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Exploring the amyloid proteome in immunoglobulin-derived lymph node amyloidosis using laser microdissection/tandem mass spectrometry. Am J Hematol 2013 Jul;88(7):577-80

Date

04/23/2013

Pubmed ID

23606017

DOI

10.1002/ajh.23456

Scopus ID

2-s2.0-84879361442   12 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.

Author List

D'Souza A, Theis J, Quint P, Kyle R, Gertz M, Zeldenrust S, Vrana J, Dogan A, Dispenzieri A

Author

Anita D'Souza MD Associate Professor in the Medicine department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Aged
Amyloidogenic Proteins
Amyloidosis
Female
Humans
Immunoglobulin Heavy Chains
Immunoglobulin Light Chains
Laser Capture Microdissection
Lymph Nodes
Male
Middle Aged
Proteome
Survival Analysis
Tandem Mass Spectrometry
jenkins-FCD Prod-482 91ad8a360b6da540234915ea01ff80e38bfdb40a