ArticleBiochemistry2006
Heparin accelerates gelsolin amyloidogenesis.
Article in Biochemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 121 citations in OpenAlex.
- Membrane orientation regulates GAPR-1 oligomerization that is suitable for interaction with beclin 1.Cellular and molecular life sciences : CMLS · 2026Article
- Pan-Amyloid Reactive Peptides p5+14 and p5R Exhibit Specific Charge-Dependent Binding to Glycosaminoglycans.Pharmaceuticals (Basel, Switzerland) · 2025Article
- Extension of the SUGRES-1P Coarse-Grained Model of Polysaccharides to Heparin.Journal of chemical theory and computation · 2023Article
- Development of an in vitro aggregation assay for long synthetic polypeptide, amyloidogenic gelsolin fragment AGelD187N 173-242.PloS one · 2023Article
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- Heparan sulfate S-domains and extracellular sulfatases (Sulfs): their possible roles in protein aggregation diseases.Glycoconjugate journal · 2018Review
- Probing amylin fibrillation at an early stage via a tetracysteine-recognising fluorophore.Talanta · 2017Article
- Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design.Interface focus · 2017Review
- Molecular Origins of the Compatibility between Glycosaminoglycans and Aβ40 Amyloid Fibrils.Journal of molecular biology · 2017Article
- Sulfated glycosaminoglycans in protein aggregation diseases.Glycoconjugate journal · 2017Review
- Inferring Mechanistic Parameters from Amyloid Formation Kinetics by Approximate Bayesian Computation.Biophysical journal · 2017Article
- The effect of glycosaminoglycans (GAGs) on amyloid aggregation and toxicity.Molecules (Basel, Switzerland) · 2015Review
- Mechanistic Contributions of Biological Cofactors in Islet Amyloid Polypeptide Amyloidogenesis.Journal of diabetes research · 2015Review
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- Looked at life from both sides now.Life (Basel, Switzerland) · 2014Review
- Divergent effect of glycosaminoglycans on the in vitro aggregation of serum amyloid A.Biochimie · 2014Article
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- Polyanionic candidate microbicides accelerate the formation of semen-derived amyloid fibrils to enhance HIV-1 infection.PloS one · 2013Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The chemical environment of the extracellular matrix may influence the tissue-selective deposition observed there in gelsolin amyloid disease. Previously, we have identified the proteases that generate the amyloidogenic fragments from the full-length gelsolin variants and demonstrated that heparin is capable of accelerating gelsolin amyloidogenesis. Herein, we identify the structural features of heparin that promote the 8 kDa disease-associated gelsolin fragments (residues 173-243) generated at the cell surface to form amyloid. In conjunction with electron microscopy analyses, our kinetic studies demonstrate that heparin efficiently accelerates the formation of gelsolin amyloid by enabling intermolecular beta-sheet formation. The use of heparin analogues reveals that sulfation is important in accelerating amyloidogenesis and that the extent of acceleration is proportional to the molecular weight of heparin. In addition, heparin accelerated aggregation at both early and late stages of amyloidogenesis. Dynamic light scattering coupled to size exclusion chromatography showed that heparin promotes the formation of soluble aggregates. Collectively, these data reveal that heparin templates fibril formation and affords solubility to the aggregating peptides through its sulfated structure. By extension, the biochemical results herein suggest that tissue-selective deposition characteristic of the gelsolin amyloidoses is likely influenced by the extracellular localization of distinct glycosaminoglycans.
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Registered trials
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.