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A novel transthyretin mutation associated with familial amyloidotic polyneuropathy

1992; Elsevier BV; Volume: 182; Issue: 2 Linguagem: Inglês

10.1016/0006-291x(92)91763-g

1090-2104

T. Murakami, Shuichiro Maeda, Shigehiro Yi, Shinichi Ikegawa, Eiji Kawashima, Soukichi Onodera, Kazunori Shimada, Shukuro Araki,

Peptidase Inhibition and Analysis

We characterized the mutation associated with familial amyloidotic polyneuropathy in a Japanese patient. Sequence analysis of polymerase chain reaction-amplified exons of the transthyretin gene revealed a novel point mutation resulting in a substitution of arginine for glycine at position 47. The mutation was confirmed using allele-specific olgonucleotide hybridization procedures. This most likely represents a de novo mutation since neither parent carries the mutant allele.