Identification of a novel transthyretin variant (Val30→Leu) associated with familial amyloidotic polyneuropathy

FEBS Letters

Shiomi, Kazutaka²  Matsukura, Shigeru²  Nakazato, Masamitsu²  Ikeda, Shu-ichi⁴  Atsumi, Tetsushi³  Kangawa, Kenji¹  Yoshida, Kunihiro⁴  Matsuo, Hisayuki³  Shimizu, Hideaki³ 

[1] Department of Biochemistry, Miyazaki Medical College, Kiyotake, Miyazaki 889-16, Japan;Department of Medicine, Miyazaki Medical College, Kiyotake, Miyazaki 889-16, Japan;Seirei Hamamatsu General Hospital, Hamamatsu 430, Japan;Department of Medicine (Neurology), Shinshu University School of Medicine, Matsumoto, Nagano 390, Japan

关键词: Familial amyloidotic polyneuropathy;    Variant transthyretin;    Amino acid sequence;    Point mutation;    DNA diagnosis;   

DOI  :  10.1016/0014-5793(92)81001-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A novel variant transthyretin which contains a leucine-for-valine substitution at position 30 was isolated and identified in the serum of a patient with familial amyloidotic polyneuropathy (FAP). The amino acid substitution was proven to result from a guanine-to-cytosine change at the first base of codon 30 located in exon 2 in the mutated transthyretin gene by restriction fragment length analysis on the amplified transthyretin gene using Cfr13 I. The study indicates that the point mutation of the transthyretin gene is a cause of the disorder.

【 授权许可】

Unknown