Finnish hereditary amyloidosis. Amino acid sequence homology between the amyloid fibril protein and human plasma gelsoline

FEBS Lett. 1990 Jan 15;260(1):85-7. doi: 10.1016/0014-5793(90)80072-q.


Amyloid fibrils were isolated from the kidney of a patient with Finnish hereditary amyloidosis. After solubilization of the fibrils in guanidine-HCl, fractionation by gel filtration, and purification by reverse-phase high-performance liquid chromatography, a homogeneous amyloid protein with an apparent Mr of 9000 was obtained. The protein was subjected to enzymatic digestion by trypsin and endoproteinase Lys-C. The amino acid sequences were determined for 6 of the released peptides and they were all found to be identical to the reported, deduced primary structure of human plasma gelsoline in the region of amino acids 235-269. The results show that the amyloid fibril protein in Finnish hereditary amyloidosis represents a new type of amyloid protein that shows amino acid sequence homology with gelsoline, an actin-modulating protein.

Publication types

  • Case Reports
  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aged
  • Amino Acid Sequence
  • Amyloidosis / epidemiology
  • Amyloidosis / genetics*
  • Amyloidosis / metabolism
  • Calcium-Binding Proteins / analysis*
  • Calcium-Binding Proteins / blood
  • Chromatography, High Pressure Liquid
  • Electrophoresis, Polyacrylamide Gel
  • Family
  • Finland
  • Gelsolin
  • Humans
  • Kidney / analysis
  • Kidney / metabolism*
  • Male
  • Microfilament Proteins / analysis*
  • Microfilament Proteins / blood
  • Molecular Sequence Data
  • Peptide Fragments / isolation & purification
  • Sequence Homology, Nucleic Acid
  • Serum Amyloid A Protein / isolation & purification*


  • Calcium-Binding Proteins
  • Gelsolin
  • Microfilament Proteins
  • Peptide Fragments
  • Serum Amyloid A Protein