Inhibition of oxLDL cell-association by Aβ requires CD36, but not CD36-associated signal transduction. A. To determine whether SRA or CD36 was essential for Aβ-inhibition of oxLDL metabolism, cell-association of 125I-oxLDL was measured in wild type, Sra-/- and Cd36-/- macrophages in the presence or absence of 20 μM Aβ. While Aβ blocked oxLDL association by approximately 50% in wild type and Sra-/- macrophages, this effect was lost in Cd36-/- macrophages indicating that CD36 is required for this inhibition. B. Inhibition of 125I-oxLDL degradation by Aβ does not utilize the Aβ-CD36 signaling pathway involving Lyn and Fyn kinases. Aβ impaired oxLDL degradation to a similar extent in wild type, and Lyn-/- or Fyn-/- macrophages in which CD36-signaling is impaired, indicating that this signal transduction pathway is not required, Data are the mean of triplicate samples ± standard deviation, *p ≤ 0.005.