Napsin A Expression in Human Tumors and Normal Tissues

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...

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Veröffentlicht in:Pathology oncology research 2021-04, Vol.27, p.613099-613099
Hauptverfasser: 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
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container_title Pathology oncology research
container_volume 27
creator 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
description 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. 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. 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 ( ≤ 0.03). 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.
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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. 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. 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 ( ≤ 0.03). This methodical approach enabled us to identify a ranking order of tumors according to their relative prevalence of Napsin A expression. 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In papillary and clear cell renal cell carcinoma, reduced Napsin A expression was linked to adverse clinic-pathological features ( ≤ 0.03). 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.</description><subject>Antibodies</subject><subject>Aspartic Acid Endopeptidases - analysis</subject><subject>Aspartic Acid Endopeptidases - biosynthesis</subject><subject>Biomarkers, Tumor - metabolism</subject><subject>Cancer</subject><subject>Esophagus</subject><subject>Humans</subject><subject>Kidney cancer</subject><subject>Lung cancer</subject><subject>Medical diagnosis</subject><subject>Metastasis</subject><subject>Neoplasms - metabolism</subject><subject>Ovaries</subject><subject>Pathology</subject><subject>Proteins</subject><subject>Small intestine</subject><subject>Society Journal Archive</subject><subject>Thyroid gland</subject><subject>Tumors</subject><issn>1532-2807</issn><issn>1219-4956</issn><issn>1532-2807</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><recordid>eNpdkc1LwzAYxoMobk7vnqTgxctmvttchDGmE8a8zHNIk1Q72qYmq-h_b8rmmF7eD_K8D--bHwDXCE4IycR967ydYIjRhCMChTgBQ8QIHuMMpqdH9QBchLCBEKZc8HMwIBSzlGV4CPhKtaFskmky_2q9DaF0TRL7RVerJll3tfMhUY1JVs7XqkrWZQidDZfgrFBVsFf7PAKvj_P1bDFevjw9z6bLsaaYbse5yXNNCmJyYQgjMVqRIs15biAsUssoznSRMWM4skYJkWomDNLUIGYUxWQEHna-bZfX1mjbbL2qZOvLWvlv6VQp_7405bt8c58ywxwjKqLB3d7Au4-4-FbWZdC2qlRjXRckZgyxlNK0l97-k25c55t4nux_K-piiiq4U2nvQvC2OCyDoOyhyB6K7KHIHZQ4cnN8xGHglwL5AR8hiPo</recordid><startdate>20210420</startdate><enddate>20210420</enddate><creator>Weidemann, Sören</creator><creator>Böhle, Jan Lukas</creator><creator>Contreras, Hendrina</creator><creator>Luebke, Andreas M</creator><creator>Kluth, Martina</creator><creator>Büscheck, Franziska</creator><creator>Hube-Magg, Claudia</creator><creator>Höflmayer, Doris</creator><creator>Möller, Katharina</creator><creator>Fraune, Christoph</creator><creator>Bernreuther, Christian</creator><creator>Rink, Michael</creator><creator>Simon, Ronald</creator><creator>Menz, Anne</creator><creator>Hinsch, Andrea</creator><creator>Lebok, Patrick</creator><creator>Clauditz, Till</creator><creator>Sauter, Guido</creator><creator>Uhlig, Ria</creator><creator>Wilczak, Waldemar</creator><creator>Steurer, Stefan</creator><creator>Burandt, Eike</creator><creator>Krech, Rainer</creator><creator>Dum, David</creator><creator>Krech, Till</creator><creator>Marx, Andreas</creator><creator>Minner, Sarah</creator><general>Frontiers Media SA</general><general>Frontiers Media S.A</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7RV</scope><scope>7X7</scope><scope>7XB</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>K9.</scope><scope>KB0</scope><scope>M0S</scope><scope>NAPCQ</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20210420</creationdate><title>Napsin A Expression in Human Tumors and Normal Tissues</title><author>Weidemann, Sören ; 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In papillary and clear cell renal cell carcinoma, reduced Napsin A expression was linked to adverse clinic-pathological features ( ≤ 0.03). 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.</abstract><cop>Switzerland</cop><pub>Frontiers Media SA</pub><pmid>34257582</pmid><doi>10.3389/pore.2021.613099</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record>
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source MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central Open Access; PubMed Central
subjects Antibodies
Aspartic Acid Endopeptidases - analysis
Aspartic Acid Endopeptidases - biosynthesis
Biomarkers, Tumor - metabolism
Cancer
Esophagus
Humans
Kidney cancer
Lung cancer
Medical diagnosis
Metastasis
Neoplasms - metabolism
Ovaries
Pathology
Proteins
Small intestine
Society Journal Archive
Thyroid gland
Tumors
title Napsin A Expression in Human Tumors and Normal Tissues
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