A novel transthyretin mutation associated with familial amyloidotic polyneuropathy.
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.
Murakami
T
T
First Department of Internal Medicine, Kumamoto University Medical School, Japan.
Maeda
S
S
Yi
S
S
Ikegawa
S
S
Kawashima
E
E
Onodera
S
S
Shimada
K
K
Araki
S
S
D000328:Adult; D000483:Alleles; D000595:Amino Acid Sequence; D000686:Amyloidosis / Q000235:genetics*; D001483:Base Sequence; D005091:Exons; D005260:Female; D006580:Genetic Carrier Screening; D005838:Genotype; D006801:Humans; D008297:Male; D008969:Molecular Sequence Data; D009154:Mutation; D009422:Nervous System Diseases / Q000235:genetics*; D009838:Oligodeoxyribonucleotides; D010375:Pedigree; D016133:Polymerase Chain Reaction / Q000379:methods; D011228:Prealbumin / Q000235:genetics*
D009838:Oligodeoxyribonucleotides; D011228:Prealbumin