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Carboxypeptidase A1 (CPA1) Immunohistochemistry Is Highly Sensitive and Specific for Acinar Cell Carcinoma (ACC) of the Pancreas

Carboxypeptidase A1 (CPA1) is a zinc metalloprotease that is produced in pancreatic acinar cells and plays a role in cleaving C-terminal branched-chain and aromatic amino acids from dietary proteins. This study assessed the utility of immunohistochemical CPA1 staining for diagnosing pancreatic acina...

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Autores principales: Uhlig, Ria, Contreras, Hendrina, Weidemann, Sören, Gorbokon, Natalia, Menz, Anne, Büscheck, Franziska, Luebke, Andreas M., Kluth, Martina, Hube-Magg, Claudia, Hinsch, Andrea, Höflmayer, Doris, Fraune, Christoph, Möller, Katharina, Bernreuther, Christian, Lebok, Patrick, Sauter, Guido, Wilczak, Waldemar, Izbicki, Jakob, Perez, Daniel, Schrader, Jörg, Steurer, Stefan, Burandt, Eike, Krech, Rainer, Dum, David, Krech, Till, Marx, Andreas, Simon, Ronald, Minner, Sarah, Jacobsen, Frank, Clauditz, Till S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Lippincott Williams & Wilkins 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8860221/
https://www.ncbi.nlm.nih.gov/pubmed/34889867
http://dx.doi.org/10.1097/PAS.0000000000001817
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author Uhlig, Ria
Contreras, Hendrina
Weidemann, Sören
Gorbokon, Natalia
Menz, Anne
Büscheck, Franziska
Luebke, Andreas M.
Kluth, Martina
Hube-Magg, Claudia
Hinsch, Andrea
Höflmayer, Doris
Fraune, Christoph
Möller, Katharina
Bernreuther, Christian
Lebok, Patrick
Sauter, Guido
Wilczak, Waldemar
Izbicki, Jakob
Perez, Daniel
Schrader, Jörg
Steurer, Stefan
Burandt, Eike
Krech, Rainer
Dum, David
Krech, Till
Marx, Andreas
Simon, Ronald
Minner, Sarah
Jacobsen, Frank
Clauditz, Till S.
author_facet Uhlig, Ria
Contreras, Hendrina
Weidemann, Sören
Gorbokon, Natalia
Menz, Anne
Büscheck, Franziska
Luebke, Andreas M.
Kluth, Martina
Hube-Magg, Claudia
Hinsch, Andrea
Höflmayer, Doris
Fraune, Christoph
Möller, Katharina
Bernreuther, Christian
Lebok, Patrick
Sauter, Guido
Wilczak, Waldemar
Izbicki, Jakob
Perez, Daniel
Schrader, Jörg
Steurer, Stefan
Burandt, Eike
Krech, Rainer
Dum, David
Krech, Till
Marx, Andreas
Simon, Ronald
Minner, Sarah
Jacobsen, Frank
Clauditz, Till S.
author_sort Uhlig, Ria
collection PubMed
description Carboxypeptidase A1 (CPA1) is a zinc metalloprotease that is produced in pancreatic acinar cells and plays a role in cleaving C-terminal branched-chain and aromatic amino acids from dietary proteins. This study assessed the utility of immunohistochemical CPA1 staining for diagnosing pancreatic acinar cell carcinoma (ACC). A total of 12,274 tumor samples from 132 different tumor types and subtypes as well as 8 samples each of 76 different normal tissue types were interpretable by immunohistochemistry in a tissue microarray format. CPA1 was strongly expressed in acinar cells of all normal pancreas samples but not in any other normal tissues. CPA1 immunostaining was detected in 100% of 11 pancreatic ACCs and 1 mixed acinar endocrine carcinoma, but absent in 449 pancreatic ductal adenocarcinomas, 75 adenocarcinomas of the ampulla Vateri, and 11,739 other evaluable cancers from 128 different tumor entities. A weak to moderate diffuse staining of epithelial and stromal cells of cancer tissues immediately adjacent to non-neoplastic pancreatic acinar cells often occurred and was considered to be caused by the diffusion of the highly abundant CPA1 from normal acinar cells that may have suffered some autolytic cell damage. In conclusion, our data show that CPA1 is a highly sensitive and largely specific marker for normal and neoplastic pancreatic acinar cells. CPA1 immunohistochemistry greatly facilitates the otherwise often difficult diagnosis of pancreatic ACC.
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spelling pubmed-88602212022-02-24 Carboxypeptidase A1 (CPA1) Immunohistochemistry Is Highly Sensitive and Specific for Acinar Cell Carcinoma (ACC) of the Pancreas Uhlig, Ria Contreras, Hendrina Weidemann, Sören Gorbokon, Natalia Menz, Anne Büscheck, Franziska Luebke, Andreas M. Kluth, Martina Hube-Magg, Claudia Hinsch, Andrea Höflmayer, Doris Fraune, Christoph Möller, Katharina Bernreuther, Christian Lebok, Patrick Sauter, Guido Wilczak, Waldemar Izbicki, Jakob Perez, Daniel Schrader, Jörg Steurer, Stefan Burandt, Eike Krech, Rainer Dum, David Krech, Till Marx, Andreas Simon, Ronald Minner, Sarah Jacobsen, Frank Clauditz, Till S. Am J Surg Pathol Original Articles Carboxypeptidase A1 (CPA1) is a zinc metalloprotease that is produced in pancreatic acinar cells and plays a role in cleaving C-terminal branched-chain and aromatic amino acids from dietary proteins. This study assessed the utility of immunohistochemical CPA1 staining for diagnosing pancreatic acinar cell carcinoma (ACC). A total of 12,274 tumor samples from 132 different tumor types and subtypes as well as 8 samples each of 76 different normal tissue types were interpretable by immunohistochemistry in a tissue microarray format. CPA1 was strongly expressed in acinar cells of all normal pancreas samples but not in any other normal tissues. CPA1 immunostaining was detected in 100% of 11 pancreatic ACCs and 1 mixed acinar endocrine carcinoma, but absent in 449 pancreatic ductal adenocarcinomas, 75 adenocarcinomas of the ampulla Vateri, and 11,739 other evaluable cancers from 128 different tumor entities. A weak to moderate diffuse staining of epithelial and stromal cells of cancer tissues immediately adjacent to non-neoplastic pancreatic acinar cells often occurred and was considered to be caused by the diffusion of the highly abundant CPA1 from normal acinar cells that may have suffered some autolytic cell damage. In conclusion, our data show that CPA1 is a highly sensitive and largely specific marker for normal and neoplastic pancreatic acinar cells. CPA1 immunohistochemistry greatly facilitates the otherwise often difficult diagnosis of pancreatic ACC. Lippincott Williams & Wilkins 2022-01 2021-10-21 /pmc/articles/PMC8860221/ /pubmed/34889867 http://dx.doi.org/10.1097/PAS.0000000000001817 Text en Copyright © 2021 The Author(s). Published by Wolters Kluwer Health, Inc. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article distributed under the terms of the Creative Commons Attribution-Non Commercial-No Derivatives License 4.0 (https://creativecommons.org/licenses/by-nc-nd/4.0/) (CCBY-NC-ND), where it is permissible to download and share the work provided it is properly cited. The work cannot be changed in any way or used commercially without permission from the journal. http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/)
spellingShingle Original Articles
Uhlig, Ria
Contreras, Hendrina
Weidemann, Sören
Gorbokon, Natalia
Menz, Anne
Büscheck, Franziska
Luebke, Andreas M.
Kluth, Martina
Hube-Magg, Claudia
Hinsch, Andrea
Höflmayer, Doris
Fraune, Christoph
Möller, Katharina
Bernreuther, Christian
Lebok, Patrick
Sauter, Guido
Wilczak, Waldemar
Izbicki, Jakob
Perez, Daniel
Schrader, Jörg
Steurer, Stefan
Burandt, Eike
Krech, Rainer
Dum, David
Krech, Till
Marx, Andreas
Simon, Ronald
Minner, Sarah
Jacobsen, Frank
Clauditz, Till S.
Carboxypeptidase A1 (CPA1) Immunohistochemistry Is Highly Sensitive and Specific for Acinar Cell Carcinoma (ACC) of the Pancreas
title Carboxypeptidase A1 (CPA1) Immunohistochemistry Is Highly Sensitive and Specific for Acinar Cell Carcinoma (ACC) of the Pancreas
title_full Carboxypeptidase A1 (CPA1) Immunohistochemistry Is Highly Sensitive and Specific for Acinar Cell Carcinoma (ACC) of the Pancreas
title_fullStr Carboxypeptidase A1 (CPA1) Immunohistochemistry Is Highly Sensitive and Specific for Acinar Cell Carcinoma (ACC) of the Pancreas
title_full_unstemmed Carboxypeptidase A1 (CPA1) Immunohistochemistry Is Highly Sensitive and Specific for Acinar Cell Carcinoma (ACC) of the Pancreas
title_short Carboxypeptidase A1 (CPA1) Immunohistochemistry Is Highly Sensitive and Specific for Acinar Cell Carcinoma (ACC) of the Pancreas
title_sort carboxypeptidase a1 (cpa1) immunohistochemistry is highly sensitive and specific for acinar cell carcinoma (acc) of the pancreas
topic Original Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8860221/
https://www.ncbi.nlm.nih.gov/pubmed/34889867
http://dx.doi.org/10.1097/PAS.0000000000001817
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