Localized laryngeal amyloidosis: partial characterization of an amyloid fibril protein AL

Amyloid fibrils were extracted from a patient Wr with more than 10 yr history of localized laryngeal amyloidosis. Degraded amyloid fibrils reacted in immunodiffusion with an antiserum against an amyloid protein of immunoglobulin kappa light chain origin, showing a line of identity with a kappa I amyloid protein. The protein Wr had a blocked aminoterminal, previously only reported in lambda chains. Amino acid sequence analysis of a fragment of the protein showed it to be an immunoglobulin light chain protein of V kappa I or V kappa III subgroup. The protein had a few unusual amino acid residues as compared to other kappa light chains. The findings support the view that the fibrils in localized, tumour-like amyloidosis are composed by homogeneous immunoglobulin light chain proteins in the same way as is seen in primary and myeloma associated systemic amyloidosis. It is possible that unusual light chains are over-represented in amyloid fibrils.