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Tytuł pozycji:

Immunoelectron microscopy and mass spectrometry for classification of amyloid deposits

Tytuł :
Immunoelectron microscopy and mass spectrometry for classification of amyloid deposits
Autorzy :
Abildgaard, Niels
Rojek, Aleksandra M
Møller, Hanne Eh
Palstrøm, Nicolai Bjødstrup
Nyvold, Charlotte Guldborg
Rasmussen, Lars Melholt
Hansen, Charlotte Toftmann
Beck, Hans Christian
Marcussen, Niels
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Źródło :
Abildgaard, N, Rojek, A M, Møller, H E, Palstrøm, N B, Nyvold, C G, Rasmussen, L M, Hansen, C T, Beck, H C & Marcussen, N 2020, ' Immunoelectron microscopy and mass spectrometry for classification of amyloid deposits ', Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis, vol. 27, no. 1, pp. 59-66 . https://doi.org/10.1080/13506129.2019.1688289
Rok publikacji :
2020
Kolekcja :
University_of_Southern_Denmark_Research_Output
Opis pliku :
application/pdf
Język :
English
ISSN :
1350-6129
13506129
DOI :
10.1080/13506129.2019.1688289
Numer akcesji :
edsair.od......3062..09d21a71711d66854ade49c12f5db29e
Amyloidosis is a shared name for several rare, complex and serious diseases caused by extra-cellular deposits of different misfolded proteins. Accurate characterization of the amyloid protein is essential for patient care. Immunoelectron microscopy (IEM) and laser microdissection followed by tandem mass spectrometry (LMD-MS) are new gold standards for molecular subtyping. Both methods perform superiorly to immunohistochemistry, but their complementarities, strengths and weaknesses across amyloid subtypes and organ biopsy origin remain undefined. Therefore, we performed a retrospective study of 106 Congo Red positive biopsies from different involved organs; heart, kidney, lung, gut mucosa, skin and bone marrow. IEM, performed with gold-labelled antibodies against kappa light chains, lambda light chains, transthyretin and amyloid A, identified specific staining of amyloid fibrils in 91.6%; in six biopsies amyloid fibrils were not identified, and in two, the fibril subtype could not be established. LMD-MS identified amyloid protein signature in 98.1%, but in nine the amyloid protein could not be clearly identified. MS identified protein subtype in 89.6%. Corresponding specificities ranged at organ level from 94-100%. Concordance was 89.6-100% for different amyloid subtypes. Importantly, combined use of both methods increased the diagnostic classification to 100%. Some variety in performances at organ level was observed.

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