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A double‐variant transthyretin allele (SER 6, ILE 33) in the Israeli patient “SKO” with familial amyloidotic polyneuropathy
Author(s) -
Jacobson Daniel R.,
Buxbaum Joel N.
Publication year - 1994
Publication title -
human mutation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 162
eISSN - 1098-1004
pISSN - 1059-7794
DOI - 10.1002/humu.1380030313
Subject(s) - transthyretin , transversion , polyneuropathy , biology , genetics , transition (genetics) , exon , allele , mutation , amyloidosis , point mutation , compound heterozygosity , dna sequencing , genomic dna , dna , microbiology and biotechnology , gene , medicine , endocrinology
Abstract Transthyretin (TTR) isolated from amyloid fibrils from an Israeli patient (“SKO”) with familial amyloidotic polyneuropathy has been studied by two groups of investigators. Originally, a position 49 Thr→Gly substitution was reported; subsequently, a position 33 Phe→Ile substitution was found instead. We have studied DNA from this patient by single strand conformation polymorphism analysis, restriction analysis, and DNA sequencing. On one allele, exon 2 contained both a T→A transversion at the first position of codon 33, encoding the previously described Phe→Ile substitution, and a G→A transition at the first position of codon 6, encoding a Gly→Ser substitution. The originally reported position 49 mutation was not encoded in the genomic DNA. This is the first report of a TTR double‐variant allele in a patient with TTR amyloidosis. © 1994 Wiley‐Liss, Inc.