Research ExplorerPublicationsNapsin A Expression in Human Tumors and Normal Tissues

Napsin A Expression in Human Tumors and Normal Tissues

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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.

In: PATHOL ONCOL RES, Vol. 27, 2021, p. 613099.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Weidemann, S, Böhle, JL, Contreras, H, Luebke, AM, Kluth, M, Büscheck, F, Hube-Magg, C, Höflmayer, D, Möller, K, Fraune, C, Bernreuther, C, Rink, M, Simon, R, Menz, A, Hinsch, A, Lebok, P, Clauditz, T, Sauter, G, Uhlig, R, Wilczak, W, Steurer, S, Burandt, E, Krech, R, Dum, D, Krech, T, Marx, A & Minner, S 2021, 'Napsin A Expression in Human Tumors and Normal Tissues', PATHOL ONCOL RES, vol. 27, pp. 613099. https://doi.org/10.3389/pore.2021.613099

APA

Weidemann, S., Böhle, J. L., Contreras, H., Luebke, A. M., Kluth, M., Büscheck, F., Hube-Magg, C., Höflmayer, D., Möller, K., Fraune, C., Bernreuther, C., Rink, M., Simon, R., Menz, A., Hinsch, A., Lebok, P., Clauditz, T., Sauter, G., Uhlig, R., ... Minner, S. (2021). Napsin A Expression in Human Tumors and Normal Tissues. PATHOL ONCOL RES, 27, 613099. https://doi.org/10.3389/pore.2021.613099

Vancouver

Weidemann S, Böhle JL, Contreras H, Luebke AM, Kluth M, Büscheck F et al. Napsin A Expression in Human Tumors and Normal Tissues. PATHOL ONCOL RES. 2021;27:613099. https://doi.org/10.3389/pore.2021.613099

Bibtex

@article{598a16a963714345b8bbcb5af0edb856,
title = "Napsin A Expression in Human Tumors and Normal Tissues",
abstract = "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.",
author = "S{\"o}ren Weidemann and B{\"o}hle, {Jan Lukas} and Hendrina Contreras and Luebke, {Andreas M} and Martina Kluth and Franziska B{\"u}scheck and Claudia Hube-Magg and Doris H{\"o}flmayer and Katharina M{\"o}ller and Christoph Fraune and Christian Bernreuther and Michael Rink and Ronald Simon and Anne Menz and Andrea Hinsch and Patrick Lebok and Till Clauditz and Guido Sauter and Ria Uhlig and Waldemar Wilczak and Stefan Steurer and Eike Burandt and Rainer Krech and David Dum and Till Krech and Andreas Marx and Sarah Minner",
note = "Copyright {\textcopyright} 2021 Weidemann, B{\"o}hle, Contreras, Luebke, Kluth, B{\"u}scheck, Hube-Magg, H{\"o}flmayer, M{\"o}ller, Fraune, Bernreuther, Rink, Simon, Menz, Hinsch, Lebok, Clauditz, Sauter, Uhlig, Wilczak, Steurer, Burandt, Krech, Dum, Krech, Marx and Minner.",
year = "2021",
doi = "10.3389/pore.2021.613099",
language = "English",
volume = "27",
pages = "613099",
journal = "PATHOL ONCOL RES",
issn = "1219-4956",
publisher = "Springer Netherlands",

}

RIS

TY - JOUR

T1 - Napsin A Expression in Human Tumors and Normal Tissues

AU - Weidemann, Sören

AU - Böhle, Jan Lukas

AU - Contreras, Hendrina

AU - Luebke, Andreas M

AU - Kluth, Martina

AU - Büscheck, Franziska

AU - Hube-Magg, Claudia

AU - Höflmayer, Doris

AU - Möller, Katharina

AU - Fraune, Christoph

AU - Bernreuther, Christian

AU - Rink, Michael

AU - Simon, Ronald

AU - Menz, Anne

AU - Hinsch, Andrea

AU - Lebok, Patrick

AU - Clauditz, Till

AU - Sauter, Guido

AU - Uhlig, Ria

AU - Wilczak, Waldemar

AU - Steurer, Stefan

AU - Burandt, Eike

AU - Krech, Rainer

AU - Dum, David

AU - Krech, Till

AU - Marx, Andreas

AU - Minner, Sarah

N1 - 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.

PY - 2021

Y1 - 2021

N2 - 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.

AB - 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.

U2 - 10.3389/pore.2021.613099

DO - 10.3389/pore.2021.613099

M3 - SCORING: Journal article

C2 - 34257582

VL - 27

SP - 613099

JO - PATHOL ONCOL RES

JF - PATHOL ONCOL RES

SN - 1219-4956

ER -