RENAL APOLIPOPROTEIN A-I AMYLOIDOSIS (AAPO-A-I) ASSOCIATED WITH A NOVEL MUTANT LEU64PRO

摘要

The apolipoprotein (apo) A-l-associated amyloidoses are an autosomal dominant familial disorder characterized by the pathologic deposition of N-terminai fragments of mutated apo A-I molecules as fibrils within vital organs throughout the body. In this hereditary disorder, 11 different sequence alterations have been detected in the amyloidogenic precursor protein that resulted from point mutations, deletions, and a deletion/insertion in the apo A-l gene. We now report that the fibrils extracted from the kidney of a patient with renal amyloidosis contained yet another apo A-I mutation, the substitution of proline for leucine at position 64 (Leu64Pro). Further, we demonstrated that this alteration resulted from a one-base transition in codon 64 of the subject's apo A-I gene.