A new transthyretin variant (Ser23Asn) associated with familial amyloidosis in a Portuguese patient

Amyloid. 1999 Jun;6(2):114-8. doi: 10.3109/13506129909007311.

Abstract

The detection and characterization of a new transthyretin (ATTR) variant, Ser23Asn, associated with cardiomyopathy in a Portuguese patient with familial amyloidosis is described. Isoelectric focusing (IEF) of serum from the propositus demonstrated heterozygosity for the presence of wild type and variant ATTR. A combination of mass spectrometric (MS) analyses, including electrospray ionization mass spectrometry (ESI MS), high performance liquid chromatography (HPLC)/ESI MS and matrix-assisted laser desorption/ionization mass spectrometry (MALDI MS) performed on the serum-derived TTR were used to identify and locate the amino acid replacement in the variant protein. Genetic mutation analysis by DNA sequencing and allele-specific PCR confirmed this finding.

Publication types

  • Case Reports
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adult
  • Amino Acid Substitution*
  • Amyloidosis / genetics*
  • Asparagine / chemistry
  • Asparagine / genetics
  • Chromatography, High Pressure Liquid
  • Humans
  • Immunoelectrophoresis
  • Isoelectric Focusing
  • Male
  • Polymorphism, Restriction Fragment Length
  • Portugal
  • Prealbumin / chemistry*
  • Prealbumin / genetics
  • Serine / chemistry
  • Serine / genetics
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Substances

  • Prealbumin
  • Serine
  • Asparagine