LOCALIZED AMYLOIDOSIS OF THE LARYNX - EVIDENCE FOR LIGHT-CHAIN COMPOSITION

We report the biochemical characterization of amyloid fibrils from a patient with localized amyloidosis of the epiglottis and larynx. Biopsy specimens showed amorphous material consistent with amyloid deposits with a plasmacytic infiltrate. Both plasma cells and amyloid deposits stained positively by immunohistochemistry for kappa light chains. Amyloid fibrils were isolated. The major constituent resolved as a 13 kd band was sequenced and found to be consistent with a kappa1 light chain. A tryptic digest was carried out and 3 tryptic peptides were sequenced defining the first 45 residues of the protein and residues 110 through 119. Four amino acid substitutions were found, 3 of which have not been described previously. This study defines the immunoglobulin origin of amyloid deposits in localized amyloidosis. The benign nature of localized amyloidosis suggests that a localized clone of plasma cells producing an amyloidogenic light chain may represent the pathogenetic mechanism of this disease, which appears to be a form of plasma cell dyscrasia.