Figure 2. ApoA-I binding to WT and Cav1^−/− MEFs at 4°C.

A.–B. ¹²⁵Iodine-labeled apoA-I (0–50 µg/mL) was bound to WT (solid diamonds) and Cav1^−/− MEFs (open squares) at 4°C on ice. Prior to exposure to apoA-I, cells in B, but not A, were treatment with the LXR agonist T0901317. Specific binding was determined by competition with 10-fold excess of unlabeled apoA-I. Specifically bound apoA-I was normalized to cell protein. The data (symbols) are a representative of independent experiments each performed in triplicate cell cultures. Solid lines represent best fits as described in Methods. C. The number of maximum binding sites, B_max and the binding affinity parameter K_D (− LXR agonist shown in filled bars, + LXR agonist hollow bars) obtained from the fit are shown as average ± range of two independent experiments each performed in triplicates. No difference (P>0.05) was found ± LXR agonist treatment.