Immunoglobulin lambda light chains are the precursors of ureteral localized amyloidosis: a micromethod for extraction of amyloid

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Abstract
We present the biochemical characterization of two amyloid proteins, including their partial amino terminal sequence, isolated from localized forms of ureteral amyfoidosis. The major component of amyloid NAv extracted from milligram quantities of biopsy tissue, had a molecular mass of 16 kDa and the 20 first amino acids showed homology to immunoglobulin (Ig) light chain of the subgroup λ II. In addition, amyloid P component co-purified with amyloid NA V as determined by Western blot analysis. Amyloid MAI was extracted from formalin fixed, paraffin embedded tissue. It had a molecular mass of 14 kDa and its amino terminal sequence (17 steps) revealed homology to Ig light chain of the subgroup λ III. These results provide additional evidence for the association between amyloidogenic Ig light chains and localized, tumor-like forms of amyloidosis. Moreover, the two simple methods presented here may facilitate the characterization of amyloid proteins from small samples of frozen tissue and rare specimens stored in paraffin blocks.