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The transthyretin cDNA sequence is normal in transthyretin‐derived senile systemic amyloidosis
Author(s) -
Christmanson L.,
Betsholtz C.,
Gustavsson Å.,
Johansson B.,
Sletten K.,
Westermark P.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80387-i
Subject(s) - transthyretin , amyloidosis , amyloid (mycology) , complementary dna , peptide sequence , mutation , sequence (biology) , pathogenesis , amyloid fibril , biology , gene , pathology , medicine , biochemistry , disease , amyloid β
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.