| Autor: |
Wang XM; Institut Pasteur de Bruxelles, Belgium., Wilkin JM, Boisteau O, Harmegnies D, Blanc C, Vandenbussche P, Montero-Julian FA, Jacques Y, Content J |
| Jazyk: |
angličtina |
| Zdroj: |
European journal of biochemistry [Eur J Biochem] 2002 Jan; Vol. 269 (1), pp. 61-8. |
| DOI: |
10.1046/j.0014-2956.2002.02622.x |
| Abstrakt: |
Human interleukin-11 (hIL-11) is a pleiotropic cytokine that is involved in numerous biological activities such as hematopoiesis, osteoclastogenesis, neurogenesis and female fertility. IL-11 is obviously a key reagent to study the IL-11 receptors. However, conventional radio-iodination techniques lead to a loss of IL-11 bioactivity. Here, we report the construction and the production of a new recombinant human IL-11 (FP Delta IL-11). In this molecule, a specific phosphorylation site (RRASVA) has been introduced at the N-terminus of rhIL-11. It can be specifically phosphorylated by bovine heart protein kinase and accordingly, easily radiolabeled with (32)P. A high radiological specific activity (250,000 c.p.m x ng(-1) of protein) was obtained with the retention of full biological activity of the protein. The binding of (32)P-labeled FP Delta IL-11 to Ba/F3 cells stably transfected with plasmids encoding human IL-11 receptors alpha and beta chains (IL-11R alpha and gp130) was specific and saturable with a high affinity as determined from Scatchard plot analysis. Availability of this new ligand should prompt further studies on IL-11R structure, expression and regulation. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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