Localized Amyloidosis of the Upper Aerodigestive Tract: Complex Analysis of the Cellular Infiltrate and the Amyloid Mass
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)...
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| Format: | Article |
| Language: | English |
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Wiley
2019-01-01
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| Series: | Analytical Cellular Pathology |
| Online Access: | http://dx.doi.org/10.1155/2019/6165140 |
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| author | Lilla Turiak Bálint Kaszás Krisztián Katona Ágnes Lacza László Márk Károly Vékey László Drahos Tamás Tornóczky |
| author_facet | Lilla Turiak Bálint Kaszás Krisztián Katona Ágnes Lacza László Márk Károly Vékey László Drahos Tamás Tornóczky |
| author_sort | Lilla Turiak |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-a2baa19ff51a4f6dba11edbd0a88db03 |
| institution | Kabale University |
| issn | 2210-7177 2210-7185 |
| language | English |
| publishDate | 2019-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | Analytical Cellular Pathology |
| spelling | doaj-art-a2baa19ff51a4f6dba11edbd0a88db032025-08-20T03:38:44ZengWileyAnalytical Cellular Pathology2210-71772210-71852019-01-01201910.1155/2019/61651406165140Localized Amyloidosis of the Upper Aerodigestive Tract: Complex Analysis of the Cellular Infiltrate and the Amyloid MassLilla Turiak0Bálint Kaszás1Krisztián Katona2Ágnes Lacza3László Márk4Károly Vékey5László Drahos6Tamás Tornóczky7Institute of Organic Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, HungaryDepartment of Pathology, Oral Pathology Unit, Medical School and Clinical Center, Pécs University, HungaryDepartment of Pathology, Oral Pathology Unit, Medical School and Clinical Center, Pécs University, HungaryDepartment of Pathology, Oral Pathology Unit, Medical School and Clinical Center, Pécs University, HungaryDepartment of Biochemistry, Medical School, Pécs University, HungaryInstitute of Organic Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, HungaryInstitute of Organic Chemistry, Research Centre for Natural Sciences, Hungarian Academy of Sciences, Budapest, HungaryDepartment of Pathology, Oral Pathology Unit, Medical School and Clinical Center, Pécs University, HungaryObjectives. 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.http://dx.doi.org/10.1155/2019/6165140 |
| spellingShingle | Lilla Turiak Bálint Kaszás Krisztián Katona Ágnes Lacza László Márk Károly Vékey László Drahos Tamás Tornóczky Localized Amyloidosis of the Upper Aerodigestive Tract: Complex Analysis of the Cellular Infiltrate and the Amyloid Mass Analytical Cellular Pathology |
| title | Localized Amyloidosis of the Upper Aerodigestive Tract: Complex Analysis of the Cellular Infiltrate and the Amyloid Mass |
| title_full | Localized Amyloidosis of the Upper Aerodigestive Tract: Complex Analysis of the Cellular Infiltrate and the Amyloid Mass |
| title_fullStr | Localized Amyloidosis of the Upper Aerodigestive Tract: Complex Analysis of the Cellular Infiltrate and the Amyloid Mass |
| title_full_unstemmed | Localized Amyloidosis of the Upper Aerodigestive Tract: Complex Analysis of the Cellular Infiltrate and the Amyloid Mass |
| title_short | Localized Amyloidosis of the Upper Aerodigestive Tract: Complex Analysis of the Cellular Infiltrate and the Amyloid Mass |
| title_sort | localized amyloidosis of the upper aerodigestive tract complex analysis of the cellular infiltrate and the amyloid mass |
| url | http://dx.doi.org/10.1155/2019/6165140 |
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