Two transthyretin variants (TTR ala-49 and TTR gin-89) in two sicilian kindreds with hereditary amyloidosis

Maria Do Rosário Almeida, Alessandra Ferlini, Antonino Forabosco, MaryAnn Gawinowicz, Pedro P. Costa, Fabrizio Salvi, Rosaria Plasmati, Carlo A. Tassinari, Klaus Altland, Maria João Saraiva

Research output: Contribution to journalArticle

Abstract

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 Gin-89).

Original languageEnglish
Pages (from-to)211-215
Number of pages5
JournalHuman Mutation
Volume1
Issue number3
Publication statusPublished - 1992

Keywords

  • Amyloidosis
  • Cardiomyopathy
  • Neuropathy
  • Transthyretin

ASJC Scopus subject areas

  • Genetics
  • Genetics(clinical)

Fingerprint Dive into the research topics of 'Two transthyretin variants (TTR ala-49 and TTR gin-89) in two sicilian kindreds with hereditary amyloidosis'. Together they form a unique fingerprint.

  • Cite this

    Do Rosário Almeida, M., Ferlini, A., Forabosco, A., Gawinowicz, M., Costa, P. P., Salvi, F., Plasmati, R., Tassinari, C. A., Altland, K., & Saraiva, M. J. (1992). Two transthyretin variants (TTR ala-49 and TTR gin-89) in two sicilian kindreds with hereditary amyloidosis. Human Mutation, 1(3), 211-215.