ArticleBiochimica et biophysica acta2014
The roles of C-terminal helices of human apolipoprotein A-I in formation of high-density lipoprotein particles.
Article in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 33 citations in OpenAlex.
- HDLR-SR-BI Expression and Cholesterol Uptake are Regulated via Indoleamine-2,3-dioxygenase 1 in Macrophages under Inflammation.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Isoform-specific modification of apolipoprotein E by 4-hydroxynonenal: protective role of apolipoprotein E3 against oxidative species.The FEBS journal · 2023Article
- The role of C-terminal ionic residues in self-association of apolipoprotein A-I.Biochimica et biophysica acta. Biomembranes · 2023Article
- Structure and intermolecular interactions in spheroidal high-density lipoprotein subpopulations.Journal of structural biology: X · 2021Article
- Fragments ofBBA advances · 2021Article
- Charged Residues in the C-Terminal Domain of Apolipoprotein A-I Modulate Oligomerization.Biochemistry · 2018Article
- Characterization of type IV antifreeze gene in Nile tilapia (Oreochromis niloticus) and influence of cold and hot weather on its expression and some immune-related genes.Fish physiology and biochemistry · 2018Article
- Characterization of covalent modifications of HDL apoproteins by endogenous oxidized phospholipids.Free radical biology & medicine · 2018Article
- Expression of the C-terminal domain of human apolipoprotein A-I using a chimeric apolipoprotein.Protein expression and purification · 2017Article
- Transfer of C-terminal residues of human apolipoprotein A-I to insect apolipophorin III creates a two-domain chimeric protein with enhanced lipid binding activity.Biochimica et biophysica acta. Biomembranes · 2017Article
- Dietary Strategies and Novel Pharmaceutical Approaches Targeting Serum ApoA-I Metabolism: A Systematic Overview.Journal of nutrition and metabolism · 2017Review
- High-Density Lipoprotein Biogenesis: Defining the Domains Involved in Human Apolipoprotein A-I Lipidation.Biochemistry · 2016Article
- Probing the C-terminal domain of lipid-free apoA-I demonstrates the vital role of the H10B sequence repeat in HDL formation.Journal of lipid research · 2016Article
- Lipid-free Apolipoprotein A-I Structure: Insights into HDL Formation and Atherosclerosis Development.Archives of medical research · 2015Review
- Structural Insights into High Density Lipoprotein: Old Models and New Facts.Frontiers in pharmacology · 2015Review
- Amyloid-Forming Properties of Human Apolipoproteins: Sequence Analyses and Structural Insights.Advances in experimental medicine and biology · 2015Review
- Development of a Novel Tetravalent Synthetic Peptide That Binds to Phosphatidic Acid.PloS one · 2015Article
- Direct detection of ABCA1-dependent HDL formation based on lipidation-induced hydrophobicity change in apoA-I.Journal of lipid research · 2014Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Apolipoprotein A-I (apoA-I) accepts cholesterol and phospholipids from ATP-binding cassette transporter A1 (ABCA1)-expressing cells to form high-density lipoprotein (HDL). Human apoA-I has two tertiary structural domains and the C-terminal domain (approximately amino acids 190-243) plays a key role in lipid binding. Although the high lipid affinity region of the C-terminal domain of apoA-I (residues 223-243) is essential for the HDL formation, the function of low lipid affinity region (residues 191-220) remains unclear. To evaluate the role of residues 191-220, we analyzed the structure, lipid binding properties, and HDL formation activity of Δ191-220 apoA-I, in comparison to wild-type and Δ223-243 apoA-I. Although deletion of residues 191-220 has a slight effect on the tertiary structure of apoA-I, the Δ191-220 variant showed intermediate behavior between wild-type and Δ223-243 regarding the formation of hydrophobic sites and lipid interaction through the C-terminal domain. Physicochemical analysis demonstrated that defective lipid binding of Δ191-220 apoA-I is due to the decreased ability to form α-helix structure which provides the energetic source for lipid binding. In addition, the ability to form HDL particles in vitro and induce cholesterol efflux from ABCA1-expressing cells of Δ191-220 apoA-I was also intermediate between wild-type and Δ223-243 apoA-I. These results suggest that despite possessing low lipid affinity, residues 191-220 play a role in enhancing the ability of apoA-I to bind to and solubilize lipids by forming α-helix upon lipid interaction. Our results demonstrate that the combination of low lipid affinity region and high lipid affinity region of apoA-I is required for efficient ABCA1-dependent HDL formation.
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