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Proteomics in protein misfolding diseases

  • Monica Stoppini , Laura Obici , Francesca Lavatelli , Sofia Giorgetti , Loredana Marchese , Remigio Moratti , Vittorio Bellotti and Giampaolo Merlini
Published/Copyright: June 1, 2009

Abstract

Protein misfolding and deposition as amyloid, with consequent tissue damage, plays a key role in the group of diseases generically termed amyloidoses. In the systemic forms, amyloid deposition is widespread and causes severe dysfunction of vital organs. Proteomic analysis, thanks to its versatility and the comprehensiveness of information obtained, is an ideal tool for the study of systemic amyloidoses. It has been successfully employed in the characterization of the circulating amyloidogenic precursors and the analysis of affected tissues, for the diagnostic identification of the fibril components and for characterizing disease-related changes in protein expression. We present the developments in the field of proteomics applied to systemic amyloidoses, and discuss the perspectives opened in the study of these diseases.

Clin Chem Lab Med 2009;47:627–35.


Corresponding author: Giampaolo Merlini, Department of Biochemistry, University of Pavia, Amyloidosis Research and Treatment Center, Biotechnology Research Laboratories, Fondazione IRCCS Policlinico San Matteo, P.le Golgi 19, 27100 Pavia, Italy Phone: +39-0382-502995, Fax: +39-0382-502990,

Received: 2009-2-15
Accepted: 2009-4-20
Published Online: 2009-06-01
Published in Print: 2009-06-01

©2009 by Walter de Gruyter Berlin New York

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