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Department of Medical and Molecular Genetics, Indiana University School of Medicine, and
Richard L. Roudebush Veteran Affairs Medical Center, Indianapolis, IN 46202
Ig amyloidosis is usually a systemic disease with multisystem
involvement. However, in a significant number of cases amyloid
deposition is limited to one specific organ. It has not been determined
if the Ig light chain (LC) amyloid precursor protein in localized
amyloidosis is synthesized by circulating plasma cells with targeting
of the amyloid fibril-forming process to one specific organ, or whether
the synthesis of Ig LC and fibril formation occurs entirely as a
localized process. In the present study local synthesis of an amyloid
fibril precursor LC was investigated. Amyloid fibrils were isolated
from a ureter that was obstructed by extensive infiltration of the wall
with amyloid. Amino acid sequence analysis of the isolated fibril
subunit protein proved it to be derived from a
II Ig LC.
Plasma cells within the lesion stained positively with labeled
anti-
Ab and by in situ hybridization using an oligonucleotide
probe specific for
-LC mRNA. RT-PCR of mRNA extracted from the tumor
and direct DNA sequencing gave the nucleotide sequence coding
specifically for the
II amyloid subunit protein, thus
confirming local synthesis of the LC protein.
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