La protéomique, une nouvelle technique pour un typage optimal des amyloses

Abstract

Amyloidosis is a rare group of diseases related to extracellular deposition of proteins in an insoluble beta-pleated sheet structure presenting a characteristic apple-green birefringence under polarized light after Congo red staining. Thirty types of proteins are known to cause amyloidosis. The accurate identification of the amyloid protein is of paramount importance since it is a key step for the clinical management and personalized treatment. Amyloid typing is usually based on immunohistochemistry and immunofluorescence on tissular sections. This approach has several limits leading to a subtyping failure rate of 15 to 58% of cases. To overcome these difficulties, proteomic methods have been developed to characterize directly the amyloid protein. The most advanced technique carried out on fixed and paraffin-embedded tissue consists of laser microdissection followed by mass spectrometry. The type of amyloidosis can be determined in more than 95% of cases. However, the experience for this technique is very limited apart from the Mayo Clinic (Rochester, United States). In France, a very close proteomic assay has been implemented in the department of pathology of Foch Hospital with similar results. The introduction of proteomics in clinical practice represents a major improvement for typing amyloidosis. In this article, we discuss the benefits and limits of the different techniques used for amyloid classification and we briefly report our proteomic results.