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The N-terminus of apolipoprotein B mediates the interaction of atherogenic lipoproteins with endothelial cells

2026/04/23 by Ainara G. Cabodevilla, Camila Calistru, Waqas Younis +17 · 1 voice · 1 citation
Immunology and Microbiology · Medicine · #Apolipoprotein B #Apolipoprotein E #Atherosclerosis and Cardiovascular Diseases #Cholesterol #Diabetes, Cardiovascular Risks, and Lipoproteins #Endothelial stem cell #Endothelium #Lipoprotein #Lipoproteins and Cardiovascular Health

paper · doi:10.1172/jci190513

published in Journal of Clinical Investigation 136(12) (American Society for Clinical Investigation)

openalex publication_date 2026/04/23 · openalex created_date 2026/04/24 · openalex updated_date 2026/08/06

Abstract

Apolipoprotein B-containing (APOB-containing) lipoproteins contribute to atherosclerosis by entering the arterial wall through the endothelial cell (EC) surface receptors scavenger receptor-BI (SR-BI) and activin receptor-like kinase 1 (ALK1). We used N-terminal fragments of APOB, molecular modeling, and site-directed mutagenesis to identify and block the binding of chylomicrons and LDL to these receptors in cells and mice. We discovered that different APOB regions interact with SR-BI and ALK1 expressed on ECs. APOB48 lipoproteins were only internalized by SR-BI. A fragment of APOB comprising 18% of the N-terminal sequence, APOB18, reduced the uptake and transport of both chylomicrons and LDL by ECs, whereas a shorter fragment, APOB12, only blocked ALK1-mediated uptake of APOB100-containing lipoproteins. Importantly, overexpressing APOB18 decreased atherosclerosis in hypercholesterolemic mice. These findings identify the N-terminal region of APOB as the cause of atherosclerosis and illustrate an approach to treating or preventing vascular disease.

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