ArticleBiophysical chemistry2011
Glycosaminoglycans promote fibril formation by amyloidogenic immunoglobulin light chains through a transient interaction.
Article in Biophysical chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
12 citing papers in PubMed, 27 citations in OpenAlex.
- Amylum forms typical self-assembled amyloid fibrils.Science advances · 2024Article
- Molecular Mechanism of Pathogenesis and Treatment Strategies for AL Amyloidosis.International journal of molecular sciences · 2022Review
- Heparin-binding Peptides as Novel Therapies to Stop SARS-CoV-2 Cellular Entry and Infection.Molecular pharmacology · 2020Review
- Understanding Mesangial Pathobiology in AL-Amyloidosis and Monoclonal Ig Light Chain Deposition Disease.Kidney international reports · 2020Review
- Immunoglobulin light chain amyloid aggregation.Chemical communications (Cambridge, England) · 2018Review
- Heparan sulfates facilitate harmless amyloidogenic fibril formation interacting with elastin-like peptides.Scientific reports · 2018Article
- Aggregation of Full-length Immunoglobulin Light Chains from Systemic Light Chain Amyloidosis (AL) Patients Is Remodeled by Epigallocatechin-3-gallate.The Journal of biological chemistry · 2017Article
- Differential effects on light chain amyloid formation depend on mutations and type of glycosaminoglycans.The Journal of biological chemistry · 2015Article
- Divergent effect of glycosaminoglycans on the in vitro aggregation of serum amyloid A.Biochimie · 2014Article
- Kinetic control in protein folding for light chain amyloidosis and the differential effects of somatic mutations.Journal of molecular biology · 2014Article
- Pathophysiology and treatment of systemic amyloidosis.Nature reviews. Nephrology · 2013Review
- Amyloid formation in light chain amyloidosis.Current topics in medicinal chemistry · 2012Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Amyloid formation occurs when a precursor protein misfolds and aggregates, forming a fibril nucleus that serves as a template for fibril growth. Glycosaminoglycans are highly charged polymers known to associate with tissue amyloid deposits that have been shown to accelerate amyloidogenesis in vitro. We studied two immunoglobulin light chain variable domains from light chain amyloidosis patients with 90% sequence identity, analyzing their fibril formation kinetics and binding properties with different glycosaminoglycan molecules. We find that the less amyloidogenic of the proteins shows a weak dependence on glycosaminoglycan size and charge, while the more amyloidogenic protein responds only minimally to changes in the glycosaminoglycan. These glycosaminoglycan effects on fibril formation do not depend on a stable interaction between the two species but still show characteristic traits of an interaction-dependent mechanism. We propose that transient, predominantly electrostatic interactions between glycosaminoglycans and the precursor proteins mediate the acceleration of fibril formation in vitro.
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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.