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Journal of Biomedicine and BiotechnologyVolume 2011 2011, Article ID 754109, 9 pages

Review Article

The University of Queensland Diamantina Institute, The University of Queensland, Brisbane, QLD 4102, Australia

Pathology Queensland, Princess Alexandra Hospital, Woolloongabba, Brisbane, QLD 4102, Australia

Received 28 April 2011; Revised 1 July 2011; Accepted 11 July 2011

Academic Editor: Jorge Sequeiros

Copyright © 2011 Dorothy Loo et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Amyloidosis is a group of disorders caused by deposition of misfolded proteins as aggregates in the extracellular tissues of the body, leading to impairment of organ function. Correct identification of the causal amyloid protein is absolutely crucial for clinical management in order to avoid misdiagnosis and inappropriate, potentially harmful treatment, to assess prognosis and to offer genetic counselling if relevant. Current diagnostic methods, including antibody-based amyloid typing, have limited ability to detect the full range of amyloid forming proteins. Recent investigations into proteomic identification of amyloid protein have shown promise. This paper will review the current state of the art in proteomic analysis of amyloidosis, discuss the suitability of techniques based on the properties of amyloidosis, and further suggest potential areas of development. Establishment of mass spectrometry aided amyloid typing procedures in the pathology laboratory will allow accurate amyloidosis diagnosis in a timely manner and greatly facilitate clinical management of the disease.

Autor: Dorothy Loo, Peter N. Mollee, Patricia Renaut, and Michelle M. Hill



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