ArticleProtein science : a publication of the Protein Society2006
The effects of sodium sulfate, glycosaminoglycans, and Congo red on the structure, stability, and amyloid formation of an immunoglobulin light-chain protein.
Article in Protein science : a publication of the Protein Society, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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45 citing papers in PubMed, 84 citations in OpenAlex.
- Effect of dynamic exclusion and the use of FAIMS, DIA and MALDI-mass spectrometry imaging with ion mobility on amyloid protein identification.Clinical proteomics · 2024Article
- Producing amyloid fibrils in vitro: A tool for studying AL amyloidosis.Biochemistry and biophysics reports · 2023Article
- The influence of cations on α-lactalbumin amyloid aggregation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Article
- Therapeutic Potential and Main Methods of Obtaining Selenium Nanoparticles.International journal of molecular sciences · 2021Review
- Understanding Mesangial Pathobiology in AL-Amyloidosis and Monoclonal Ig Light Chain Deposition Disease.Kidney international reports · 2020Review
- Analysis of gene expression profiling of amyloidogenic immunoglobulin light-chains on cultured rat cardiomyocytes.Experimental and therapeutic medicine · 2020Article
- Immunoglobulin light chain amyloid aggregation.Chemical communications (Cambridge, England) · 2018Review
- Isolation and purification of recombinant immunoglobulin light chain variable domains from the periplasmic space of Escherichia coli.PloS one · 2018Article
- Neuroprotective effect of chondroitin sulfate on SH‑SY5Y cells overexpressing wild‑type or A53T mutant α‑synuclein.Molecular medicine reports · 2017Article
- Critical Influence of Cosolutes and Surfaces on the Assembly of Serpin-Derived Amyloid Fibrils.Biophysical journal · 2017Article
- Sulfated glycosaminoglycans in protein aggregation diseases.Glycoconjugate journal · 2017Review
- Solid-state NMR chemical shift assignments for AL-09 VBiomolecular NMR assignments · 2017Article
- Immunoglobulin Light Chains Form an Extensive and Highly Ordered Fibril Involving the N- and C-Termini.ACS omega · 2017Article
- 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
- Tau Pathology Promotes the Reorganization of the Extracellular Matrix and Inhibits the Formation of Perineuronal Nets by Regulating the Expression and the Distribution of Hyaluronic Acid Synthases.Journal of Alzheimer's disease : JAD · 2017Article
- The Kinetic Stability of a Full-Length Antibody Light Chain Dimer Determines whether Endoproteolysis Can Release Amyloidogenic Variable Domains.Journal of molecular biology · 2016Article
- Mutations can cause light chains to be too stable or too unstable to form amyloid fibrils.Protein science : a publication of the Protein Society · 2015Article
- Differential effects on light chain amyloid formation depend on mutations and type of glycosaminoglycans.The Journal of biological chemistry · 2015Article
- The effect of glycosaminoglycans (GAGs) on amyloid aggregation and toxicity.Molecules (Basel, Switzerland) · 2015Review
- Article
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5 authors at 1 institution in 1 country.
Funding
Abstract
Light-chain amyloidosis (AL) is characterized by immunoglobulin light-chain fragments aggregating into amyloid fibrils that deposit extracellularly in vital organs such as the kidney, the heart, and the liver, resulting in tissue degeneration and organ failure, leading to death. Cardiac involvement is found in 50% of AL patients and presents the most severe cases with a life expectancy of less than a year after diagnosis. In this study, we have characterized the variable domain of a cardiac AL patient light chain called AL-09. AL-09 folds as a beta-sheet and is capable of forming amyloid fibrils both in the presence of sodium sulfate and in self-seeded reactions under physiological conditions. Glycosaminoglycans such as dermatan sulfate and heparin promote amyloid formation of self-seeded AL-09 reactions, while the glycosaminoglycan chondroitin sulfate A stabilized oligomeric intermediates and did not elongate the preformed fibrils (nucleus) present in the reaction. Finally, the histological dye Congo red, known to bind to the cross beta-sheet structure of amyloid fibrils, inhibits AL-09 amyloid fibril formation in the presence of sodium sulfate and in self-seeded reactions. This paper provides insight into the impact of different reagents on light-chain stability, structure, amyloid fibril formation, and inhibition.
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