ArticleJournal of lipid research2012
The fibrillogenic L178H variant of apolipoprotein A-I forms helical fibrils.
Article in Journal of lipid research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 47 citations in OpenAlex.
- Cryo-EM reveals structural variability of apolipoprotein A-I amyloid fibrils across organs, mutations, and clinical presentations.Nature communications · 2026Article
- The APOA1 p.Leu202Arg variant potentially causes autosomal recessive cardiac amyloidosis.Human genome variation · 2024Article
- Article
- The Apparent Organ-Specificity of Amyloidogenic ApoA-I Variants Is Linked to Tissue-Specific Extracellular Matrix Components.International journal of molecular sciences · 2022Article
- Autophagy Alteration in ApoA-I Related Systemic Amyloidosis.International journal of molecular sciences · 2022Article
- Lipids and Lipoproteins in Health and Disease: Focus on Targeting Atherosclerosis.Biomedicines · 2021Review
- Probing the Structure-Function relationship and amyloidogenic propensities in natural variants of apolipoprotein A-I.Biochemistry and biophysics reports · 2020Article
- A short peptide of the C-terminal class Y helices of apolipoprotein A-I has preserved functions in cholesterol efflux and in vivo metabolic control.Scientific reports · 2020Article
- ApoA-1 improves glucose tolerance by increasing glucose uptake into heart and skeletal muscle independently of AMPKαMolecular metabolism · 2020Article
- Thrombin-derived C-terminal fragments aggregate and scavenge bacteria and their proinflammatory products.The Journal of biological chemistry · 2020Article
- High-efficient bacterial production of human ApoA-I amyloidogenic variants.Protein science : a publication of the Protein Society · 2018Article
- ApoA-I Milano stimulates lipolysis in adipose cells independently of cAMP/PKA activation.Journal of lipid research · 2015Article
- Elucidation of the Aggregation Pathways of Helix-Turn-Helix Peptides: Stabilization at the Turn Region Is Critical for Fibril Formation.Biochemistry · 2015Article
- Myeloperoxidase-mediated Methionine Oxidation Promotes an Amyloidogenic Outcome for Apolipoprotein A-I.The Journal of biological chemistry · 2015Article
- Article
- Structural Insights into High Density Lipoprotein: Old Models and New Facts.Frontiers in pharmacology · 2015Review
- Conformational and aggregation properties of the 1-93 fragment of apolipoprotein A-I.Protein science : a publication of the Protein Society · 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
- Amyloid triangles, squares, and loops of apolipoprotein C-III.Biochemistry · 2014Article
- Single injections of apoA-I acutely improve in vivo glucose tolerance in insulin-resistant mice.Diabetologia · 2014Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A number of amyloidogenic variants of apoA-I have been discovered but most have not been analyzed. Previously, we showed that the G26R mutation of apoA-I leads to increased β-strand structure, increased N-terminal protease susceptibility, and increased fibril formation after several days of incubation. In vivo, this and other variants mutated in the N-terminal domain (residues 26 to ∼90) lead to renal and hepatic accumulation. In contrast, several mutations identified within residues 170 to 178 lead to cardiac, laryngeal, and cutaneous protein deposition. Here, we describe the structural changes in the fibrillogenic variant L178H. Like G26R, the initial structure of the protein exhibits altered tertiary conformation relative to wild-type protein along with decreased stability and an altered lipid binding profile. However, in contrast to G26R, L178H undergoes an increase in helical structure upon incubation at 37°C with a half time (t(1/2)) of about 12 days. Upon prolonged incubation, the L178H mutant forms fibrils of a diameter of 10 nm that ranges in length from 30 to 120 nm. These results show that apoA-I, known for its dynamic properties, has the ability to form multiple fibrillar conformations, which may play a role in the tissue-specific deposition of the individual variants.
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