Changes in tissue proteome associated with ATTR amyloidosis: Insights into pathogenesis

Francesca Brambilla, Francesca Lavatelli, Veronica Valentini, Dario Di Silvestre, Laura Obici, Pierluigi Mauri, Giampaolo Merlini

Research output: Contribution to journalArticle

Abstract

In Transthyretin amyloidosis (ATTR), tissue deposition of transthyretin fibrils translates into a significant subversion of the tissues proteome. We used multidimensional protein identification technology for profiling the proteome of subcutaneous adipose tissue in patients with ATTR, in comparison with controls and patients with other types of amyloidoses, to identify the global proteomic changes related specifically with this disease. The adipose tissue proteome of five ATTR patients and 11 non-affected controls was analyzed. Samples from patients with Light Chain (AL) or reactive (AA) amyloidosis were studied alongside. In all ATTR samples, mass spectrometry data showed that transthyretin was specifically up-represented, being a marker of the nature of the deposits. Tissue resident proteins, involved in key biological processes, were also found to be differently represented compared to controls. The high-throughput analysis of the proteome of amyloid affected fat, combined with bioinformatic data interpretation, is a powerful tool for identification of perturbed protein expression in ATTR amyloidosis.

Original languageEnglish
Pages (from-to)11-13
Number of pages3
JournalAmyloid
Volume19
Issue numberSUPPL. 1
DOIs
Publication statusPublished - Jun 2012

Keywords

  • Differential proteomics
  • Mass spectrometry
  • Transthyretin amyloidosis

ASJC Scopus subject areas

  • Internal Medicine

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