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Napsin A Expression in Human Tumors and Normal Tissues
Background: Novel aspartic proteinase of the pepsin family A (Napsin A, TAO1/TAO2) is a functional aspartic proteinase which is involved in the maturation of prosurfactant protein B in type II pneumocytes and the lysosomal protein catabolism in renal cells. Napsin A is highly expressed in adenocarci...
Autores principales: | , , , , , , , , , , , , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8262149/ https://www.ncbi.nlm.nih.gov/pubmed/34257582 http://dx.doi.org/10.3389/pore.2021.613099 |
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author | Weidemann, Sören Böhle, Jan Lukas Contreras, Hendrina Luebke, Andreas M. Kluth, Martina Büscheck, Franziska Hube-Magg, Claudia Höflmayer, Doris Möller, Katharina Fraune, Christoph Bernreuther, Christian Rink, Michael Simon, Ronald Menz, Anne Hinsch, Andrea Lebok, Patrick Clauditz, Till Sauter, Guido Uhlig, Ria Wilczak, Waldemar Steurer, Stefan Burandt, Eike Krech, Rainer Dum, David Krech, Till Marx, Andreas Minner, Sarah |
author_facet | Weidemann, Sören Böhle, Jan Lukas Contreras, Hendrina Luebke, Andreas M. Kluth, Martina Büscheck, Franziska Hube-Magg, Claudia Höflmayer, Doris Möller, Katharina Fraune, Christoph Bernreuther, Christian Rink, Michael Simon, Ronald Menz, Anne Hinsch, Andrea Lebok, Patrick Clauditz, Till Sauter, Guido Uhlig, Ria Wilczak, Waldemar Steurer, Stefan Burandt, Eike Krech, Rainer Dum, David Krech, Till Marx, Andreas Minner, Sarah |
author_sort | Weidemann, Sören |
collection | PubMed |
description | Background: Novel aspartic proteinase of the pepsin family A (Napsin A, TAO1/TAO2) is a functional aspartic proteinase which is involved in the maturation of prosurfactant protein B in type II pneumocytes and the lysosomal protein catabolism in renal cells. Napsin A is highly expressed in adenocarcinomas of the lung and is thus commonly used to affirm this diagnosis. However, studies have shown that other tumors can also express Napsin A. Methods: To comprehensively determine Napsin A expression in normal and tumor tissue, 11,957 samples from 115 different tumor types and subtypes as well as 500 samples of 76 different normal tissue types were evaluable by immunohistochemistry on tissue microarrays. Results: Napsin A expression was present in 16 different tumor types. Adenocarcinoma of the lung (85.6%), clear cell adenocarcinoma of the ovary (71.7%), clear cell adenocarcinoma of the endometrium (42.8%), papillary renal cell carcinoma (40.2%), clear cell (tubulo) papillary renal cell carcinoma (16.7%), endometrial serous carcinoma (9.3%), papillary thyroid carcinoma (9.3%) and clear cell renal cell carcinoma (8.2%) were among the tumors with the highest prevalence of Napsin A positivity. In papillary and clear cell renal cell carcinoma, reduced Napsin A expression was linked to adverse clinic-pathological features (p ≤ 0.03). Conclusion: This methodical approach enabled us to identify a ranking order of tumors according to their relative prevalence of Napsin A expression. The data also show that loss of Napsin A is linked to tumor dedifferentiation in renal cell carcinomas. |
format | Online Article Text |
id | pubmed-8262149 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-82621492021-07-12 Napsin A Expression in Human Tumors and Normal Tissues Weidemann, Sören Böhle, Jan Lukas Contreras, Hendrina Luebke, Andreas M. Kluth, Martina Büscheck, Franziska Hube-Magg, Claudia Höflmayer, Doris Möller, Katharina Fraune, Christoph Bernreuther, Christian Rink, Michael Simon, Ronald Menz, Anne Hinsch, Andrea Lebok, Patrick Clauditz, Till Sauter, Guido Uhlig, Ria Wilczak, Waldemar Steurer, Stefan Burandt, Eike Krech, Rainer Dum, David Krech, Till Marx, Andreas Minner, Sarah Pathol Oncol Res Society Journal Archive Background: Novel aspartic proteinase of the pepsin family A (Napsin A, TAO1/TAO2) is a functional aspartic proteinase which is involved in the maturation of prosurfactant protein B in type II pneumocytes and the lysosomal protein catabolism in renal cells. Napsin A is highly expressed in adenocarcinomas of the lung and is thus commonly used to affirm this diagnosis. However, studies have shown that other tumors can also express Napsin A. Methods: To comprehensively determine Napsin A expression in normal and tumor tissue, 11,957 samples from 115 different tumor types and subtypes as well as 500 samples of 76 different normal tissue types were evaluable by immunohistochemistry on tissue microarrays. Results: Napsin A expression was present in 16 different tumor types. Adenocarcinoma of the lung (85.6%), clear cell adenocarcinoma of the ovary (71.7%), clear cell adenocarcinoma of the endometrium (42.8%), papillary renal cell carcinoma (40.2%), clear cell (tubulo) papillary renal cell carcinoma (16.7%), endometrial serous carcinoma (9.3%), papillary thyroid carcinoma (9.3%) and clear cell renal cell carcinoma (8.2%) were among the tumors with the highest prevalence of Napsin A positivity. In papillary and clear cell renal cell carcinoma, reduced Napsin A expression was linked to adverse clinic-pathological features (p ≤ 0.03). Conclusion: This methodical approach enabled us to identify a ranking order of tumors according to their relative prevalence of Napsin A expression. The data also show that loss of Napsin A is linked to tumor dedifferentiation in renal cell carcinomas. Frontiers Media S.A. 2021-04-20 /pmc/articles/PMC8262149/ /pubmed/34257582 http://dx.doi.org/10.3389/pore.2021.613099 Text en Copyright © 2021 Weidemann, Böhle, Contreras, Luebke, Kluth, Büscheck, Hube-Magg, Höflmayer, Möller, Fraune, Bernreuther, Rink, Simon, Menz, Hinsch, Lebok, Clauditz, Sauter, Uhlig, Wilczak, Steurer, Burandt, Krech, Dum, Krech, Marx and Minner. https://creativecommons.org/licenses/by/4.0/This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Society Journal Archive Weidemann, Sören Böhle, Jan Lukas Contreras, Hendrina Luebke, Andreas M. Kluth, Martina Büscheck, Franziska Hube-Magg, Claudia Höflmayer, Doris Möller, Katharina Fraune, Christoph Bernreuther, Christian Rink, Michael Simon, Ronald Menz, Anne Hinsch, Andrea Lebok, Patrick Clauditz, Till Sauter, Guido Uhlig, Ria Wilczak, Waldemar Steurer, Stefan Burandt, Eike Krech, Rainer Dum, David Krech, Till Marx, Andreas Minner, Sarah Napsin A Expression in Human Tumors and Normal Tissues |
title | Napsin A Expression in Human Tumors and Normal Tissues |
title_full | Napsin A Expression in Human Tumors and Normal Tissues |
title_fullStr | Napsin A Expression in Human Tumors and Normal Tissues |
title_full_unstemmed | Napsin A Expression in Human Tumors and Normal Tissues |
title_short | Napsin A Expression in Human Tumors and Normal Tissues |
title_sort | napsin a expression in human tumors and normal tissues |
topic | Society Journal Archive |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8262149/ https://www.ncbi.nlm.nih.gov/pubmed/34257582 http://dx.doi.org/10.3389/pore.2021.613099 |
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