Identification of two novel amyloid A protein subsets coexisting in an individual patient of AA-amyloidosis

Biochim Biophys Acta. 1992 Dec 10;1180(2):195-200. doi: 10.1016/0925-4439(92)90068-x.

Abstract

Amyloid A protein (AA), the major fibril protein in AA-amyloidosis, is an N-terminal cleavage product of the precursor protein, serum amyloid A (SAA). Using mass spectrometry and amino-acid sequencing, we identified and characterized two novel AA protein subsets co-deposited as amyloid fibrils in an patient having AA-amyloidosis associated with rheumatoid arthritis. One of the AA proteins corresponded to positions 2-76 (or 75) of SAA2 alpha and the other corresponded to positions 2-76 (or 75) of known SAA1 subsets, except for position 52 or 57, where SAA1 alpha has valine and alanine and SAA1 beta has alanine and valine in position 52 and 57, respectively, whereas the AA protein had alanine at the both positions. Our findings (1), demonstrate that not only one but two SAA subsets could be deposited together as an AA-amyloid in a single individual and (2), support the existence of a novel SAA1 allotype, i.e., SAA152,57Ala.

Publication types

  • Case Reports

MeSH terms

  • Alanine
  • Amino Acid Sequence
  • Amyloid / analysis*
  • Amyloidosis / complications
  • Amyloidosis / metabolism*
  • Arthritis, Rheumatoid / complications
  • Female
  • Humans
  • Middle Aged
  • Molecular Sequence Data
  • Molecular Weight
  • Serum Amyloid A Protein / chemistry
  • Serum Amyloid A Protein / isolation & purification*
  • Thyroid Gland / chemistry
  • Trypsin
  • Valine

Substances

  • Amyloid
  • Serum Amyloid A Protein
  • Trypsin
  • Valine
  • Alanine