Journal
AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS
Volume 19, Issue -, Pages 11-13Publisher
TAYLOR & FRANCIS LTD
DOI: 10.3109/13506129.2012.674989
Keywords
Differential proteomics; mass spectrometry; transthyretin amyloidosis
Categories
Funding
- Fondazione CARIPLO NOBEL
- Proteomic platform
- Fondazione Cariplo [N2009-2532]
- Ricerca Finalizzata Malattie Rare
- Italian Ministry of Health
- ISS [526D/63]
- Ministry of Research and University [2007AESFX2_003]
- Associazione Italiana per la Ricerca sul Cancro [9965]
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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.
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