ArticleJournal of lipid research2009
Surface study of apoB1694-1880, a sequence that can anchor apoB to lipoproteins and make it nonexchangeable.
Article in Journal of lipid research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Dual binding motifs underpin the hierarchical association of perilipins1-3 with lipid droplets.Molecular biology of the cell · 2019Article
- Identification of a novel lipid binding motif in apolipoprotein B by the analysis of hydrophobic cluster domains.Biochimica et biophysica acta. Biomembranes · 2017Article
- Targeting Fat: Mechanisms of Protein Localization to Lipid Droplets.Trends in cell biology · 2016Review
- Protein Crowding Is a Determinant of Lipid Droplet Protein Composition.Developmental cell · 2015Article
- Apolipoprotein B100 quality control and the regulation of hepatic very low density lipoprotein secretion.Journal of biomedical research · 2014Article
- Surface tensiometry of apolipoprotein B domains at lipid interfaces suggests a new model for the initial steps in triglyceride-rich lipoprotein assembly.The Journal of biological chemistry · 2014Article
- Surface behavior of apolipoprotein A-I and its deletion mutants at model lipoprotein interfaces.Journal of lipid research · 2014Article
- Ubiquitination regulates the assembly of VLDL in HepG2 cells and is the committing step of the apoB-100 ERAD pathway.Journal of lipid research · 2011Article
- Interfacial properties of apolipoprotein B292-593 (B6.4-13) and B611-782 (B13-17). Insights into the structure of the lipovitellin homology region in apolipoprotein B.Biochemistry · 2010Article
- Recent progress in understanding protein and lipid factors affecting hepatic VLDL assembly and secretion.Nutrition & metabolism · 2010Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Apolipoprotein B (apoB) is a nonexchangeable apolipoprotein. During lipoprotein assembly, it recruits phospholipids and triacylglycerols (TAG) into TAG-rich lipoprotein particles. It remains bound to secreted lipoproteins during lipid metabolism in plasma. The beta1 region (residues 827-1880) of apoB has a high amphipathic beta strand (AbetaS) content and is proposed to be one region anchoring apoB to lipoproteins. The AbetaS-rich region between apoB37 and apoB41 (residues 1694-1880) was cloned, expressed, and purified. The interfacial properties were studied at the triolein/water (TO/W) and air/water (A/W) interfaces. ApoB[37-41] is surface-active and adsorbs to the TO/W interface. After adsorption the unbound apoB[37-41] was removed from the aqueous phase. Adsorbed apoB[37-41] did not desorb and could not be forced off by increasing the surface pressure up to 23 mN/m. ApoB[37-41] adsorbed on the TO/W interface was completely elastic when compressed and expanded by +/-13% of its area. On an A/W interface, the apoB[37-41] monolayer became solid when compressed to 4 mN/m pressure indicating extended beta-sheet formation. It could be reversibly compressed and expanded between low pressure and its collapse pressure (35 mN/m). Our studies confirm that the AbetaS structure of apoB[37-41] is a lipid-binding motif that can irreversibly anchor apoB to lipoproteins.
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