The transthyretin cDNA sequence is normal in transthyretin‐derived senile systemic amyloidosis

FEBS Letters

Betsholtz, C.¹  Gustavsson, Å.²  Johansson, B.³  Sletten, K.⁴  Westermark, P.²  Christmanson, L.¹ 

[1] Department of Pathology, University of Uppsala, Sweden;Department of Rehabilitation Medicine, University of Uppsala, Sweden;Department of Pathology, University of Linköping, Sweden;Department of Biochemistry, University of Oslo, Oslo, Norway

关键词: Transthyretin;    Prealbumin;    cDNA;    Polymerase chain reaction;    AA;    fibril protein in secondary systemic amyloidosis;    AL;    fibril protein in primary (plasma cell dyscrasia-associated) amyloid;    ATTR;    amyloid fibril protein derived from TTR;    FAP;    familial amyloidotic polyneuropathy;    SSA;    senile systemic amyloidosis;    TTR;    transthyretin;   

DOI  :  10.1016/0014-5793(91)80387-I

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown