An updated AL-base reveals ranked enrichment of immunoglobulin light chain variable genes in AL amyloidosis.

Background: Each monoclonal antibody light chain associated with AL amyloidosis has a unique sequence. Defining how these sequences drive amyloid deposition could facilitate faster diagnosis and lead to new treatments.

Methods: Light chain sequences are collected in the AL-Base repository.

Predicting Structural Consequences of Antibody Light Chain N-Glycosylation in AL Amyloidosis.

Antibody light chains form amyloid fibrils that lead to progressive tissue damage in amyloid light chain (AL) amyloidosis. The properties of each patient's unique light chain appear to determine its propensity to form amyloid. One factor is N-glycosylation, which is more frequent in amyloid-associated light chains than in light chains from the normal immune repertoire.

High-Sensitivity and Conventional Cardiac Troponin-I Assays in AL Amyloidosis.

Background: Circulating cardiac troponin-I (cTnI) plays a crucial role in biomarker staging systems, offering important information for prognostification and risk stratification of patients with AL amyloidosis. High-sensitivity cTnI (HS-cTnI) assays have been introduced in practice; however, the data on the concordance between conventional and HS-cTnI and the utility of HS-cTnI in cardiac biomarker staging are lacking.

Methods: Seventy-eight consecutive patients with AL amyloidosis who were prospectively evaluated at the Boston University Amyloidosis Center from October 2022 through March 2023 were included.

Conformational Differences in the Light Chain Constant Domain of Immunoglobulin G and Free Light Chain May Influence Proteolysis in AL Amyloidosis.

Immunoglobulin light chain amyloidosis (AL) is a life-threatening disease caused by the deposition of light chain (LC) and its fragments containing variable (V) and portions of constant (C) domains. AL patients feature either monoclonal free LCs (FLCs) circulating as covalent and noncovalent homodimers, or monoclonal immunoglobulin (Ig) wherein the LC and heavy chain (HC) form disulfide-linked heterodimers, or both. The role of full-length Ig in AL amyloidosis is unclear as prior studies focused on FLC or V domain.

An updated AL-Base reveals ranked enrichment of immunoglobulin light chain variable genes in AL amyloidosis.

Background: Each monoclonal antibody light chain associated with AL amyloidosis has a unique sequence. Defining how these sequences lead to amyloid deposition could facilitate faster diagnosis and lead to new treatments.

Methods: Light chain sequences are collected in the Boston University AL-Base repository.