Chemerin activates p44/42 mitogen-activated protein kinase, p38 mitogen-activated protein kinase and Akt in rheumatoid arthritis fibroblast-like synoviocytes. Rheumatoid arthritis (RA) fibroblast-like synoviocytes (FLSs) were left unstimulated (zero minutes) or stimulated with 10 nM chemerin for 5 to 30 minutes. Cell lysates were examined by Western blot analysis with anti-phospho-p44/42 mitogen-activated protein kinase (anti-phospho-ERK1/2) and pan-ERK1/2 (A), phospho-p38 mitogen-activated protein kinase (phospho-p38MAPK) and pan-p38MAPK (B), phospho-c-Jun N-terminal kinase (pan-JNK)1/2 and pan-c-pan-JNK1/2 (C) and (D), phospho-Akt and pan-Akt (E) and regulator of NF-κB (IκBα), and β-actin (F). Shown are band intensity (expressed in arbitrary units) of phospho-ERK1/2 (G), p38MAPK (H), JNK1 (I), JNK2 (J) and Akt (K) normalized to pan-ERK1/2, p38MAPK, JNK1, JNK2 and Akt, respectively. Relative expression of IκBα protein to β-actin is also shown (L). The results are representative of three different experiments performed using RA FLSs from three different patients.
Kaneko et al. Arthritis Research & Therapy 2011 13:R158 doi:10.1186/ar3475