ArticlePloS one2009
Mutations in specific structural regions of immunoglobulin light chains are associated with free light chain levels in patients with AL amyloidosis.
Article in PloS one, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 87 citations in OpenAlex.
- Exploring the MicroRNA Landscape in Cardiac Amyloidosis: Molecular Insights and Clinical Applications.Genes · 2026Review
- Article
- Antibody Aggregation: A Problem Within the Biopharmaceutical Industry and Its Role in AL Amyloidosis Disease.The protein journal · 2025Review
- Occurrence of Monoclonal Band in Alpha Region on Serum Electrophoresis in Multiple Myeloma: A Diagnostic Conundrum.Indian journal of hematology & blood transfusion : an official journal of Indian Society of Hematology and Blood Transfusion · 2025Article
- Clone-specific residue changes at multiple positions are associated with amyloid formation by antibody light chains.Frontiers in immunology · 2025Article
- Tubular basement membrane amyloid deposition: is it an indicator of renal progression in light chain amyloidosis?Renal failure · 2023Article
- Role of the mechanisms for antibody repertoire diversification in monoclonal light chain deposition disorders: when a friend becomes foe.Frontiers in immunology · 2023Review
- Role of mutations and post-translational modifications in systemic AL amyloidosis studied by cryo-EM.Nature communications · 2021Article
- Dissecting the Molecular Features of Systemic Light Chain (AL) Amyloidosis: Contributions from Proteomics.Medicina (Kaunas, Lithuania) · 2021Review
- Genetic pathogenesis of immunoglobulin light chain amyloidosis: basic characteristics and clinical applications.Experimental hematology & oncology · 2021Review
- Seeded fibrils of the germline variant of human λ-III immunoglobulin light chain FOR005 have a similar core as patient fibrils with reduced stability.The Journal of biological chemistry · 2020Article
- Understanding Mesangial Pathobiology in AL-Amyloidosis and Monoclonal Ig Light Chain Deposition Disease.Kidney international reports · 2020Review
- Site-Specific Interactions with Copper Promote Amyloid Fibril Formation for λ6aJL2-R24G.ACS omega · 2020Article
- Immunoglobulin light chain amyloid aggregation.Chemical communications (Cambridge, England) · 2018Review
- Structure and energetic basis of overrepresented λ light chain in systemic light chain amyloidosis patients.Biochimica et biophysica acta. Molecular basis of disease · 2018Article
- Animal models of monoclonal immunoglobulin-related renal diseases.Nature reviews. Nephrology · 2018Review
- Mechanisms of recognition of amyloid-β (Aβ) monomer, oligomer, and fibril by homologous antibodies.The Journal of biological chemistry · 2017Article
- Kinetic stability and sequence/structure studies of urine-derived Bence-Jones proteins from multiple myeloma and light chain amyloidosis patients.Biophysical chemistry · 2017Article
- Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study.Scientific reports · 2017Article
- Epigallocatechin-3-gallate preferentially induces aggregation of amyloidogenic immunoglobulin light chains.Scientific reports · 2017Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
backgroundThe amyloidoses are protein misfolding diseases characterized by the deposition of amyloid that leads to cell death and tissue degeneration. In immunoglobulin light chain amyloidosis (AL), each patient has a unique monoclonal immunoglobulin light chain (LC) that forms amyloid deposits. Somatic mutations in AL LCs make these proteins less thermodynamically stable than their non-amyloidogenic counterparts, leading to misfolding and ultimately the formation of amyloid fibrils. We hypothesize that location rather than number of non-conservative mutations determines the amyloidogenicity of light chains. METHODOLOGY/PRINCIPAL
findingsWe performed sequence alignments on the variable domain of 50 kappa and 91 lambda AL light chains and calculated the number of non-conservative mutations over total number of patients for each secondary structure element in order to identify regions that accumulate non-conservative mutations. Among patients with AL, the levels of circulating immunoglobulin free light chain varies greatly, but even patients with very low levels can have very advanced amyloid deposition.
conclusionsOur results show that in specific secondary structure elements, there are significant differences in the number of non-conservative mutations between normal and AL sequences. AL sequences from patients with different levels of secreted light chain have distinct differences in the location of non-conservative mutations, suggesting that for patients with very low levels of light chains and advanced amyloid deposition, the location of non-conservative mutations rather than the amount of free light chain in circulation may determine the amyloidogenic propensity of light chains.
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