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Figure 7 | Journal of Inflammation

Figure 7

From: Salivary histatin 3 inhibits heat shock cognate protein 70-mediated inflammatory cytokine production through toll-like receptors in human gingival fibroblasts

Figure 7

MAPK phosphorylation and IκB-α degradation induced by HSC70 and the effect of histatin 3. (A) MAPK and IκB-α phosphorylation and IκB-α degradation after HSC70 or LPS stimulation. HGFs were stimulated with LPSs or HSC70 for the indicated time periods. Phosphorylation of p42/44 (ERK), JNK, p38, and IκB-α (pp42/44, pJNK, pp38, and pIκB-α) and degradation of IκB-α were examined by Western blotting with the respective antibodies. (B) Densitometry analysis of Western blotting from (A). Phosphorylation of p42/44, JNK, p38, and IκB-α was quantified as levels relative to respective MAPKs and IκB-α after normalization with β-actin. Bars represent the means of 3 experiments; error bars show standard deviations. The values are shown as fold induction of phosphorylation over the “0 min” sample. *, P < 0.05; **, p < 0.01; ***, p < 0.001. (C) Histatin 3 inhibition of HSC70-stimulated p42/44 phosphorylation and IκB-α degradation. HGFs were stimulated with HSC70 in the presence of control peptide (cont. pep.) or histatin3 for 30 min. The effects of histatin 3 on p42/44 phosphorylation and IκB-α degradation were examined by Western blotting with the indicated antibodies. (D) Phosphorylation of p42/44 was quantified as levels relative to p42/44 after normalization with β-actin. Bars represent the means of 3 experiments; error bars show standard deviations. The values are shown as fold induction of phosphorylation over the “0 min” sample.

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