Human Tissue Distribution of TA02, Which is Homologous with a New Type of Aspartic Proteinase, Napsin A
The N‐terminal amino acid sequence of TA02 (molecular weight 35.0 kDa, isoelectric point 5.29), which is associated with primary lung adenocarcinoma, was determined and a fragment peptide was used to generate mouse monoclonal antibodies (mAbs) against TA02. The amino acid sequence suggested that TA0...
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| Veröffentlicht in: | Cancer science 2000-10, Vol.91 (10), p.1015-1021 |
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| creator | Hirano, Takashi Auer, Gert Maeda, Masahiro Hagiwara, Yoshiaki Okada, Shinya Ohira, Tatsuo Okuzawa, Ken Fujioka, Kaoru Franzén, Bo Hibi, Nozomu Seito, Tsutomu Ebihara, Yoshiro Kato, Harubumi |
| description | The N‐terminal amino acid sequence of TA02 (molecular weight 35.0 kDa, isoelectric point 5.29), which is associated with primary lung adenocarcinoma, was determined and a fragment peptide was used to generate mouse monoclonal antibodies (mAbs) against TA02. The amino acid sequence suggested that TA02 might be homologous with napsin A, a new type of aspartic proteinase. In this context, we confirmed the expression of napsin A in primary lung adenocarcinoma using reversetranscription polymerare chain reaction (RT‐PCR) and showed that the TA02 mAbs reacted with glutathione‐S‐transferase (GST)‐napsin A fusion protein. We concluded that TA02 is the same molecule as napsin A, and showed immunohistochemically that it is distributed mainly in type II pneumocytes, alveolar macrophages, renal tubules and exocrine glands and ducts in the pancreas. In particular, type II pneumocytes and alveolar macrophages showed high expression of TA02 among human normal tissues. In primary lung adenocarcinoma, 47 out of 58 (81.0%) primary lesions were positive. All well‐differentiated adenocarcinomas except those of goblet cell type showed high expression of TA02. In addition, two out of seven (28.6%) large cell carcinomas showed low expression of TA02. The other histopathological types of primary lung cancer did not express TA02 at all. A few cases of renal cell cancer, pancreatic cancer, breast cancer, thyroid cancer, colon cancer and ovarian cancer showed low expression, but the staining patterns were completely different from that of primary lung adenocarcinoma, which showed a granular staining pattern. Our novel mAbs should be valuable for immunochemical detection of TA02/napsin A. |
| doi_str_mv | 10.1111/j.1349-7006.2000.tb00879.x |
| format | Article |
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The amino acid sequence suggested that TA02 might be homologous with napsin A, a new type of aspartic proteinase. In this context, we confirmed the expression of napsin A in primary lung adenocarcinoma using reversetranscription polymerare chain reaction (RT‐PCR) and showed that the TA02 mAbs reacted with glutathione‐S‐transferase (GST)‐napsin A fusion protein. We concluded that TA02 is the same molecule as napsin A, and showed immunohistochemically that it is distributed mainly in type II pneumocytes, alveolar macrophages, renal tubules and exocrine glands and ducts in the pancreas. In particular, type II pneumocytes and alveolar macrophages showed high expression of TA02 among human normal tissues. In primary lung adenocarcinoma, 47 out of 58 (81.0%) primary lesions were positive. All well‐differentiated adenocarcinomas except those of goblet cell type showed high expression of TA02. In addition, two out of seven (28.6%) large cell carcinomas showed low expression of TA02. The other histopathological types of primary lung cancer did not express TA02 at all. A few cases of renal cell cancer, pancreatic cancer, breast cancer, thyroid cancer, colon cancer and ovarian cancer showed low expression, but the staining patterns were completely different from that of primary lung adenocarcinoma, which showed a granular staining pattern. Our novel mAbs should be valuable for immunochemical detection of TA02/napsin A.</description><identifier>ISSN: 0910-5050</identifier><identifier>ISSN: 1347-9032</identifier><identifier>EISSN: 1349-7006</identifier><identifier>EISSN: 1876-4673</identifier><identifier>DOI: 10.1111/j.1349-7006.2000.tb00879.x</identifier><identifier>PMID: 11050472</identifier><identifier>CODEN: GANNA2</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Adenocarcinoma ; Adenocarcinoma - metabolism ; Alveoli ; Amino Acid Sequence ; Antibodies, Monoclonal ; Aspartic Acid Endopeptidases - chemistry ; Aspartic Acid Endopeptidases - genetics ; Aspartic Acid Endopeptidases - immunology ; Aspartic proteinase ; Biological and medical sciences ; Biomarkers, Tumor - metabolism ; Blotting, Western ; Breast cancer ; Cancer ; Carcinoma ; Cloning, Molecular ; Colon cancer ; Escherichia coli ; Exocrine glands ; Fusion protein ; Gene Expression ; Glutathione ; human aspartic proteinase ; Humans ; Immunohistochemistry ; Lung cancer ; Lung Neoplasms - metabolism ; Macrophages ; Medical sciences ; Molecular Sequence Data ; Molecular weight ; Monoclonal antibodies ; monoclonal antibody against TA02 ; napsin A ; Ovarian cancer ; Pancreatic cancer ; Pneumocytes ; Pneumology ; primary lung adenocarcinoma ; Proteinase ; Rapid Communication ; Renal cell carcinoma ; Renal tubules ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Analysis, Protein ; TA02 ; Thyroid cancer ; Tissue Distribution ; Tumors of the respiratory system and mediastinum</subject><ispartof>Cancer science, 2000-10, Vol.91 (10), p.1015-1021</ispartof><rights>2001 INIST-CNRS</rights><rights>Copyright John Wiley & Sons, Inc. Oct 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6015-b2f4e6d4125506c752d9daedb534c62a93a9104271fcc2a7227f5305d2d099b83</citedby><cites>FETCH-LOGICAL-c6015-b2f4e6d4125506c752d9daedb534c62a93a9104271fcc2a7227f5305d2d099b83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5926263/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5926263/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,552,727,780,784,885,1416,27915,27916,45565,45566,53782,53784</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=835167$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11050472$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttp://kipublications.ki.se/Default.aspx?queryparsed=id:1934540$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Hirano, Takashi</creatorcontrib><creatorcontrib>Auer, Gert</creatorcontrib><creatorcontrib>Maeda, Masahiro</creatorcontrib><creatorcontrib>Hagiwara, Yoshiaki</creatorcontrib><creatorcontrib>Okada, Shinya</creatorcontrib><creatorcontrib>Ohira, Tatsuo</creatorcontrib><creatorcontrib>Okuzawa, Ken</creatorcontrib><creatorcontrib>Fujioka, Kaoru</creatorcontrib><creatorcontrib>Franzén, Bo</creatorcontrib><creatorcontrib>Hibi, Nozomu</creatorcontrib><creatorcontrib>Seito, Tsutomu</creatorcontrib><creatorcontrib>Ebihara, Yoshiro</creatorcontrib><creatorcontrib>Kato, Harubumi</creatorcontrib><title>Human Tissue Distribution of TA02, Which is Homologous with a New Type of Aspartic Proteinase, Napsin A</title><title>Cancer science</title><addtitle>Jpn J Cancer Res</addtitle><description>The N‐terminal amino acid sequence of TA02 (molecular weight 35.0 kDa, isoelectric point 5.29), which is associated with primary lung adenocarcinoma, was determined and a fragment peptide was used to generate mouse monoclonal antibodies (mAbs) against TA02. The amino acid sequence suggested that TA02 might be homologous with napsin A, a new type of aspartic proteinase. In this context, we confirmed the expression of napsin A in primary lung adenocarcinoma using reversetranscription polymerare chain reaction (RT‐PCR) and showed that the TA02 mAbs reacted with glutathione‐S‐transferase (GST)‐napsin A fusion protein. We concluded that TA02 is the same molecule as napsin A, and showed immunohistochemically that it is distributed mainly in type II pneumocytes, alveolar macrophages, renal tubules and exocrine glands and ducts in the pancreas. In particular, type II pneumocytes and alveolar macrophages showed high expression of TA02 among human normal tissues. In primary lung adenocarcinoma, 47 out of 58 (81.0%) primary lesions were positive. All well‐differentiated adenocarcinomas except those of goblet cell type showed high expression of TA02. In addition, two out of seven (28.6%) large cell carcinomas showed low expression of TA02. The other histopathological types of primary lung cancer did not express TA02 at all. A few cases of renal cell cancer, pancreatic cancer, breast cancer, thyroid cancer, colon cancer and ovarian cancer showed low expression, but the staining patterns were completely different from that of primary lung adenocarcinoma, which showed a granular staining pattern. Our novel mAbs should be valuable for immunochemical detection of TA02/napsin A.</description><subject>Adenocarcinoma</subject><subject>Adenocarcinoma - metabolism</subject><subject>Alveoli</subject><subject>Amino Acid Sequence</subject><subject>Antibodies, Monoclonal</subject><subject>Aspartic Acid Endopeptidases - chemistry</subject><subject>Aspartic Acid Endopeptidases - genetics</subject><subject>Aspartic Acid Endopeptidases - immunology</subject><subject>Aspartic proteinase</subject><subject>Biological and medical sciences</subject><subject>Biomarkers, Tumor - metabolism</subject><subject>Blotting, Western</subject><subject>Breast cancer</subject><subject>Cancer</subject><subject>Carcinoma</subject><subject>Cloning, Molecular</subject><subject>Colon cancer</subject><subject>Escherichia coli</subject><subject>Exocrine glands</subject><subject>Fusion protein</subject><subject>Gene Expression</subject><subject>Glutathione</subject><subject>human aspartic proteinase</subject><subject>Humans</subject><subject>Immunohistochemistry</subject><subject>Lung cancer</subject><subject>Lung Neoplasms - metabolism</subject><subject>Macrophages</subject><subject>Medical sciences</subject><subject>Molecular Sequence Data</subject><subject>Molecular weight</subject><subject>Monoclonal antibodies</subject><subject>monoclonal antibody against TA02</subject><subject>napsin A</subject><subject>Ovarian cancer</subject><subject>Pancreatic cancer</subject><subject>Pneumocytes</subject><subject>Pneumology</subject><subject>primary lung adenocarcinoma</subject><subject>Proteinase</subject><subject>Rapid Communication</subject><subject>Renal cell carcinoma</subject><subject>Renal tubules</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>Sequence Analysis, Protein</subject><subject>TA02</subject><subject>Thyroid cancer</subject><subject>Tissue Distribution</subject><subject>Tumors of the respiratory system and mediastinum</subject><issn>0910-5050</issn><issn>1347-9032</issn><issn>1349-7006</issn><issn>1876-4673</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</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><sourceid>GNUQQ</sourceid><sourceid>D8T</sourceid><recordid>eNqVkcGO0zAQhi0EYsvCKyALJE6bMHZiJ-EAispCkVYLhyKOluM4rUsaBzuh27fHUaOyyw1fxpr5ZvTP_Ai9IhCT8N7uYpKkRZQB8JgCQDxUAHlWxHeP0OJceowWUBCIGDC4QM-83wGQDDh9ii4ICck0owu0WY172eG18X7U-KPxgzPVOBjbYdvgdQn0Cv_YGrXFxuOV3dvWbuzo8cEMWyzxrT7g9bHXE1z6XrrBKPzN2UGbTnp9hW9l702Hy-foSSNbr1_M8RJ9_3S9Xq6im6-fvyzLm0hxICyqaJNqXqeEMgZcZYzWRS11XbEkVZzKIpFhp5RmpFGKyozSrGEJsJrWUBRVnlyi6DTXH3Q_VqJ3Zi_dUVhpxJz6GX5a8HCNHAL__sSHyl7XSneDk-2DtoeVzmzFxv4WrKCc8iQMeDMPcPbXqP0g9sYr3bay0-FQIqMJyxPGA_j6H3BnR9eFYwiaFAXLgaQT9e5EKWe9d7o5SyEgJvfFTkwWi8liMbkvZvfFXWh-eX-Zv62z3fc0SK9k2zjZKePPXNBJeBaoDyfqYFp9_A8BYllek2Bj8gf6HctL</recordid><startdate>200010</startdate><enddate>200010</enddate><creator>Hirano, Takashi</creator><creator>Auer, Gert</creator><creator>Maeda, Masahiro</creator><creator>Hagiwara, Yoshiaki</creator><creator>Okada, Shinya</creator><creator>Ohira, Tatsuo</creator><creator>Okuzawa, Ken</creator><creator>Fujioka, Kaoru</creator><creator>Franzén, Bo</creator><creator>Hibi, Nozomu</creator><creator>Seito, Tsutomu</creator><creator>Ebihara, Yoshiro</creator><creator>Kato, Harubumi</creator><general>Blackwell Publishing Ltd</general><general>Japanese Cancer Association</general><general>John Wiley & Sons, Inc</general><scope>IQODW</scope><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>8FE</scope><scope>8FH</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>7X8</scope><scope>5PM</scope><scope>ADTPV</scope><scope>AOWAS</scope><scope>D8T</scope><scope>ZZAVC</scope></search><sort><creationdate>200010</creationdate><title>Human Tissue Distribution of TA02, Which is Homologous with a New Type of Aspartic Proteinase, Napsin A</title><author>Hirano, Takashi ; Auer, Gert ; Maeda, Masahiro ; Hagiwara, Yoshiaki ; Okada, Shinya ; Ohira, Tatsuo ; Okuzawa, Ken ; Fujioka, Kaoru ; Franzén, Bo ; Hibi, Nozomu ; Seito, Tsutomu ; Ebihara, Yoshiro ; Kato, Harubumi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6015-b2f4e6d4125506c752d9daedb534c62a93a9104271fcc2a7227f5305d2d099b83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Adenocarcinoma</topic><topic>Adenocarcinoma - metabolism</topic><topic>Alveoli</topic><topic>Amino Acid Sequence</topic><topic>Antibodies, Monoclonal</topic><topic>Aspartic Acid Endopeptidases - chemistry</topic><topic>Aspartic Acid Endopeptidases - genetics</topic><topic>Aspartic Acid Endopeptidases - immunology</topic><topic>Aspartic proteinase</topic><topic>Biological and medical sciences</topic><topic>Biomarkers, Tumor - metabolism</topic><topic>Blotting, Western</topic><topic>Breast cancer</topic><topic>Cancer</topic><topic>Carcinoma</topic><topic>Cloning, Molecular</topic><topic>Colon cancer</topic><topic>Escherichia coli</topic><topic>Exocrine glands</topic><topic>Fusion protein</topic><topic>Gene Expression</topic><topic>Glutathione</topic><topic>human aspartic proteinase</topic><topic>Humans</topic><topic>Immunohistochemistry</topic><topic>Lung cancer</topic><topic>Lung Neoplasms - metabolism</topic><topic>Macrophages</topic><topic>Medical sciences</topic><topic>Molecular Sequence Data</topic><topic>Molecular weight</topic><topic>Monoclonal antibodies</topic><topic>monoclonal antibody against TA02</topic><topic>napsin A</topic><topic>Ovarian cancer</topic><topic>Pancreatic cancer</topic><topic>Pneumocytes</topic><topic>Pneumology</topic><topic>primary lung adenocarcinoma</topic><topic>Proteinase</topic><topic>Rapid Communication</topic><topic>Renal cell carcinoma</topic><topic>Renal tubules</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>Sequence Analysis, Protein</topic><topic>TA02</topic><topic>Thyroid cancer</topic><topic>Tissue Distribution</topic><topic>Tumors of the respiratory system and mediastinum</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hirano, Takashi</creatorcontrib><creatorcontrib>Auer, Gert</creatorcontrib><creatorcontrib>Maeda, Masahiro</creatorcontrib><creatorcontrib>Hagiwara, Yoshiaki</creatorcontrib><creatorcontrib>Okada, Shinya</creatorcontrib><creatorcontrib>Ohira, Tatsuo</creatorcontrib><creatorcontrib>Okuzawa, Ken</creatorcontrib><creatorcontrib>Fujioka, Kaoru</creatorcontrib><creatorcontrib>Franzén, Bo</creatorcontrib><creatorcontrib>Hibi, Nozomu</creatorcontrib><creatorcontrib>Seito, Tsutomu</creatorcontrib><creatorcontrib>Ebihara, Yoshiro</creatorcontrib><creatorcontrib>Kato, Harubumi</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>SwePub</collection><collection>SwePub Articles</collection><collection>SWEPUB Freely available online</collection><collection>SwePub Articles full text</collection><jtitle>Cancer science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hirano, Takashi</au><au>Auer, Gert</au><au>Maeda, Masahiro</au><au>Hagiwara, Yoshiaki</au><au>Okada, Shinya</au><au>Ohira, Tatsuo</au><au>Okuzawa, Ken</au><au>Fujioka, Kaoru</au><au>Franzén, Bo</au><au>Hibi, Nozomu</au><au>Seito, Tsutomu</au><au>Ebihara, Yoshiro</au><au>Kato, Harubumi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Human Tissue Distribution of TA02, Which is Homologous with a New Type of Aspartic Proteinase, Napsin A</atitle><jtitle>Cancer science</jtitle><addtitle>Jpn J Cancer Res</addtitle><date>2000-10</date><risdate>2000</risdate><volume>91</volume><issue>10</issue><spage>1015</spage><epage>1021</epage><pages>1015-1021</pages><issn>0910-5050</issn><issn>1347-9032</issn><eissn>1349-7006</eissn><eissn>1876-4673</eissn><coden>GANNA2</coden><abstract>The N‐terminal amino acid sequence of TA02 (molecular weight 35.0 kDa, isoelectric point 5.29), which is associated with primary lung adenocarcinoma, was determined and a fragment peptide was used to generate mouse monoclonal antibodies (mAbs) against TA02. The amino acid sequence suggested that TA02 might be homologous with napsin A, a new type of aspartic proteinase. In this context, we confirmed the expression of napsin A in primary lung adenocarcinoma using reversetranscription polymerare chain reaction (RT‐PCR) and showed that the TA02 mAbs reacted with glutathione‐S‐transferase (GST)‐napsin A fusion protein. We concluded that TA02 is the same molecule as napsin A, and showed immunohistochemically that it is distributed mainly in type II pneumocytes, alveolar macrophages, renal tubules and exocrine glands and ducts in the pancreas. In particular, type II pneumocytes and alveolar macrophages showed high expression of TA02 among human normal tissues. In primary lung adenocarcinoma, 47 out of 58 (81.0%) primary lesions were positive. All well‐differentiated adenocarcinomas except those of goblet cell type showed high expression of TA02. In addition, two out of seven (28.6%) large cell carcinomas showed low expression of TA02. The other histopathological types of primary lung cancer did not express TA02 at all. A few cases of renal cell cancer, pancreatic cancer, breast cancer, thyroid cancer, colon cancer and ovarian cancer showed low expression, but the staining patterns were completely different from that of primary lung adenocarcinoma, which showed a granular staining pattern. Our novel mAbs should be valuable for immunochemical detection of TA02/napsin A.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>11050472</pmid><doi>10.1111/j.1349-7006.2000.tb00879.x</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Cancer science, 2000-10, Vol.91 (10), p.1015-1021 |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; SWEPUB Freely available online; IngentaConnect Free/Open Access Journals; EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Adenocarcinoma Adenocarcinoma - metabolism Alveoli Amino Acid Sequence Antibodies, Monoclonal Aspartic Acid Endopeptidases - chemistry Aspartic Acid Endopeptidases - genetics Aspartic Acid Endopeptidases - immunology Aspartic proteinase Biological and medical sciences Biomarkers, Tumor - metabolism Blotting, Western Breast cancer Cancer Carcinoma Cloning, Molecular Colon cancer Escherichia coli Exocrine glands Fusion protein Gene Expression Glutathione human aspartic proteinase Humans Immunohistochemistry Lung cancer Lung Neoplasms - metabolism Macrophages Medical sciences Molecular Sequence Data Molecular weight Monoclonal antibodies monoclonal antibody against TA02 napsin A Ovarian cancer Pancreatic cancer Pneumocytes Pneumology primary lung adenocarcinoma Proteinase Rapid Communication Renal cell carcinoma Renal tubules Reverse Transcriptase Polymerase Chain Reaction Sequence Analysis, Protein TA02 Thyroid cancer Tissue Distribution Tumors of the respiratory system and mediastinum |
| title | Human Tissue Distribution of TA02, Which is Homologous with a New Type of Aspartic Proteinase, Napsin A |
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