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. 2015 Nov 26;38(12):1111–1117. doi: 10.14348/molcells.2015.0213

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© The Korean Society for Molecular and Cellular Biology. All rights reserved.

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Fig. 5. — Molecular mechanism of caveolin-1-dependent TLR5 expression. Caveolin-1 was overexpressed in HeLa and NS-HDF cells using a lentivirus (LV) carrying RFP-caveolin-1 (RFP/Cav1). (A, B) The protein half-life of TLR5 in caveolin-1 overexpressing HeLa and NS-HDF after treatment with 100 μg/ml cycloheximide for the indicated time period was detected by Western blotting with anti-TLR5 specific antibody. (C) The proteins associated with the MAPK signaling pathway (Erk1, p-Erk, p38α, p-p38, SAPK/JNK, p-SAPK/JNK) were detected in caveolin-1 over-expressing HeLa cells by Western blotting using specific antibodies. The β-actin was used as the loading control. The relative density of protein expression was normalized to β-actin and represented by quantitative graphs. Data are presented as mean ± SD from five independent experiments; ^*p < 0.05; ns, not significant.