A new transthyretin mutation associated with amyloidotic vitreous opacities. Asparagine for isoleucine at position 84.

doi:10.1016/s0161-6420(92)31949-9

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Article

A new transthyretin mutation associated with amyloidotic vitreous opacities. Asparagine for isoleucine at position 84.

Ophthalmology - 1 Apr 1992

Skinner M, Harding J, Skare I, Jones L A, Cohen A S, Milunsky A, Skare J

Abstract excerpt

An inherited type of amyloidosis was suspected in an individual of Italian descent who presented with vitreous opacities. Although no family history of amyloidosis was apparent, the patient's transthyretin gene was examined and found not to possess any of the known transthyretin mutations. Complete DNA sequencing revealed a substitution of adenine for thymine in the second base of codon 84 causing an amino acid...

Topics

Aged
Amyloidosis
Asparagine
Base Sequence
DNA Mutational Analysis
Electrophoresis, Polyacrylamide Gel
Eye Diseases
Female
Humans
Isoleucine
Molecular Sequence Data

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Pedigree

Polymerase Chain Reaction

Polymorphism, Restriction Fragment Length

Prealbumin

Vitreous Body

Source

Open in PubMed

Identifiers

PMID: 1350083
DOI: 10.1016/s0161-6420(92)31949-9

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1350083-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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