Premium
Two transthyretin variants (TTR Ala‐49 and TTR Gln‐89) in two sicilian kindreds with hereditary amyloidosis
Author(s) -
Almeida Maria do Rosário,
Ferlini Alessandra,
Forabosco Antonino,
Gawinowicz Maryann,
Costa Pedro P.,
Salvi Fabrizio,
Plasmati Rosaria,
Tassinari Carlo A.,
Altland Klaus,
Saraiva Maria Joã
Publication year - 1992
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.1380010306
Subject(s) - transthyretin , amyloidosis , biology , genetics , alanine , threonine , biochemistry , isoelectric focusing , glutamine , amino acid , microbiology and biotechnology , medicine , serine , endocrinology , enzyme , phosphorylation
We report the biochemical and molecular characterization of two new transthyretin (TTR) variants in two Italian families with hereditary amyloidosis. Both families presented neuropathy and cardiomyopathy but they differ in other clinical features. These TTR variants were previously detected by isoelectric focusing (IEF); one is a neutral TTR variant and the other one is basic. By protein and DNA analysis the neutral variant was found to have a substitution of an alanine for a threonine residue at position 49 (TTR Ala‐49) of the polypeptide chain. The basic variant has a glutamine residue replacing glutamate at position 89 (TTR Gln‐89). © 1992 Wiley‐Liss, Inc.