A Clinical Test for the Identification of Amyloid Proteins in Fat Aspirate Biopsy Specimens by Mass Spectrometry

Reference #:

2007-219

Inventors/Contributors

Julie A. Vrana, Ph.D., Ahmet Dogan, M.D., Ph.D., David R. Barnidge, Ph.D., Jason D. Theis, Jeffrey D. Gamez, Steven R. Zeldenrust, M.D., Harold R. Bergen, III, Ph.D.,

Description

The management of systemic amyloidosis relies on the treatment of the underlying etiology and differs radically for different amyloid types. Therefore, given that at least 25 different proteins have been associated with amyloidosis, accurate indentification of proteins deposited as amyloid fibrils is an important clinical problem. This is a novel method that can characterize amyloid subtypes using mass spectrometry (MS) on fat aspirate tissue biopsies. Proteins are extracted, digested with trypsin and identified following MS/MS analysis. Proteins that make up the amyloid plaque such as TTR and light chain amyloids are identified, as well as other constituents of the amyloid deposition such as Serum Amyloid P component and Apolipoprotein E. This method promises to be a clinical test for accurtate identification of amyloid proteins in routinely processed biopsy specimens and overcomes many of the specificity and sensitivity issues associated with current methods such as immunohistochemistry of paraffin embedded sections.

Patent Status

Pending