Increased CD36 protein as a response to defective insulin signaling in macrophages
J. Clin. Invest. Chien-Ping Liang, et al. 113:764 doi:10.1172/JCI19528 [Go to this article.]

Figure 3
CD36 is internalized similarly in WT and ob/ob macrophages and is increased in lysosome- and proteasome-inhibited WT but not in ob/ob macrophages. (A) CD36 in ob/ob macrophages is endocytosed at a rate similar to that of WT cells. Cell surface proteins were biotinylated in pooled macrophages of five mice of each strain. One experiment representative of two independent experiments is shown. Biotinylated CD36 was allowed to internalize for different times, as indicated. Surface biotin was then removed with glutathione (+). Cells without glutathione (–) were used for the measurement of total biotinylated CD36 left in the cells at the time point. The total biotinylated CD36 at time 0 was used as a reference (100%) for the quantification of internalized CD36 (all corrected for input with β-actin). Percent internalization was calculated as described (27). (B) CD36 protein is increased by lysosomal and proteasomal inhibitors in WT but not in ob/ob macrophages. Pooled macrophages isolated from five mice of each strain were treated with calpeptin (30 μg/ml), chloroquine (50 μM), or lactacystin (1 μM) for 1 day. Total lysates were prepared, and Western analysis was performed. One experiment representative of three independent experiments is shown.