AMΦ and lung tissues were lysated in radio-immunoprecipitation lysis buffer (RIPA), protease inhibitors (Roche, Mannheim, Germany) and phenylmethylsulfonyl fluoride (PMSF). Protein concentrations were subsequently determined by standard BCA assay. After addition of 6 × sodium dodecyl sulfate (SDS) loading buffer, equivalent amounts of protein were heated (100 °C; 5 min) and separated by gel electrophoresis using a 10% SDS-polyacrylamide electrophoresis gel. Resolved proteins were then transferred to a nitrocellulose membrane and blocked with Tris-buffered saline containing Tween-20 (TBST) and 5% nonfat milk (1 h; 24 °C). Nitrocellulose membranes were incubated overnight at 4 °C with primary antibody against TLR3 (ab62566; Abcam, Hong Kong, China), NF-κB p65 (ab7970, Abcam, Hong Kong, China), Abcam, MIP-2 (ab25130, Hong Kong, China), PCNA (ab18197, Abcam, Hong Kong, China) and β-actin (ab8226, Abcam, Hong Kong, China). The membranes were washed in TBST three times, incubated with secondary antibody (926-32221 IRDye 680 mouse-anti-rabbit secondary antibody; Licor Biosciences, Lincoln, NE, USA) for 1 h at 37 °C and then washed in TBST three additional times. The membranes were determined by using an Odyssey image analysis system (Licor Biosciences). Western blots were quantitated using Quantity One software (Bio-Rad, Foster City, CA, USA) and normalized to β-actin and PCNA signal.