ArticleJournal of lipid research2010
Disruption of the C-terminal helix by single amino acid deletion is directly responsible for impaired cholesterol efflux ability of apolipoprotein A-I Nichinan.
Article in Journal of lipid research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- Review
- 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
- Mimetic peptides of human apoA-I helix 10 get together to lower lipids and ameliorate atherosclerosis: is the action in the gut?Journal of lipid research · 2014Article
- Amyloidogenic mutations in human apolipoprotein A-I are not necessarily destabilizing - a common mechanism of apolipoprotein A-I misfolding in familial amyloidosis and atherosclerosis.The FEBS journal · 2014Article
- The roles of C-terminal helices of human apolipoprotein A-I in formation of high-density lipoprotein particles.Biochimica et biophysica acta · 2014Article
- New insights into the determination of HDL structure by apolipoproteins: Thematic review series: high density lipoprotein structure, function, and metabolism.Journal of lipid research · 2013Review
- Helical domains that mediate lipid solubilization and ABCA1-specific cholesterol efflux in apolipoproteins C-I and A-II.Journal of lipid research · 2013Article
- Dietary fats and health: dietary recommendations in the context of scientific evidence.Advances in nutrition (Bethesda, Md.) · 2013Review
- Dual role of an N-terminal amyloidogenic mutation in apolipoprotein A-I: destabilization of helix bundle and enhancement of fibril formation.The Journal of biological chemistry · 2013Article
- Effects of the Iowa and Milano mutations on apolipoprotein A-I structure and dynamics determined by hydrogen exchange and mass spectrometry.Biochemistry · 2012Article
- Naturally occurring variant of mouse apolipoprotein A-I alters the lipid and HDL association properties of the protein.Journal of lipid research · 2012Article
- Impact of self-association on function of apolipoprotein A-I.The Journal of biological chemistry · 2011Article
- Structure of apolipoprotein A-I N terminus on nascent high density lipoproteins.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
Abstract
Apolipoprotein A-I (apoA-I) Nichinan, a naturally occurring variant with DeltaE235 in the C terminus, is associated with low plasma HDL levels. Here, we investigated the tertiary structure, lipid-binding properties, and ability to induce cellular cholesterol efflux of apoA-I Nichinan and its C-terminal peptide. Thermal and chemical denaturation experiments demonstrated that the DeltaE235 mutation decreased the protein stability compared with wild type (WT). ApoA-I Nichinan exhibited capabilities to bind to or solubilize lipid vesicles that are intermediate to that of WT and a L230P/L233P/Y236P variant in which the C-terminal alpha-helix folding is completely disrupted and forms relatively larger and unstable discoidal complexes, indicating that perturbation of the C-terminal alpha-helical structure by the DeltaE235 mutation leads to reduced lipid binding. Supporting this, apoA-I 209-241/DeltaE235 peptide showed significantly decreased ability to form alpha-helix both in the lipid-free and lipid-bound states, and reduced efficiency to solubilize vesicles. In addition, both apoA-I Nichinan and its C-terminal peptide exhibited reduced activity in ABCA1-mediated cellular cholesterol efflux. Thus, the disruption of the ability of the C-terminal region to form alpha-helix caused by the E235 deletion appears to be the important determinant of impaired lipid binding and cholesterol efflux ability and, consequently, the low plasma HDL levels of apoA-I Nichinan probands.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.