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 Lettjournal_title
FEBS lettersauthors
Christmanson L,Betsholtz C,Gustavsson A,Johansson B,Sletten K,Westermark Pdoi
10.1016/0014-5793(91)80387-isubject
Has Abstractpub_date
1991-04-09 00:00:00pages
177-80issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(91)80387-Ijournal_volume
281pub_type
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