The transthyretin cDNA sequence is normal in transthyretin-derived senile systemic amyloidosis.

Abstract:

:A variety of mutations leading to amino acid substitutions have been described in the transthyretin gene in association with different familial amyloidoses and have been implicated to be involved in the pathogenesis of amyloid deposits. However, there has been disagreement whether or not a transthyretin mutation is present in the most common form of transthyretin-derived amyloid, namely senile systemic amyloidosis. Therefore, the cDNA sequence of liver transthyretin was determined in a 91-year-old patient with typical senile systemic amyloidosis. This sequence was completely normal and lacked any variation. We conclude that in senile systemic amyloidosis factors other than the presence of a sequentially variant transthyretin must determine the amyloid fibril formation.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Christmanson L,Betsholtz C,Gustavsson A,Johansson B,Sletten K,Westermark P

doi

10.1016/0014-5793(91)80387-i

subject

Has Abstract

pub_date

1991-04-09 00:00:00

pages

177-80

issue

1-2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(91)80387-I

journal_volume

281

pub_type

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