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Localized Amyloidosis of the Upper Aerodigestive Tract: Complex Analysis of the Cellular Infiltrate and the Amyloid Mass
Joint Authors
Drahos, L.
Turiak, Lilla
Kaszás, Bálint
Katona, Krisztián
Lacza, Ágnes
Márk, László
Vékey, Károly
Tornóczky, Tamás
Source
Issue
Vol. 2019, Issue 2019 (31 Dec. 2019), pp.1-9, 9 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2019-08-19
Country of Publication
Egypt
No. of Pages
9
Main Subjects
Abstract EN
Objectives.
The aim of this study was to analyse the composition of amyloid mass and the plasmacytic infiltrate of localized amyloidosis of the upper aerodigestive tract.
Methods.
Biopsy materials were studied by light microscopy, immunohistochemistry (IHC), and mRNA in situ hybridization (mRNA-ISH).
The amyloid mass was also analysed with high-performance liquid chromatography mass spectrometry- (HPLC-MS-) based proteomics.
Results.
Nodular and diffuse forms of amyloid deposition were detected.
IHC analysis revealed λ-light chain (LC) in two cases, κ-LC in one case.
The remaining two were positive with both.
Proteins, well known from other amyloidoses like amyloid A (AA), prealbumin/transthyretin (PA), apolipoprotein A-I (ApoAI), and amyloid P component (APC), and also keratin were found with variable intensities in the cases.
HPLC-MS revealed dozens of proteins with both LCs in all the lesions but sometimes with surprisingly small intensities.
mRNA-ISH analysis revealed identical λ and κ dominance and only one normal κ/λ cell ratio.
Conclusion.
Cellular infiltrate and protein components in the amyloid showed congruent results in all but one case.
The only exception with normal cell ratio and λ-dominant amyloid could be originated from the different protein-secreting activity of plasma cell clones.
HPLC-MS analysis explored both LCs in all the amyloid in variable amount, but other proteins with much higher intensities like keratins, apolipoprotein A-IV (ApoAIV), were also detected.
Proteins like AA, PA, ApoAI, and APC, previously known about amyloid-forming capability, also appeared.
This indicates that localized amyloid in the upper aerodigestive tract is not a homogenous immunoglobulin mass but a mixture of proteins.
The sometimes very low light chain intensities might also suggest that not all the localized amyloidosis cases of the upper aerodigestive tract are of convincingly AL type, and the analysis of the cellular infiltrate might indicate that not all are monoclonal.
American Psychological Association (APA)
Turiak, Lilla& Kaszás, Bálint& Katona, Krisztián& Lacza, Ágnes& Márk, László& Vékey, Károly…[et al.]. 2019. Localized Amyloidosis of the Upper Aerodigestive Tract: Complex Analysis of the Cellular Infiltrate and the Amyloid Mass. Analytical Cellular Pathology،Vol. 2019, no. 2019, pp.1-9.
https://search.emarefa.net/detail/BIM-1117867
Modern Language Association (MLA)
Turiak, Lilla…[et al.]. Localized Amyloidosis of the Upper Aerodigestive Tract: Complex Analysis of the Cellular Infiltrate and the Amyloid Mass. Analytical Cellular Pathology No. 2019 (2019), pp.1-9.
https://search.emarefa.net/detail/BIM-1117867
American Medical Association (AMA)
Turiak, Lilla& Kaszás, Bálint& Katona, Krisztián& Lacza, Ágnes& Márk, László& Vékey, Károly…[et al.]. Localized Amyloidosis of the Upper Aerodigestive Tract: Complex Analysis of the Cellular Infiltrate and the Amyloid Mass. Analytical Cellular Pathology. 2019. Vol. 2019, no. 2019, pp.1-9.
https://search.emarefa.net/detail/BIM-1117867
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-1117867