Heterogeneity in Primary Structure, Post-Translational Modifications, and Germline Gene Usage of Nine Full-Length Amyloidogenic κ1 Immunoglobulin Light Chains

Abstract excerpt

Immunoglobulin light chain amyloidosis is a protein misfolding disease in which a monoclonal immunoglobulin (Ig) light chain (LC) with a critically folded beta-conformation self-aggregates to form highly ordered, nonbranching amyloid fibrils. The insoluble nature of amyloid fibrils ultimately results in the extracellular deposition of the LC in tissues and organs throughout the body. Structural features that...

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