Proteomics of β2-microglobulin amyloid fibrils

Monica Stoppini, Palma Mangione, Maria Monti, Sofia Giorgetti, Loredana Marchese, Patrizia Arcidiaco, Laura Verga, Siro Segagni, Piero Pucci, Giampaolo Merlini, Vittorio Bellotti

Research output: Contribution to journalArticlepeer-review

Abstract

Knowledge on the chemical structure of β2-microglobulin in natural amyloid fibrils is quite limited because of the difficulty in obtaining tissue samples suitable for biochemical studies. We have reviewed the available information on the chemical modifications and we present new data of β2-microglobulin extracted from non-osteotendinous tissues. β2-microglobulin can accumulate in these compartments after long-term haemodialysis but rarely forms amyloid deposits. We confirm that truncation at the N-terminus is an event specific to β2-microglobulin derived from fibrils but is not observed in the β2-microglobulin from plasma or from the insoluble non-fibrillar material deposited in the heart and spleen. We also confirm the partial deamidation of Asn 17 and Asn 42, as well as the oxidation of Met 99 in fibrillar β2-microglobulin. Other previously reported chemical modifications cannot be excluded, but should involve less than 1-2% of the intact molecule.

Original languageEnglish
Pages (from-to)23-33
Number of pages11
JournalBiochimica et Biophysica Acta - Proteins and Proteomics
Volume1753
Issue number1
DOIs
Publication statusPublished - Nov 10 2005

Keywords

  • β2-m modification
  • β2-microglobulin
  • Amyloid fibril
  • Fibril extraction
  • Proteomic analysis

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Genetics

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