Abstract
Aim: Apolipoprotein J (apoJ) is an extracellular chaperone involved in the quality control system against protein unfolding and aggregation. A minor part of apoJ is transported in blood bound to low-density lipoproteins (LDL), but its role is poorly understood. Since LDL aggregation is considered the initial event triggering atherosclerosis, our aim was to determine the role of apoJ bound to LDL.
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