ArticleJournal of cellular and molecular medicine2011
Insights into the fate of the N-terminal amyloidogenic polypeptide of ApoA-I in cultured target cells.
Article in Journal of cellular and molecular medicine, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 27 citations in OpenAlex.
- Cryo-EM reveals structural variability of apolipoprotein A-I amyloid fibrils across organs, mutations, and clinical presentations.Nature communications · 2026Article
- Insights into Bioactive Molecules inBiomolecules · 2026Article
- Enzymatically Crafted Bacterial Cellulose Nanoparticles Functionalized With Antimicrobial Peptides: Toward Sustainable Antimicrobial Formulations.Biotechnology journal · 2025Article
- The Apparent Organ-Specificity of Amyloidogenic ApoA-I Variants Is Linked to Tissue-Specific Extracellular Matrix Components.International journal of molecular sciences · 2022Article
- Correction of oxidative stress enhances enzyme replacement therapy in Pompe disease.EMBO molecular medicine · 2021Article
- Green Compressed Fluid Technologies To Extract Antioxidants and Lipids fromACS sustainable chemistry & engineering · 2020Article
- The effects of short-chain fatty acids on the transcription and secretion of apolipoprotein A-I in human hepatocytes in vitro.Journal of cellular biochemistry · 2019Article
- Characterization of a Surface-Active Protein Extracted from a Marine Strain ofInternational journal of molecular sciences · 2019Article
- Alternative use of Bacillus subtilis spores: protection against environmental oxidative stress in human normal keratinocytes.Scientific reports · 2018Article
- Cellular mechanism of fibril formation from serum amyloid A1 protein.EMBO reports · 2017Article
- Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein A-I on Lipid Membranes.The Journal of biological chemistry · 2015Article
- Amyloid-Forming Properties of Human Apolipoproteins: Sequence Analyses and Structural Insights.Advances in experimental medicine and biology · 2015Review
- 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
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Apolipoprotein A-I (ApoA-I) is an extracellular lipid acceptor, whose role in cholesterol efflux and high-density lipoprotein formation is mediated by ATP-binding cassette transporter A1 (ABCA1). Nevertheless, some ApoA-I variants are associated to systemic forms of amyloidosis, characterized by extracellular fibril deposition in peripheral organs. Heart amyloid fibrils were found to be mainly constituted by the 93-residue N-terminal fragment of ApoA-I, named [1-93]ApoA-I. In this paper, rat cardiomyoblasts were used as target cells to analyse binding, internalization and intracellular fate of the fibrillogenic polypeptide in comparison to full-length ApoA-I. We provide evidence that the polypeptide: (i) binds to specific sites on cell membrane (K(d) = 5.90 ± 0.70 × 10(-7) M), where it partially co-localizes with ABCA1, as also described for ApoA-I; (ii) is internalized mostly by chlatrin-mediated endocytosis and lipid rafts, whereas ApoA-I is internalized preferentially by chlatrin-coated pits and macropinocytosis and (iii) is rapidly degraded by proteasome and lysosomes, whereas ApoA-I partially co-localizes with recycling endosomes. Vice versa, amyloid fibrils, obtained by in vitro aggregation of [1-93]ApoA-I, were found to be unable to enter the cells. We propose that internalization and intracellular degradation of [1-93]ApoA-I may divert the polypeptide from amyloid fibril formation and contribute to the slow progression and late onset that characterize this pathology.
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