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Exploring the amyloid proteome in immunoglobulin‐derived lymph node amyloidosis using laser microdissection/tandem mass spectrometry
Author(s) -
D'Souza Anita,
Theis Jason,
Quint Patrick,
Kyle Robert,
Gertz Morie,
Zeldenrust Steven,
Vrana Julie,
Dogan Ahmet,
Dispenzieri Angela
Publication year - 2013
Publication title -
american journal of hematology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.456
H-Index - 105
eISSN - 1096-8652
pISSN - 0361-8609
DOI - 10.1002/ajh.23456
Subject(s) - laser capture microdissection , proteome , amyloidosis , microdissection , tandem mass spectrometry , pathology , antibody , lymph node , medicine , computational biology , mass spectrometry , chemistry , biology , immunology , chromatography , bioinformatics , biochemistry , gene , gene expression
Amyloidosis affecting lymph nodes (LN) may occur in the setting of systemic amyloidosis or as an entity localized to the site of production (peritumoral). Why some LN amyloid remains peritumoral is unknown. We speculated that the composition of amyloid in these two presentations differs. We analyzed the amyloid proteome in LN amyloid samples to identify differences between the systemic and peritumoral subtypes. In immunoglobulin‐derived LN amyloidosis ( N = 26), 70% had heavy chain amyloid (AH or mixed AH/AL). True localized LN amyloidosis was rare, with only 2 patients without a monoclonal protein component. Nineteen patients (73%) had typical amyloid syndromes (100% of AL vs 67% of AH/AL, P = 0.02). A trend to improved survival for the AH/AL group in comparison to AL (median 5‐year survival 48 vs. 19 months, P = 0.06) was seen. Mass spectrometric amyloid analysis is a powerful tool for characterizing amyloid and may provide additional prognostic information. Am. J. Hematol. 88:577–580, 2013. © 2013 Wiley Periodicals, Inc.