Identification of a New Transthyretin Variant (Ile49) in Familial Amyloidotic Polyneuropathy Using Electrospray Ionization Mass Spectrometry and Nonisotopic RNase Cleavage Assay

Mutation of the transthyretin (TTR) plasma protein and gene in a Japanese patient with amyloid polyneuropathy was investigated by electrospray ionization mass spectrometry (ESI-MS) and nonisotopic RNase cleavage assay (NIRCA), respectively. ESI-MS analysis showed normal TTR peaks and additionally a...

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Bibliographic Details
Published in:Human heredity 1999-01, Vol.49 (4), p.186-189
Main Authors: Nakamura, Masaaki, Yamashita, Taro, Ando, Yukio, Hamidi Asl, Kamran, Tashima, Kazuhiro, Ohlsson, Per-Ingvar, Kususe, Yukio, Benson, Merrill D.
Format: Article
Language:English
Subjects:
Aged
Amyloid Neuropathies - genetics
Female
Genetic Variation
Humans
Mass Spectrometry - methods
Original Paper
Polymerase Chain Reaction
Prealbumin - genetics
Restriction Mapping
Ribonucleases - metabolism
RNA, Messenger - metabolism
Sequence Analysis, DNA
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Summary:Mutation of the transthyretin (TTR) plasma protein and gene in a Japanese patient with amyloid polyneuropathy was investigated by electrospray ionization mass spectrometry (ESI-MS) and nonisotopic RNase cleavage assay (NIRCA), respectively. ESI-MS analysis showed normal TTR peaks and additionally a variant TTR with 12- dalton-higher molecular weight than normal TTR. NIRCA suggested that the mutation existed near either the 5' or 3' end of exon 3. Direct DNA sequencing revealed both a normal ACC (threonine) and a variant ATC (isoleucine) at codon 49, which was located near the 5' end of exon 3. The molecular weight shift of this mutation was 12 D, consistent with the result of ESI-MS.
ISSN:0001-5652
1423-0062
DOI:10.1159/000022872