Exploring the amyloid proteome in immunoglobulin-derived lymph node amyloidosis using laser microdissection/tandem mass spectrometry

Anita D'Souza, Jason Theis, Patrick Quint, Robert Kyle, Morie Gertz, Steven Zeldenrust, Julie Vrana, Ahmet Dogan, Angela Dispenzieri

Research output: Contribution to journalArticle

11 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)577-580
Number of pages4
JournalAmerican journal of hematology
Volume88
Issue number7
DOIs
StatePublished - Jul 1 2013

ASJC Scopus subject areas

  • Hematology

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