The disulfide bond between cysteine 10 and ...
Type de document :
Compte-rendu et recension critique d'ouvrage
PMID :
Titre :
The disulfide bond between cysteine 10 and cysteine 34 is required for CCL18 activity.
Auteur(s) :
Legendre, Benjamin [Auteur]
Tokarski, Caroline [Auteur]
Miniaturisation pour la Synthèse, l’Analyse et la Protéomique - UAR 3290 [MSAP]
Chang, Ying [Auteur]
de Freitas Caires, Nathalie [Auteur]
Lortat-Jacob, Hugues [Auteur]
Institut de biologie structurale [IBS - UMR 5075 ]
Nadaï, Patricia De [Auteur]
Rolando, Christian [Auteur]
Miniaturisation pour la Synthèse, l’Analyse et la Protéomique - UAR 3290 [MSAP]
Duez, Catherine [Auteur]
Biomolécules et inflammation pulmonaire
Tsicopoulos, Anne [Auteur]
Lassalle, Philippe [Auteur]
Biomolécules et inflammation pulmonaire
![refId](/themes/Mirage2//images/idref.png)
Tokarski, Caroline [Auteur]
Miniaturisation pour la Synthèse, l’Analyse et la Protéomique - UAR 3290 [MSAP]
Chang, Ying [Auteur]
de Freitas Caires, Nathalie [Auteur]
Lortat-Jacob, Hugues [Auteur]
Institut de biologie structurale [IBS - UMR 5075 ]
Nadaï, Patricia De [Auteur]
Rolando, Christian [Auteur]
![refId](/themes/Mirage2//images/idref.png)
Miniaturisation pour la Synthèse, l’Analyse et la Protéomique - UAR 3290 [MSAP]
Duez, Catherine [Auteur]
Biomolécules et inflammation pulmonaire
Tsicopoulos, Anne [Auteur]
Lassalle, Philippe [Auteur]
![refId](/themes/Mirage2//images/idref.png)
Biomolécules et inflammation pulmonaire
Titre de la revue :
Cytokine
Pagination :
463-70
Éditeur :
Elsevier
Date de publication :
2013-10
ISSN :
1043-4666
Discipline(s) HAL :
Sciences du Vivant [q-bio]/Biochimie, Biologie Moléculaire
Résumé en anglais : [en]
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 ...
Lire la suite >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.Lire moins >
Lire la suite >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.Lire moins >
Langue :
Anglais
Vulgarisation :
Non
Source :
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