Immunohistochemical typing of amyloid in fixed paraffin-embedded samples by an automatic procedure: Comparison with immunofluorescence data on fresh-frozen tissue.

Amyloidosis comprises a spectrum of disorders characterized by the extracellular deposition of amorphous material, originating from an abnormal serum protein. The typing of amyloid into its many variants represents a pivotal step for a correct patient management. Several methods are currently used,...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Antonella Barreca, Emanuel Bottasso, Francesca Veneziano, Manuela Giarin, Alberto Nocifora, Nadia Martinetti, Angelo Attanasio, Luigi Biancone, Giulia Benevolo, Dario Roccatello, Paola Cassoni, Mauro G Papotti, Amyloidosis Group of the “Rete Interregionale Piemonte e Valle d’Aosta per le Malattie Rare”
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/b14ee4b771494c2d95f1b93f6dcc3886
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:b14ee4b771494c2d95f1b93f6dcc3886
record_format	dspace
spelling	oai:doaj.org-article:b14ee4b771494c2d95f1b93f6dcc38862021-12-02T20:17:38ZImmunohistochemical typing of amyloid in fixed paraffin-embedded samples by an automatic procedure: Comparison with immunofluorescence data on fresh-frozen tissue.1932-620310.1371/journal.pone.0256306https://doaj.org/article/b14ee4b771494c2d95f1b93f6dcc38862021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0256306https://doaj.org/toc/1932-6203Amyloidosis comprises a spectrum of disorders characterized by the extracellular deposition of amorphous material, originating from an abnormal serum protein. The typing of amyloid into its many variants represents a pivotal step for a correct patient management. Several methods are currently used, including mass spectrometry, immunofluorescence, immunohistochemistry, and immunogold labeling. The aim of the present study was to investigate the accuracy and reliability of immunohistochemistry by means of a recently developed amyloid antibody panel applicable on fixed paraffin-embedded tissues in an automated platform. Patients with clinically and pathologically proven amyloidosis were divided into two cohorts: a pilot one, which included selected amyloidosis cases from 2009 to 2018, and a retrospective one (comprising all consecutive amyloidosis cases analyzed between November 2018 and May 2020). The above-referred panel of antibodies for amyloid classification was tested in all cases using an automated immunohistochemistry platform. When fresh-frozen material was available, immunofluorescence was also performed. Among 130 patients, a total of 143 samples from different organs was investigated. They corresponded to 51 patients from the pilot cohort and 79 ones from the retrospective cohort. In 82 cases (63%), fresh-frozen tissue was tested by immunofluorescence, serving to define amyloid subtype only in 30 of them (36.6%). On the contrary, the automated immunohistochemistry procedure using the above-referred new antibodies allowed to establish the amyloid type in all 130 cases (100%). These included: ALλ (n = 60, 46.2%), ATTR (n = 29, 22.3%), AA (n = 19, 14.6%), ALκ (n = 18, 13.8%), ALys (n = 2, 1.5%), and Aβ2M amyloidosis (n = 2, 1.5%). The present immunohistochemistry antibody panel represents a sensitive, reliable, fast, and low-cost method for amyloid typing. Since immunohistochemistry is available in most pathology laboratories, it may become the new gold standard for amyloidosis classification, either used alone or combined with mass spectrometry in selected cases.Antonella BarrecaEmanuel BottassoFrancesca VenezianoManuela GiarinAlberto NociforaNadia MartinettiAngelo AttanasioLuigi BianconeGiulia BenevoloDario RoccatelloPaola CassoniMauro G PapottiAmyloidosis Group of the “Rete Interregionale Piemonte e Valle d’Aosta per le Malattie Rare”Public Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 8, p e0256306 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Antonella Barreca Emanuel Bottasso Francesca Veneziano Manuela Giarin Alberto Nocifora Nadia Martinetti Angelo Attanasio Luigi Biancone Giulia Benevolo Dario Roccatello Paola Cassoni Mauro G Papotti Amyloidosis Group of the “Rete Interregionale Piemonte e Valle d’Aosta per le Malattie Rare” Immunohistochemical typing of amyloid in fixed paraffin-embedded samples by an automatic procedure: Comparison with immunofluorescence data on fresh-frozen tissue.
description	Amyloidosis comprises a spectrum of disorders characterized by the extracellular deposition of amorphous material, originating from an abnormal serum protein. The typing of amyloid into its many variants represents a pivotal step for a correct patient management. Several methods are currently used, including mass spectrometry, immunofluorescence, immunohistochemistry, and immunogold labeling. The aim of the present study was to investigate the accuracy and reliability of immunohistochemistry by means of a recently developed amyloid antibody panel applicable on fixed paraffin-embedded tissues in an automated platform. Patients with clinically and pathologically proven amyloidosis were divided into two cohorts: a pilot one, which included selected amyloidosis cases from 2009 to 2018, and a retrospective one (comprising all consecutive amyloidosis cases analyzed between November 2018 and May 2020). The above-referred panel of antibodies for amyloid classification was tested in all cases using an automated immunohistochemistry platform. When fresh-frozen material was available, immunofluorescence was also performed. Among 130 patients, a total of 143 samples from different organs was investigated. They corresponded to 51 patients from the pilot cohort and 79 ones from the retrospective cohort. In 82 cases (63%), fresh-frozen tissue was tested by immunofluorescence, serving to define amyloid subtype only in 30 of them (36.6%). On the contrary, the automated immunohistochemistry procedure using the above-referred new antibodies allowed to establish the amyloid type in all 130 cases (100%). These included: ALλ (n = 60, 46.2%), ATTR (n = 29, 22.3%), AA (n = 19, 14.6%), ALκ (n = 18, 13.8%), ALys (n = 2, 1.5%), and Aβ2M amyloidosis (n = 2, 1.5%). The present immunohistochemistry antibody panel represents a sensitive, reliable, fast, and low-cost method for amyloid typing. Since immunohistochemistry is available in most pathology laboratories, it may become the new gold standard for amyloidosis classification, either used alone or combined with mass spectrometry in selected cases.
format	article
author	Antonella Barreca Emanuel Bottasso Francesca Veneziano Manuela Giarin Alberto Nocifora Nadia Martinetti Angelo Attanasio Luigi Biancone Giulia Benevolo Dario Roccatello Paola Cassoni Mauro G Papotti Amyloidosis Group of the “Rete Interregionale Piemonte e Valle d’Aosta per le Malattie Rare”
author_facet	Antonella Barreca Emanuel Bottasso Francesca Veneziano Manuela Giarin Alberto Nocifora Nadia Martinetti Angelo Attanasio Luigi Biancone Giulia Benevolo Dario Roccatello Paola Cassoni Mauro G Papotti Amyloidosis Group of the “Rete Interregionale Piemonte e Valle d’Aosta per le Malattie Rare”
author_sort	Antonella Barreca
title	Immunohistochemical typing of amyloid in fixed paraffin-embedded samples by an automatic procedure: Comparison with immunofluorescence data on fresh-frozen tissue.
title_short	Immunohistochemical typing of amyloid in fixed paraffin-embedded samples by an automatic procedure: Comparison with immunofluorescence data on fresh-frozen tissue.
title_full	Immunohistochemical typing of amyloid in fixed paraffin-embedded samples by an automatic procedure: Comparison with immunofluorescence data on fresh-frozen tissue.
title_fullStr	Immunohistochemical typing of amyloid in fixed paraffin-embedded samples by an automatic procedure: Comparison with immunofluorescence data on fresh-frozen tissue.
title_full_unstemmed	Immunohistochemical typing of amyloid in fixed paraffin-embedded samples by an automatic procedure: Comparison with immunofluorescence data on fresh-frozen tissue.
title_sort	immunohistochemical typing of amyloid in fixed paraffin-embedded samples by an automatic procedure: comparison with immunofluorescence data on fresh-frozen tissue.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/b14ee4b771494c2d95f1b93f6dcc3886
work_keys_str_mv	AT antonellabarreca immunohistochemicaltypingofamyloidinfixedparaffinembeddedsamplesbyanautomaticprocedurecomparisonwithimmunofluorescencedataonfreshfrozentissue AT emanuelbottasso immunohistochemicaltypingofamyloidinfixedparaffinembeddedsamplesbyanautomaticprocedurecomparisonwithimmunofluorescencedataonfreshfrozentissue AT francescaveneziano immunohistochemicaltypingofamyloidinfixedparaffinembeddedsamplesbyanautomaticprocedurecomparisonwithimmunofluorescencedataonfreshfrozentissue AT manuelagiarin immunohistochemicaltypingofamyloidinfixedparaffinembeddedsamplesbyanautomaticprocedurecomparisonwithimmunofluorescencedataonfreshfrozentissue AT albertonocifora immunohistochemicaltypingofamyloidinfixedparaffinembeddedsamplesbyanautomaticprocedurecomparisonwithimmunofluorescencedataonfreshfrozentissue AT nadiamartinetti immunohistochemicaltypingofamyloidinfixedparaffinembeddedsamplesbyanautomaticprocedurecomparisonwithimmunofluorescencedataonfreshfrozentissue AT angeloattanasio immunohistochemicaltypingofamyloidinfixedparaffinembeddedsamplesbyanautomaticprocedurecomparisonwithimmunofluorescencedataonfreshfrozentissue AT luigibiancone immunohistochemicaltypingofamyloidinfixedparaffinembeddedsamplesbyanautomaticprocedurecomparisonwithimmunofluorescencedataonfreshfrozentissue AT giuliabenevolo immunohistochemicaltypingofamyloidinfixedparaffinembeddedsamplesbyanautomaticprocedurecomparisonwithimmunofluorescencedataonfreshfrozentissue AT darioroccatello immunohistochemicaltypingofamyloidinfixedparaffinembeddedsamplesbyanautomaticprocedurecomparisonwithimmunofluorescencedataonfreshfrozentissue AT paolacassoni immunohistochemicaltypingofamyloidinfixedparaffinembeddedsamplesbyanautomaticprocedurecomparisonwithimmunofluorescencedataonfreshfrozentissue AT maurogpapotti immunohistochemicaltypingofamyloidinfixedparaffinembeddedsamplesbyanautomaticprocedurecomparisonwithimmunofluorescencedataonfreshfrozentissue AT amyloidosisgroupofthereteinterregionalepiemonteevalledaostaperlemalattierare immunohistochemicaltypingofamyloidinfixedparaffinembeddedsamplesbyanautomaticprocedurecomparisonwithimmunofluorescencedataonfreshfrozentissue
_version_	1718374367067373568

Immunohistochemical typing of amyloid in fixed paraffin-embedded samples by an automatic procedure: Comparison with immunofluorescence data on fresh-frozen tissue.

Ejemplares similares