A new transthyretin variant (his 69) associated with vitreous amyloid in an FAP family

Steven R. Zeldenrust, Martha Skinner, James Share, Merrill Benson

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

Direct sequencing of the TTR gene from a patient with vitreous amyloid deposits revealed heterozygosity for a previously unreported variant transthyretin gene. Both the normal T and mutant C were present at the first position of codon 69, resulting in a substitution of histidine for tyrosine at amino acid 69 of the TTR protein. This mutation can be detected by conventional RFLP analysis, since a novel Dra III restriction site is created by the mutant base. In addition, a variation of the polymerase chain reaction was used to create an alternative method of detection. The patient presented with vitreous opacities and without polyneuropathy or cardiomyopathy which are normally seen in FAP. Mutant transthyretin may be responsible for the formation of vitreous deposits in other instances where there are minimal systemic findings and no family history of disease.

Original languageEnglish
Pages (from-to)17-22
Number of pages6
JournalAmyloid
Volume1
Issue number1
DOIs
StatePublished - 1994

Fingerprint

Prealbumin
Amyloid
Polyneuropathies
Amyloid Plaques
Cardiomyopathies
Histidine
Codon
Restriction Fragment Length Polymorphisms
Genes
Tyrosine
Amino Acids
Polymerase Chain Reaction
Mutation
Proteins

Keywords

  • Amyloidosis
  • Fap
  • Transthyretin
  • Vitreous opacities

ASJC Scopus subject areas

  • Internal Medicine

Cite this

A new transthyretin variant (his 69) associated with vitreous amyloid in an FAP family. / Zeldenrust, Steven R.; Skinner, Martha; Share, James; Benson, Merrill.

In: Amyloid, Vol. 1, No. 1, 1994, p. 17-22.

Research output: Contribution to journalArticle

Zeldenrust, Steven R. ; Skinner, Martha ; Share, James ; Benson, Merrill. / A new transthyretin variant (his 69) associated with vitreous amyloid in an FAP family. In: Amyloid. 1994 ; Vol. 1, No. 1. pp. 17-22.
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