Amino-terminal identity of co-existent amyloid and non-amyloid immunoglobulin κ light chain deposits. A human disease to study alterations of protein conformation

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Abstract
Tissue deposition of monoclonal immunoglobulin light chains is a serious complication in some patients with B cell proliferative disorders. The deposits are typically fibrillar and Congophilic in amyloid (AL) and non‐fibrillar and Congophobic in light chain deposition disease (LCDD), and rarely coexist in the same patient. From post‐mortem tissue of an individual with fibrillar and non‐fibrillar κ light chain deposits in different sites, we separately extracted and analysed biochemically and immunochemically the non‐amyloid deposits from isolated glomeruli, the amyloid from isolated renal arteries and the amyloid from myocardium in which the only deposits were amyloid restricted to mural arteries. Western blotting analysis of both the extracted amyloid and the non‐amyloid deposits demonstrated 25‐kD bands immunoreactive with anti‐κ antibody, and the identity of the N‐terminal amino acid sequences that belong to the variable region κIV light chain subgroup. This is the first human disease in which antigenically similar but morphologically different deposits have been separately biochemically analysed. We propose that combined LCDD and AL is an ideal human disease to study the relationships and the factors that influence the conversion of non‐amyloidogenic to amyloidogenic conformations.

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