Figure 2. The effect of ET and thymulin pretreatment on IκB-α. Regulated by an upstream kinase (IKK), IκB-α is phosphorylated prior to the nuclear translocation of NF-κB. ET induced the phosphorylation of IκB-α, thereby tagging it for proteasome degradation, hence its cytosolic concentration was decreased (Lane-3). Thymulin, in a dose-dependent manner, reduced the phosphorylation of IκB-α, with maximal inhibitory effect at ICV concentration of 5μg (Lanes-4, 5 and 6). Thymulin restored IκB-α cytosolic accumulation, in a dose-dependent manner, consistent with the downregulation of its phosphorylation (Lanes-4, 5 and 6; Figure 2). Neither the control (Lane-1) nor thymulin alone (Lane-2) showed any effect on the phosphorylation of IκB-α, but there is constitutive expression as compared with ET alone. β-Actin standard was used as an internal reference for semi-quantitative loading in parallel lanes for each variable. n = 3 – 5, which represents the number of independent experiments in separate animals

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The Anti-Inflammatory and Immunomodulatory Activity of Thymulin Peptide is NF-κB-Dependent and Involves the Downregulation of IκB-α

John J. Haddad, Lama H. Hanbali

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