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Article Dans Une Revue Cytokine Année : 2013

The disulfide bond between cysteine 10 and cysteine 34 is required for CCL18 activity.

Résumé

Asthma is a Th2-mediated disease that involves Th2 cell and eosinophil migration into the bronchial mucosa which is dependent upon the expression of a specific set of chemokines within the lung. Among them, CCL18 seems to play a key role because of its preferential expression in the lung, and its up-regulation by Th2 cytokines. Here, we show that the optimal naïve T cell and basophil chemotaxis, and basophil histamine release induced by rhCCL18 occurred at a 100 time lower concentration with CHO-derived rhCCL18 than with E. coli-derived rhCCL18. FT-ICR mass spectrometry of the intact chemokines showed that the rhCCL18 produced by CHO cells contained the 2 disulfide bonds Cys10-Cys34 and Cys11-Cys50, in clear contrast to the rhCCL18 derived from E. coli where the Cys10-Cys34 bond was absent. We found that reduction of the Cys10-Cys34 of the CHO-derived rhCCL18 resulted in a shift of its activity, reaching the same level as the E. coli-derived rhCCL18. These results demonstrate that the Cys10-Cys34 disulfide bond is involved in the function of CCL18.

Dates et versions

hal-00871113 , version 1 (08-10-2013)

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Citer

Benjamin Legendre, Caroline Tokarski, Ying Chang, Nathalie de Freitas Caires, Hugues Lortat-Jacob, et al.. The disulfide bond between cysteine 10 and cysteine 34 is required for CCL18 activity.. Cytokine, 2013, 64 (1), pp.463-70. ⟨10.1016/j.cyto.2013.04.028⟩. ⟨hal-00871113⟩
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