock-in of hIL-11 cDNA in the lysozyme gene. The bioactivity of the expressed protein is demonstrated and quantified with the hIL-11 dependent 7TD1 and B9 cell lines. The electrophoretic mobility, receptor binding properties and growth promoting effect of the chicken-derived cytokine are identical to those of a rhIL-11 expressed in Escherichia coli. These results describe the secretion of a biologically active rhIL-11 expressed by an avian cellular machinery.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Endocrinology
Authors
Arnaud Léon, Xiao-Ming Wang, Patrick Champion-Arnaud, André Sobczyk, Bertrand Pain, Jean Content, Yannick Jacques, Isabelle Valarché,