Proteomics in molecular diagnosis: typing of amyloidosis

Loo, Dorothy, Mollee, Peter N., Renaut, Patricia and Hill, Michelle M. (2011) Proteomics in molecular diagnosis: typing of amyloidosis. Journal of Biomedicine and Biotechnology, 2011 754109.1-754109.9. doi:10.1155/2011/754109

Author Loo, Dorothy
Mollee, Peter N.
Renaut, Patricia
Hill, Michelle M.
Title Proteomics in molecular diagnosis: typing of amyloidosis
Journal name Journal of Biomedicine and Biotechnology   Check publisher's open access policy
ISSN 1110-7243
Publication date 2011
Sub-type Critical review of research, literature review, critical commentary
DOI 10.1155/2011/754109
Open Access Status DOI
Volume 2011
Start page 754109.1
End page 754109.9
Total pages 9
Place of publication New York, NY, United States
Publisher Hindawi Publishing Corporation
Collection year 2012
Language eng
Abstract 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.
Keyword Tandem mass-spectrometry
Light-chain amyloidosis
Systemic amyloidosis
Variant transthyretins
Laboratory features
Sequence databases
Q-Index Code CX
Q-Index Status Confirmed Code
Institutional Status UQ
Additional Notes Article # 754109

Document type: Journal Article
Sub-type: Critical review of research, literature review, critical commentary
Collections: Non HERDC
ERA White List Items
UQ Diamantina Institute - Open Access Collection
UQ Diamantina Institute Publications
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Citation counts: TR Web of Science Citation Count  Cited 7 times in Thomson Reuters Web of Science Article | Citations
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