A new transthyretin mutation associated with amyloid cardiomyopathy

In transthyretin (TTR) a new mutation (TTR-Thr45) has been identified in a patient with familial amyloidosis characterized clinically by prominent cardiomyopathy and the absence of peripheral neuropathy. Comparative peptide mapping by high-performance liquid chromatography of the patient's plas...

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Bibliographic Details
Published in:American journal of human genetics 1992-05, Vol.50 (5), p.1027-1030
Main Authors: Saraiva, M J, Almeida, M do R, Sherman, W, Gawinowicz, M, Costa, P, Costa, P P, Goodman, D S
Format: Article
Language:English
Subjects:
Amino Acid Sequence
amyloidosis
Amyloidosis - genetics
Base Sequence
Cardiomyopathies - genetics
Exons - genetics
Humans
Male
Molecular Sequence Data
Mutation - genetics
Oligodeoxyribonucleotides - genetics
Peptide Mapping
Polymerase Chain Reaction
Prealbumin - chemistry
Prealbumin - genetics
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Summary:In transthyretin (TTR) a new mutation (TTR-Thr45) has been identified in a patient with familial amyloidosis characterized clinically by prominent cardiomyopathy and the absence of peripheral neuropathy. Comparative peptide mapping by high-performance liquid chromatography of the patient's plasma TTR together with normal TTR showed the presence of an abnormal tryptic peptide in the patient's TTR. The sequence of this peptide (peptide 6, residues 36-48) demonstrated the presence of a threonine-for-alanine substitution at position 45. This change can be explained by a single base change of adenine for guanine in the Ala-45 codon and was demonstrated directly by DNA sequence analysis of PCR-amplified exon 2 of the TTR gene; allele-specific oligonucleotide hybridization both in the patient and in fixed heart tissue from his aunt confirmed the base change. The TTR-Thr45 mutation is a new variant TTR found associated with cardiomyopathy.
ISSN:0002-9297
1537-6605