A new mutant transthyretin (Arg 10) associated with familial amyloid polyneuropathy

T. Uemichi, J. R. Murrell, S. Zeldenrust, Merrill Benson

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

We report a new kindred with systemic amyloidosis presenting as peripheral neuropathy in the sixth and seventh decades of life. Polymorphism in exon 2 of the transthyretin (TTR) gene was suggested by single strand conformation polymorphism analysis and determined by direct DNA sequencing. We also developed restriction fragment length polymorphism analysis by polymerase chain reaction using a primer with an induced mutation. The point mutation (cytosine for thymine at position 1038 of the TTR gene) is responsible for substitution of arginine for cysteine at position 10 of the TTR molecule. It is hypothesised that the TTR molecules which have no cysteine have a unique structure in heterozygous TTR polymers and are responsible for amyloid fibril formation.

Original languageEnglish
Pages (from-to)888-891
Number of pages4
JournalJournal of Medical Genetics
Volume29
Issue number12
StatePublished - 1992

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Familial Amyloid Neuropathies
Prealbumin
substitution
Cysteine
Thymine
Cytosine
Peripheral Nervous System Diseases
Amyloidosis
DNA Sequence Analysis
Point Mutation
Amyloid
Restriction Fragment Length Polymorphisms
Genes
Arginine
Exons
Polymers
Arg(10)-transthyretin
Polymerase Chain Reaction
Mutation

ASJC Scopus subject areas

  • Genetics
  • Genetics(clinical)
  • Public Health, Environmental and Occupational Health
  • Health(social science)

Cite this

A new mutant transthyretin (Arg 10) associated with familial amyloid polyneuropathy. / Uemichi, T.; Murrell, J. R.; Zeldenrust, S.; Benson, Merrill.

In: Journal of Medical Genetics, Vol. 29, No. 12, 1992, p. 888-891.

Research output: Contribution to journalArticle

Uemichi, T. ; Murrell, J. R. ; Zeldenrust, S. ; Benson, Merrill. / A new mutant transthyretin (Arg 10) associated with familial amyloid polyneuropathy. In: Journal of Medical Genetics. 1992 ; Vol. 29, No. 12. pp. 888-891.
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