There’s a saying that goes: “everything old is new again,” and I am reminded of this by the article by Luangrath et al1 in this issue of Arteriosclerosis, Thrombosis and Vascular Biology . Not that this article shows old data, but that what was old, now cast in a different light, leads to new ideas and hypotheses. Just about 10 years ago, Calvo et al2 showed that human CD36 bound native LDL, HDL, and VLDL. Later, Connelly et al3 found that CD36 could mediate selective cholesterol ester uptake from LDL. These were both intriguing findings, but without in vivo data there was a question of relevance. Since then, most studies have focused on CD36 recognition of aberrant lipoproteins, and a role for CD36 in native lipoprotein biology has been overshadowed. With this article, and several others recently published, the spotlight has begun to shift to potential functional roles of CD36 in native lipoprotein biology. See accompanying article on page 1290 CD36 was first identified as a platelet glycoprotein (GP) and originally primarily thought of as a receptor for thrombospondin-1, and involved in adhesion. As the oxidation theory of lipoprotein modification gained traction as an underlying mechanism for atherogenesis, interest in receptors for oxidized LDL (oxLDL) increased. The observation that CD36 was an oxLDL receptor was the catalyst for many to probe the role of CD36 in atherosclerosis. Further work to define the …