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K(dabsyl)-TSLLMAAPQ-Lucifer yellow + H2O
K(dabsyl)-TSLL + MAAPQ-Lucifer yellow
K(dabsyl)-TSVLMAAPQ-Lucifer yellow + H2O
K(dabsyl)-TSVL + MAAPQ-Lucifer yellow
polypeptide + H2O
peptides
precursor form of surfactant protein B + H2O
fragments of precursor form of surfactant protein B
pulmonary surfactant protein B + H2O
?
pulmonary surfactant protein C + H2O
?
additional information
?
-
K(dabsyl)-TSLLMAAPQ-Lucifer yellow + H2O
K(dabsyl)-TSLL + MAAPQ-Lucifer yellow
-
-
-
?
K(dabsyl)-TSLLMAAPQ-Lucifer yellow + H2O
K(dabsyl)-TSLL + MAAPQ-Lucifer yellow
-
-
-
?
K(dabsyl)-TSVLMAAPQ-Lucifer yellow + H2O
K(dabsyl)-TSVL + MAAPQ-Lucifer yellow
-
-
-
?
K(dabsyl)-TSVLMAAPQ-Lucifer yellow + H2O
K(dabsyl)-TSVL + MAAPQ-Lucifer yellow
synthetic fluorogenic substrate
-
-
?
polypeptide + H2O
peptides
-
-
-
?
polypeptide + H2O
peptides
-
-
-
-
?
polypeptide + H2O
peptides
-
-
-
?
polypeptide + H2O
peptides
-
-
-
-
?
polypeptide + H2O
peptides
-
-
-
?
polypeptide + H2O
peptides
-
-
-
-
?
polypeptide + H2O
peptides
-
-
-
-
?
polypeptide + H2O
peptides
-
-
-
?
precursor form of surfactant protein B + H2O
fragments of precursor form of surfactant protein B
napsin A is involved in the N- and C-terminal processing of proSP-B in type II pneumocytes
-
-
?
precursor form of surfactant protein B + H2O
fragments of precursor form of surfactant protein B
proSP-B, 42 kDa protein, critical component of pulmonary surfactant, several cleavage sites in the N-and C-terminus, 1 cleavage site in the mature protein part
3 processing products
-
?
pulmonary surfactant protein B + H2O
?
-
-
-
-
?
pulmonary surfactant protein B + H2O
?
-
-
-
?
pulmonary surfactant protein B + H2O
?
-
napsin A is involved in the post-translational processing of pulmonary surfactant protein B and C in multivesivular bodies of type II pneumocytes
-
-
?
pulmonary surfactant protein B + H2O
?
-
napsin is involved in the maturation of the biologically active surfactant protein B peptide. Napsin cleaves within the NH2-terminal propeptide between Leu178 and Pro179
-
-
?
pulmonary surfactant protein B + H2O
?
-
napsin cleaves within the NH2-terminal propeptide between Leu178 and Pro179
-
-
?
pulmonary surfactant protein C + H2O
?
-
-
-
-
?
pulmonary surfactant protein C + H2O
?
-
napsin A is involved in the post-translational processing of pulmonary surfactant protein B and C in multivesivular bodies of type II pneumocytes
-
-
?
additional information
?
-
napsin A as a immunocytochemical marker for metastatic lung adenocarcinoma in pleural effusions analyzed
-
-
?
additional information
?
-
napsin A expression analyzed in juvenile and adult forms of Pulmonary alveolar proteinosis (PALP)
-
-
?
additional information
?
-
-
napsin A expression analyzed in juvenile and adult forms of Pulmonary alveolar proteinosis (PALP)
-
-
?
additional information
?
-
napsin A expression in kidney analyzed by in situ hybridization of mRNA, association to tumor growth inhibition determined
-
-
?
additional information
?
-
-
napsin A expression in kidney analyzed by in situ hybridization of mRNA, association to tumor growth inhibition determined
-
-
?
additional information
?
-
association of napsin A to tumor growth inhibition determined
-
-
?
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in pleural effusions
brenda
A0A5F4D0L0
-
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bronchoalveolar lavage fluid (BALF), expression in
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napsin A expression in 82% of 65 samples
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napsin A expression in 37% of 19 samples
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A0A5F4D0L0
-
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A0A5F4D0L0
-
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of peripheral blood
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-
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A0A5F4D0L0
-
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napsin A expression in 60% of 45 samples
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-
-
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-
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the distribution of histotypes for 279 ovarian tumours are analysed
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-
-
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-
-
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-
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-
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-
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-
-
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-
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-
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-
weak detection of napsin A in cytoplasm of lung sarcomatoid carcinoma cells
brenda
A0A5F4D0L0
-
brenda
A0A5F4D0L0
napsin A is expressed mainly by C-cells in thyroid tumors
brenda
-
-
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-
enzymatically active napsin A can be detected in urine of healthy individuals or in patients with transplanted kidney whose kidney function appears half to fully normal. Low activity in samples from patients with diseased kidneys
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napsin A expression in 92% of 101 samples
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napsin A expression in 100% of 7 samples
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-
-
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pneumocyte type II
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-
pneumocyte type II
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pneumocyte type II
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-
pneumocyte type II
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-
enzyme is detected at day 16 of gestation
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pneumocyte type II
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-
-
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-
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-
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-
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-
-
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alveolar
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-
alveolar
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alveolar
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-
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re-expression of napsin A in tumorigenic HEK293 kidney cell line, reduced capacity for anchorage-independent growth observed
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-
-
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-
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high expression level
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fetal, low expression level
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proximal tubule, expression patterns determined by in situ hybridization
brenda
-
napsin-A is strongly expressed in tubules from normal kidney tissue
brenda
-
-
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-
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high expression level
brenda
-
-
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-
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-
-
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-
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high expression level
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high expression level, adult and fetal lung
brenda
-
napsin-A is strongly expressed in the normal lung tissue (macrophages and pneumocytes)
brenda
sclerosing hemangiomas of the lung
brenda
-
-
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-
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A0A5F4D0L0
-
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-
-
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-
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high expression level
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primary lung adenocarcinoma
brenda
-
primary sites of 83 lung adenocarcinomas
brenda
-
primary, napsin A is expressed in more than 90% of primary lung adenocarcinomas but not in other malignancies
brenda
-
brenda
-
-
brenda
A0A5F4D0L0
-
brenda
-
-
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-
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expression in only one of 29 renal cell carcinomas determined, correlation to loss of napsin A expression in high-grade lung adenocarcinomas
brenda
-
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-
-
brenda
-
brenda
-
-
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adult
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low expression level
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low expression level
brenda
A0A5F4D0L0
-
brenda
-
brenda
additional information
A0A5F4D0L0
immunohistochemic enzyme detection, overview
brenda
additional information
-
immunohistochemic enzyme detection, overview
brenda
additional information
-
napsin is not expressed at primary sites or metastatic sites of adenocarcinomas of other organs than lung. Napsin is not expressed at primary sites of other types of lung carcinomas than adenocarcinomas
brenda
additional information
-
napsin-A is not detected in small cell carcinomas or in other carcinomas of nonlung origin except for renal cell carcinoma. Napsin-A expression is absent in control lymph node and gastrointestinal sections
brenda
additional information
-
no detection of napsin A in squamous cell carcinoma cell, colonic adenocarcinoma cell, pancreatic adenocarcinoma cell, breast adenocarcinoma cell, and malignant mesothelioma cell
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additional information
-
not detected in pleural sarcomatoid mesothelioma cells
brenda
additional information
in the endometrium, one lesion in the differential diagnosis of clear cell carcinoma is the nonneoplastic, progestin-related alteration, Arias-Stella reaction. Napsin A is frequently expressed in ovarian clear cell carcinomas (O-CCCs) and endometrial (EM) CCCs, but rarely in ovarian carcinomas (O-EC) and endometrioid carcinomas (EM-EC), and never in high-grade serous carcinoma [HGSC] cases
brenda
additional information
napsin A is predominantly expressed in lung and kidney. Lung napsin A in many mammals is a heterogeneous enzyme with a characteristic ladder-like appearance in SDS-PAGE that might be caused by proteolytically processed N- and/or C-termini, in contrast to the more homogeneous form found in kidneys and primary lung adenocarcinoma
brenda
additional information
no expression is observed in 30 serous adenocarcinomas, 11 serous adenomas or borderline tumors, 19 endometrioid adenocarcinomas, 22 mucinous adenomas or borderline tumors, 10 mucinous adenocarcinomas, or 3 yolk sac tumors of the ovary. Expression of napsin A is also not observed in the normal surface epithelium of the ovary, epithelia of the fallopian tubes, squamous epithelium, endocervical epithelium, or the endometrium of the uterus
brenda
additional information
-
no expression is observed in 30 serous adenocarcinomas, 11 serous adenomas or borderline tumors, 19 endometrioid adenocarcinomas, 22 mucinous adenomas or borderline tumors, 10 mucinous adenocarcinomas, or 3 yolk sac tumors of the ovary. Expression of napsin A is also not observed in the normal surface epithelium of the ovary, epithelia of the fallopian tubes, squamous epithelium, endocervical epithelium, or the endometrium of the uterus
brenda
additional information
no napsin A expression in six steroid cell tumours, 18 adult-type granulosa cell tumours, eight dysgerminomas, and nine other miscellaneous tumour types. Napsin A detection is specific but of intermediate sensitivity as a biomarker. Immunohistochemic analysis, overview
brenda
additional information
-
no activity and mRNA expression in B-lymphocytes
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additional information
no activity and mRNA expression in B-lymphocytes
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analysis
enzyme is a specific marker in diagnosis of primary lung adenocarcinoma and to distinguish it from metastatic adenocarcinoma
analysis
identification of suitable fluorogenic protease substrates for the pharmaceutically important napsin A by an easy, solid-phase combinatorial assay technology
diagnostics
napsin A is a reliable marker for pulmonary adenocarcinoma and is expressed in a subset of ovarian clear cell carcinomas (O-CCCs), endometrial (EM) CCCs, and endometrioid carcinomas (EC). Napsin A levels in O-CCC and EM-CCC are analyzed and compared with levels in other nonmucinous ovarian carcinomas and EM-EC, respectively. But for diagnostics of napsin A expression in Arias-Stella reactions, napsin A expression is frequently present in foci of Arias-Stella reaction, a feature that they share with clear cell carcinomas. Therefore, Napsin A, in and of itself, is of minimal utility in this specific differential diagnostic scenario
diagnostics
napsin A is an intracellular aspartic protease and biomarker of various malignancies like lung adenocarcinoma and ovarian clear cell carcinoma
diagnostics
napsin A is another sensitive and specific marker for distinguishing ovarian clear cell tumors (especially adenocarcinomas) from other ovarian tumor
diagnostics
A0A5F4D0L0
napsin A is useful as a biomarker. Napsin A is as sensitive as calcitonin for C-cell neoplasms, but is less sensitive than thyroglobulin for follicular neoplasms. The tested markers are sensitive and, except for renal cell carcinoma (for Pax8, napsin A) and pulmonary adenocarcinoma (for napsin A), they are specific thyroid tumour markers
diagnostics
napsin A, is useful as a marker of ovarian clear cell carcinoma, immunohistochemical study with 279 ovarian tumour samples, overview. Napsin A detection is specific but of intermediate sensitivity as a biomarker
medicine
enzyme is a specific marker in diagnosis of primary lung adenocarcinoma and to distinguish it from metastatic adenocarcinoma
medicine
-
napsin A is useful to distinguish primary lung adenocarcinoma from adenocarcinomas of other organs
medicine
-
observation that napsin A is expressed in more than 90% of primary lung adenocarcinomas but not in other malignancies shows that napsin A might be a marker for this type of carcinoma. Potential use as a marker for kidney dysfunction
medicine
immunocytochemical markers for lung adenocarcinoma, identification of malignancy in effusions
medicine
studies on differentiation of primary from secondary effects in the pathogenesis of juvenile and adult forms of Pulmonary alveolar proteinosis
medicine
-
napsin A is a sensitive marker for pulmonary adenocarcinoma
medicine
-
napsin-A is a marker for lung adenocarcinoma, napsin-A is useful as a surrogate marker when encountering a poorly differentiated lung adenocarcinoma or an unknown primary tumor
medicine
napsin-A is useful for stages IA and IIIA and also related to regional lymph node metastasis, napsin-A contents correlate with better prognosis in stage IA
medicine
-
among 10 probes of surgically resected sclerosing haemangioma, all tumours have diffuse and intense expression of napsin A in cuboidal superficial cells, whereas the round interstitial component is completely negative in four cases, and shows focal granular cytoplasmic positivity in six cases
medicine
-
use of napsin A to distinguish between metastatic pulmonary and non-pulmonary adenocarvcinomas in cell blocks prepared from malignant pleural effusions. Napsin A is positive in 83% of pulmonary adenocarcinomas tested, while thyroid transcription factor TTF-1 is positive in 57% of pulmonary adenocarcinomas. All non-pulmonary adenocarcinoas tested are negative for napsin A and TTF-1. Napsin A shows a reactivity in more than 75% of the tumor cells in 82% of the positive cases, whereas TTF-1 shows a reactivity in more than 75% of the tumor cells only in 20% of the positive cases
medicine
napsin A is expressed in a wider variety of metastatic nonpulmonary carcinomas than thyroid transcription factorTTF-1, and the monoclonal antibody is more specific. Napsin A is a useful adjunct to TTF-1, because occasional lung adenocarcinomas are TTF-1 negative but napsin A positive
medicine
napsin A is frequently expressed in ovarian clear cell carcinomas and endometrian clear cell carcinomas, rarely in ovarian endometroid carcinomas and endometrian endometroid carcinomas, and never in high-grade serous carcinoma cases. Findings confirm the importance of using a panel of antibodies that includes napsin A, TTF-1, and PAX8 when evaluating metastatic carcinomas of unknown origin
medicine
napsin A staining occurs commonly in the surface cells and less commonly in the round cell component of sclerosing hemangioma, supporting a respiratory epithelial (specifically type II pneumocyte) origin for this tumor. Cytokeratin and TTF-1 staining in surface cells and TTF-1 staining with only weak and inconsistent cytokeratin staining in round cells confirms studies suggesting primitive or incompletely differentiated respiratory epithelium as the likely cell of origin for stromal round cells
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Mori, K.; Shimizu, H.; Konno, A.; Iwanaga, T.
Immunohistochemical localization of napsin and its potential role in protein catabolism in renal proximal tubules
Arch. Histol. Cytol.
65
359-368
2002
Mus musculus, Rattus norvegicus (Q9QX71)
brenda
Schauer-Vukasinovic, V.; Wright, M.B.; Breu, V.; Giller, T.
Cloning, expression and functional characterization of rat napsin
Biochim. Biophys. Acta
1492
207-210
2000
Rattus norvegicus (Q9QX71)
brenda
Ueno, T.; Linder, S.; Elmberger, G.
Aspartic proteinase napsin is a useful marker for diagnosis of primary lung adenocarcinoma
Br. J. Cancer
88
1229-1233
2003
Homo sapiens (O96009)
brenda
Schauer-Vukasinovic, V.; Bur, D.; Kitas, E.; Schlatter, D.; Rosse, G.; Lahm, H.W.; Giller, T.
Purification and characterization of active recombinant human napsin A
Eur. J. Biochem.
267
2573-2580
2000
Homo sapiens (O96009), Homo sapiens
brenda
Tatnell, P.J.; Powell, D.J.; Hill, J.; Smith, T.S.; Tew, D.G.; Kay, J.
Napsins: new human aspartic proteinases. Distinction between two closely related genes
FEBS Lett.
441
43-48
1998
Homo sapiens, Homo sapiens (O96009)
brenda
Chuman, Y.; Bergman, A.; Ueno, T.; Saito, S.; Sakaguchi, K.; Alaiya, A.A.; Franzen, B.; Bergman, T.; Arnott, D.; Auer, G.; Appella, E.; Jornvall, H.; Linder, S.
Napsin A, a member of the aspartic protease family, is abundantly expressed in normal lung and kidney tissue and is expressed in lung adenocarcinomas
FEBS Lett.
462
129-134
1999
Homo sapiens (O96009), Homo sapiens
brenda
Schauer-Vukasinovic, V.; Bur, D.; Kling, D.; Gruninger, F.; Giller, T.
Human napsin A: expression, immunochemical detection, and tissue localization
FEBS Lett.
462
135-139
1999
Homo sapiens (O96009), Homo sapiens
brenda
Brasch, F.; Ochs, M.; Kahne, T.; Guttentag, S.; Schauer-Vukasinovic, V.; Derrick, M.; Johnen, G.; Kapp, N.; Muller, K.M.; Richter, J.; Giller, T.; Hawgood, S.; Buhling, F.
Involvement of napsin A in the C- and N-terminal processing of surfactant protein B in type-II-pneumocytes of the human lung
J. Biol. Chem.
278
49006-49014
2003
Homo sapiens (O96009), Homo sapiens
brenda
Rosse, G.; Kueng, E.; Page, M.G.; Schauer-Vukasinovic, V.; Giller, T.; Lahm, H.W.; Hunziker, P.; Schlatter, D.
Rapid identification of substrates for novel proteases using a combinatorial peptide library
J. Comb. Chem.
2
461-466
2000
Homo sapiens (O96009)
brenda
Hirano, T.; Gong, Y.; Yoshida, K.; Kato, Y.; Yashima, K.; Maeda, M.; Nakagawa, A.; Fujioka, K.; Ohira, T.; Ikeda, N.; Ebihara, Y.; Auer, G.; Kato, H.
Usefulness of TA02 (napsin A) to distinguish primary lung adenocarcinoma from metastatic lung adenocarcinoma
Lung Cancer
41
155-162
2003
Homo sapiens (O96009)
brenda
Benson, D.A.; Boguski, M.S.; Lipman, D.J.; Ostell, J.; Ouellette, B.F.F.; Rapp, B.A.; Wheeler, D.L.
GenBank
Nucleic Acids Res.
27
12-17
1999
Homo sapiens (O96009)
brenda
Cronshaw, R.F.; Schauer-Vukasinovic, V.; Powell, D.J.; Giller, T.; Bur, D.; Kay, J.
Inhibition of human napsin A
Protein Pept. Lett.
10
35-42
2003
Homo sapiens (O96009), Homo sapiens
brenda
Giller, T.; Schauer-Vukasinovic, V.
Napsin A
Handbook of proteolytic enzymes (Barrett, A. J. , Rawlings, N. D. , Woessner, J. F. , eds. ) Academic Press
1
52-53
2004
Homo sapiens
-
brenda
Ueno, T.; Linder, S.; Na, C.L.; Rice, W.R.; Johansson, J.; Weaver, T.E.
Processing of pulmonary surfactant protein B by napsin and cathepsin H
J. Biol. Chem.
279
16178-16184
2004
Homo sapiens
brenda
Suzuki, A.; Shijubo, N.; Yamada, G.; Ichimiya, S.; Satoh, M.; Abe, S.; Sato, N.
Napsin A is useful to distinguish primary lung adenocarcinoma from adenocarcinomas of other organs
Pathol. Res. Pract.
201
579-586
2005
Homo sapiens
brenda
Woischnik, M.; Bauer, A.; Aboutaam, R.; Pamir, A.; Stanzel, F.; de Blic, J.; Griese, M.
Cathepsin H and napsin A are active in the alveoli and increased in alveolar proteinosis
Eur. Respir. J.
31
1197-1204
2008
Homo sapiens (O96009), Homo sapiens
brenda
Dejmek, A.; Naucler, P.; Smedjeback, A.; Kato, H.; Maeda, M.; Yashima, K.; Maeda, J.; Hirano, T.
Napsin A (TA02) is a useful alternative to thyroid transcription factor-1 (TTF-1) for the identification of pulmonary adenocarcinoma cells in pleural effusions
Diagn. Cytopathol.
35
493-497
2007
Homo sapiens (O96009)
brenda
Ueno, T.; Elmberger, G.; Weaver, T.E.; Toi, M.; Linder, S.
The aspartic protease napsin A suppresses tumor growth independent of its catalytic activity
Lab. Invest.
88
256-263
2008
Mus musculus (O09043), Homo sapiens (O96009), Homo sapiens
brenda
Stoll, L.M.; Johnson, M.W.; Gabrielson, E.; Askin, F.; Clark, D.P.; Li, Q.K.
The utility of napsin-A in the identification of primary and metastatic lung adenocarcinoma among cytologically poorly differentiated carcinomas
Cancer Cytopathol.
118
441-449
2010
Homo sapiens
brenda
Takeshima, Y.; Amatya, V.J.; Kushitani, K.; Kaneko, M.; Inai, K.
Value of immunohistochemistry in the differential diagnosis of pleural sarcomatoid mesothelioma from lung sarcomatoid carcinoma
Histopathology
54
667-676
2009
Homo sapiens
brenda
Bishop, J.A.; Sharma, R.; Illei, P.B.
Napsin A and thyroid transcription factor-1 expression in carcinomas of the lung, breast, pancreas, colon, kidney, thyroid, and malignant mesothelioma
Hum. Pathol.
41
20-25
2010
Homo sapiens
brenda
Nishimura, T.; Nomura, M.; Tojo, H.; Hamasaki, H.; Fukuda, T.; Fujii, K.; Mikami, S.; Bando, Y.; Kato, H.
Proteomic analysis of laser-microdissected paraffin-embedded tissues: (2) MRM assay for stage-related proteins upon non-metastatic lung adenocarcinoma
J. Proteomics
73
1100-1110
2010
Homo sapiens (O96009), Homo sapiens
brenda
Kim, J.H.; Kim, Y.S.; Choi, Y.D.; Lee, J.S.; Park, C.S.
Utility of napsin A and thyroid transcription factor 1 in differentiating metastatic pulmonary from non-pulmonary adenocarcinoma in pleural effusion
Acta Cytol.
55
266-270
2011
Homo sapiens
brenda
Rossi, G.; Cadioli, A.; Mengoli, M.; Piccioli, S.; Cavazza, A.
Napsin A expression in pulmonary sclerosing haemangioma
Histopathology
60
361-363
2012
Homo sapiens
brenda
Mukhopadhyay, S.; Katzenstein, A.L.
Comparison of monoclonal napsin A, polyclonal napsin A, and TTF-1 for determining lung origin in metastatic adenocarcinomas
Am. J. Clin. Pathol.
138
703-711
2012
Homo sapiens (O96009)
brenda
Schmidt, L.A.; Myers, J.L.; McHugh, J.B.
Napsin A is differentially expressed in sclerosing hemangiomas of the lung
Arch. Pathol. Lab. Med.
136
1580-1584
2012
Homo sapiens (O96009), Homo sapiens
brenda
Iwamoto, M.; Nakatani, Y.; Fugo, K.; Kishimoto, T.; Kiyokawa, T.
Napsin A is frequently expressed in clear cell carcinoma of the ovary and endometrium
Hum. Pathol.
46
957-962
2015
Homo sapiens (O96009)
brenda
Maurer, A.; Kalbacher, H.
Pepstatin pull-down at high pH is a powerful tool for detection and analysis of napsin A
Biochem. Biophys. Res. Commun.
515
145-148
2019
Homo sapiens (O96009)
brenda
Iwamoto, M.; Nakatani, Y.; Fugo, K.; Kishimoto, T.; Kiyokawa, T.
Napsin A is frequently expressed in clear cell carcinoma of the ovary and endometrium
Hum. Pathol.
46
957-962
2015
Homo sapiens (O96009)
brenda
Ramos-Vara, J.A.; Frank, C.B.; DuSold, D.; Miller, M.A.
Immunohistochemical detection of Pax8 and napsin A in canine thyroid tumours comparison with thyroglobulin, calcitonin and thyroid transcription factor 1
J. Comp. Pathol.
155
286-298
2016
Canis lupus familiaris (A0A5F4D0L0), Canis lupus familiaris
brenda
Yamashita, Y.; Nagasaka, T.; Naiki-Ito, A.; Sato, S.; Suzuki, S.; Toyokuni, S.; Ito, M.; Takahashi, S.
Napsin A is a specific marker for ovarian clear cell adenocarcinoma
Mod. Pathol.
28
111-117
2015
Homo sapiens (O96009), Homo sapiens
brenda
Fadare, O.; Zhao, C.; Khabele, D.; Parkash, V.; Quick, C.M.; Gwin, K.; Desouki, M.M.
Comparative analysis of Napsin A, alpha-methylacyl-coenzyme A racemase (AMACR, P504S), and hepatocyte nuclear factor 1 beta as diagnostic markers of ovarian clear cell carcinoma an immunohistochemical study of 279 ovarian tumours
Pathology
47
105-111
2015
Homo sapiens (O96009)
brenda