ArticleThe Journal of biological chemistry2012
Serum albumin prevents protein aggregation and amyloid formation and retains chaperone-like activity in the presence of physiological ligands.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers, 1 of them a synthesis that pooled it.
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Who cites it
71 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Pooled it
- Stabilization of Bone Morphogenetic Protein-2 at Physiological pH: Contrasting Roles of CHAPS and Arginine in Aggregation Inhibition.Proteins · 2026Article
- Fatty Acid Deaggregation and Extraction from Vesicles by Serum Albumin Proceeds Via a Dock-and-Load Mechanism.The journal of physical chemistry letters · 2026Article
- The Impact of Collection Protocol on the Yield and Purity of Mesenchymal Stem Cell-Derived Extracellular Vesicles Isolated From Serum-Free Media.Biotechnology journal · 2026Article
- Modulation of islet amyloid polypeptide induced β-cell toxicity and amyloid formation by serum albumin proteins.Biophysical chemistry · 2026Article
- Association between the Naples Prognostic Score and cognitive function in older adults: validation in Alzheimer's disease and vascular dementia.Frontiers in nutrition · 2026Article
- Oxidative environments promote the formation of detergent-resistant IgG aggregates mediated by Cu(II) assessed by optical density: implications in vivo.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Article
- Article
- Surface-modified protein crowders influence mutant huntingtin exon 1 aggregation via crowding effects, crowder association, and crowder solution stability.Protein science : a publication of the Protein Society · 2025Article
- Article
- Underestimated role of macromolecular crowding in bioengineeredMaterials today. Bio · 2025Article
- Single-molecule observations of human small heat shock proteins in complex with aggregation-prone client proteins.The Biochemical journal · 2025Article
- Chlorogenic Acid Enhances the Chaperone Potential of BSA at Physiological Concentrations on Model Protein Cytochrome c.Cell biochemistry and biophysics · 2025Article
- A quantitative Lewy-fold-specific alpha-synuclein seed amplification assay as a progression marker for Parkinson's disease.Acta neuropathologica · 2025Article
- An emulsion electrospun nanofibrous scaffold loaded with glial cell line-derived neurotrophic factor for nerve regeneration.Frontiers in cell and developmental biology · 2025Article
- Novel vanadyl complexes synthesis, characterization and interactions with bovine serum albumin-effects on STZ- diabetes rats.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2024Article
- Unlocking Potential: Low Bovine Serum Albumin Enhances the Chondrogenicity of Human Adipose-Derived Stromal Cells in Pellet Cultures.Biomolecules · 2024Article
- Inhibition of toxic metal-alpha synuclein interactions by human serum albumin.Chemical science · 2024Article
- Complexing Protein-Free Botulinum Neurotoxin A Formulations: Implications of Excipients for Immunogenicity.Toxins · 2024Review
- Protective role of serum albumin in dementia: a prospective study from United Kingdom biobank.Frontiers in neurology · 2024Article
11 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Although serum albumin has an established function as a transport protein, evidence is emerging that serum albumin may also have a role as a molecular chaperone. Using established techniques to characterize chaperone interactions, this study demonstrates that bovine serum albumin: 1) preferentially binds stressed over unstressed client proteins; 2) forms stable, soluble, high molecular weight complexes with stressed client proteins; 3) reduces the aggregation of client proteins when it is present at physiological levels; and 4) inhibits amyloid formation by both WT and L55P transthyretin. Although the antiaggregatory effect of serum albumin is maintained in the presence of physiological levels of Ca(2+) and Cu(2+), the presence of free fatty acids significantly alters this activity: stabilizing serum albumin at normal levels but diminishing chaperone-like activity at high concentrations. Moreover, here it is shown that depletion of albumin from human plasma leads to a significant increase in aggregation under physiologically relevant heat and shear stresses. This study demonstrates that serum albumin possesses chaperone-like properties and that this activity is maintained under a number of physiologically relevant conditions.
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Registered trials
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