Development of novel monoclonal antibodies with specific binding affinity for denatured human CD26 in formalin-fixed paraffin-embedded and decalcified specimens
A 110-kDa type II transmembrane glycoprotein with dipeptidyl peptidase IV (DPPIV) activity in its extracellular region, CD26 has a multitude of biological functions and plays an important role in the regulation of inflammatory responses and tumor biology. Our work has focused on CD26 as a novel ther...
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| Veröffentlicht in: | PloS one 2019-06, Vol.14 (6), p.e0218330-e0218330 |
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| creator | Hatano, Ryo Yamada, Taketo Madokoro, Hiroko Otsuka, Haruna Komiya, Eriko Itoh, Takumi Narita, Yuka Iwata, Satoshi Yamazaki, Hiroto Matsuoka, Shuji Dang, Nam H Ohnuma, Kei Morimoto, Chikao |
| description | A 110-kDa type II transmembrane glycoprotein with dipeptidyl peptidase IV (DPPIV) activity in its extracellular region, CD26 has a multitude of biological functions and plays an important role in the regulation of inflammatory responses and tumor biology. Our work has focused on CD26 as a novel therapeutic target for various tumors and immune disorders, and we have recently developed a humanized anti-CD26 monoclonal antibody (mAb), YS110, which has promising safety profile and clinical activity in patients with malignant pleural mesothelioma. The development of an anti-human CD26 mAb that can clearly and reliably detect the denatured CD26 molecule in formalin-fixed paraffin-embedded (FFPE) tissues in the clinical setting is therefore of the utmost importance. To develop novel anti-CD26 mAbs capable of binding to denatured CD26, we immunized mice with urea-treated CD26 protein. Hybridoma supernatants were screened for specific reactivity with human CD26 by immunostaining through the use of a set of FFPE human CD26-positive or negative tumor cell lines. This screening method enables us to develop novel anti-human CD26 mAbs suitable for immunohistochemical staining of CD26 in FFPE non-tumor and tumor tissue sections with reliable clarity and intensity. Specifically, these mAbs display strong binding affinity to denatured human CD26 rather than undenatured human CD26, and are capable of detecting denatured human CD26 in decalcified specimens. These novel anti-CD26 mAbs are potentially useful for the analysis of CD26 expression in cancer patients with bony metastasis, and may help decide the appropriateness of YS110 therapy for future cancer patients. |
| doi_str_mv | 10.1371/journal.pone.0218330 |
| format | Article |
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Our work has focused on CD26 as a novel therapeutic target for various tumors and immune disorders, and we have recently developed a humanized anti-CD26 monoclonal antibody (mAb), YS110, which has promising safety profile and clinical activity in patients with malignant pleural mesothelioma. The development of an anti-human CD26 mAb that can clearly and reliably detect the denatured CD26 molecule in formalin-fixed paraffin-embedded (FFPE) tissues in the clinical setting is therefore of the utmost importance. To develop novel anti-CD26 mAbs capable of binding to denatured CD26, we immunized mice with urea-treated CD26 protein. Hybridoma supernatants were screened for specific reactivity with human CD26 by immunostaining through the use of a set of FFPE human CD26-positive or negative tumor cell lines. This screening method enables us to develop novel anti-human CD26 mAbs suitable for immunohistochemical staining of CD26 in FFPE non-tumor and tumor tissue sections with reliable clarity and intensity. Specifically, these mAbs display strong binding affinity to denatured human CD26 rather than undenatured human CD26, and are capable of detecting denatured human CD26 in decalcified specimens. These novel anti-CD26 mAbs are potentially useful for the analysis of CD26 expression in cancer patients with bony metastasis, and may help decide the appropriateness of YS110 therapy for future cancer patients.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0218330</identifier><identifier>PMID: 31194830</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Affinity ; Amino acids ; Animals ; Antibodies ; Antibodies, Monoclonal - immunology ; Antibodies, Monoclonal, Humanized - genetics ; Antibodies, Monoclonal, Humanized - immunology ; Antigens ; Antineoplastic agents ; Antineoplastic Agents, Immunological - immunology ; Binding ; Biology and Life Sciences ; Cancer ; Cancer metastasis ; Cancer research ; Cancer treatment ; Cell growth ; Cell Line, Tumor ; Clinical trials ; Composition ; Cyclin-dependent kinases ; Dipeptidyl Peptidase 4 - analysis ; Dipeptidyl Peptidase 4 - immunology ; Dipeptidyl Peptidase 4 - metabolism ; Dipeptidyl-peptidase IV ; Displays (Marketing) ; EDTA ; Formaldehyde ; Glycoproteins ; Health aspects ; Humans ; Hybridomas - metabolism ; Immunization ; Immunoglobulins ; Immunohistochemistry ; Inflammation ; Kinases ; Lymphoma ; Medical schools ; Medicine ; Medicine and Health Sciences ; Mesothelioma ; Metastases ; Mice ; Monoclonal antibodies ; Paraffin ; Paraffin Embedding ; Paraffins ; Pathology ; Peptidase ; Prostate cancer ; Proteases ; Protein Engineering - methods ; Research and Analysis Methods ; Signal transduction ; Testing ; Therapeutic applications ; Thyroid cancer ; Tumor cell lines ; Tumors ; Urea</subject><ispartof>PloS one, 2019-06, Vol.14 (6), p.e0218330-e0218330</ispartof><rights>COPYRIGHT 2019 Public Library of Science</rights><rights>2019 Hatano et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2019 Hatano et al 2019 Hatano et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c622t-d4c5119ee25d104ba02a6e94087063045d44ac8d9eb6e50d4f39840013de781d3</citedby><cites>FETCH-LOGICAL-c622t-d4c5119ee25d104ba02a6e94087063045d44ac8d9eb6e50d4f39840013de781d3</cites><orcidid>0000-0002-3140-3596</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6564021/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6564021/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79342,79343</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31194830$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hatano, Ryo</creatorcontrib><creatorcontrib>Yamada, Taketo</creatorcontrib><creatorcontrib>Madokoro, Hiroko</creatorcontrib><creatorcontrib>Otsuka, Haruna</creatorcontrib><creatorcontrib>Komiya, Eriko</creatorcontrib><creatorcontrib>Itoh, Takumi</creatorcontrib><creatorcontrib>Narita, Yuka</creatorcontrib><creatorcontrib>Iwata, Satoshi</creatorcontrib><creatorcontrib>Yamazaki, Hiroto</creatorcontrib><creatorcontrib>Matsuoka, Shuji</creatorcontrib><creatorcontrib>Dang, Nam H</creatorcontrib><creatorcontrib>Ohnuma, Kei</creatorcontrib><creatorcontrib>Morimoto, Chikao</creatorcontrib><title>Development of novel monoclonal antibodies with specific binding affinity for denatured human CD26 in formalin-fixed paraffin-embedded and decalcified specimens</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>A 110-kDa type II transmembrane glycoprotein with dipeptidyl peptidase IV (DPPIV) activity in its extracellular region, CD26 has a multitude of biological functions and plays an important role in the regulation of inflammatory responses and tumor biology. Our work has focused on CD26 as a novel therapeutic target for various tumors and immune disorders, and we have recently developed a humanized anti-CD26 monoclonal antibody (mAb), YS110, which has promising safety profile and clinical activity in patients with malignant pleural mesothelioma. The development of an anti-human CD26 mAb that can clearly and reliably detect the denatured CD26 molecule in formalin-fixed paraffin-embedded (FFPE) tissues in the clinical setting is therefore of the utmost importance. To develop novel anti-CD26 mAbs capable of binding to denatured CD26, we immunized mice with urea-treated CD26 protein. Hybridoma supernatants were screened for specific reactivity with human CD26 by immunostaining through the use of a set of FFPE human CD26-positive or negative tumor cell lines. This screening method enables us to develop novel anti-human CD26 mAbs suitable for immunohistochemical staining of CD26 in FFPE non-tumor and tumor tissue sections with reliable clarity and intensity. Specifically, these mAbs display strong binding affinity to denatured human CD26 rather than undenatured human CD26, and are capable of detecting denatured human CD26 in decalcified specimens. 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Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Nursing & Allied Health Premium</collection><collection>Advanced Technologies & Aerospace Database</collection><collection>ProQuest Advanced Technologies & Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Materials Science Collection</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>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hatano, Ryo</au><au>Yamada, Taketo</au><au>Madokoro, Hiroko</au><au>Otsuka, Haruna</au><au>Komiya, Eriko</au><au>Itoh, Takumi</au><au>Narita, Yuka</au><au>Iwata, Satoshi</au><au>Yamazaki, Hiroto</au><au>Matsuoka, Shuji</au><au>Dang, Nam H</au><au>Ohnuma, Kei</au><au>Morimoto, Chikao</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Development of novel monoclonal antibodies with specific binding affinity for denatured human CD26 in formalin-fixed paraffin-embedded and decalcified specimens</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2019-06-13</date><risdate>2019</risdate><volume>14</volume><issue>6</issue><spage>e0218330</spage><epage>e0218330</epage><pages>e0218330-e0218330</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>A 110-kDa type II transmembrane glycoprotein with dipeptidyl peptidase IV (DPPIV) activity in its extracellular region, CD26 has a multitude of biological functions and plays an important role in the regulation of inflammatory responses and tumor biology. Our work has focused on CD26 as a novel therapeutic target for various tumors and immune disorders, and we have recently developed a humanized anti-CD26 monoclonal antibody (mAb), YS110, which has promising safety profile and clinical activity in patients with malignant pleural mesothelioma. The development of an anti-human CD26 mAb that can clearly and reliably detect the denatured CD26 molecule in formalin-fixed paraffin-embedded (FFPE) tissues in the clinical setting is therefore of the utmost importance. To develop novel anti-CD26 mAbs capable of binding to denatured CD26, we immunized mice with urea-treated CD26 protein. Hybridoma supernatants were screened for specific reactivity with human CD26 by immunostaining through the use of a set of FFPE human CD26-positive or negative tumor cell lines. This screening method enables us to develop novel anti-human CD26 mAbs suitable for immunohistochemical staining of CD26 in FFPE non-tumor and tumor tissue sections with reliable clarity and intensity. Specifically, these mAbs display strong binding affinity to denatured human CD26 rather than undenatured human CD26, and are capable of detecting denatured human CD26 in decalcified specimens. These novel anti-CD26 mAbs are potentially useful for the analysis of CD26 expression in cancer patients with bony metastasis, and may help decide the appropriateness of YS110 therapy for future cancer patients.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>31194830</pmid><doi>10.1371/journal.pone.0218330</doi><tpages>e0218330</tpages><orcidid>https://orcid.org/0000-0002-3140-3596</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1932-6203 |
| ispartof | PloS one, 2019-06, Vol.14 (6), p.e0218330-e0218330 |
| issn | 1932-6203 1932-6203 |
| language | eng |
| recordid | cdi_plos_journals_2239663787 |
| source | Public Library of Science (PLoS) Journals Open Access; MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Affinity Amino acids Animals Antibodies Antibodies, Monoclonal - immunology Antibodies, Monoclonal, Humanized - genetics Antibodies, Monoclonal, Humanized - immunology Antigens Antineoplastic agents Antineoplastic Agents, Immunological - immunology Binding Biology and Life Sciences Cancer Cancer metastasis Cancer research Cancer treatment Cell growth Cell Line, Tumor Clinical trials Composition Cyclin-dependent kinases Dipeptidyl Peptidase 4 - analysis Dipeptidyl Peptidase 4 - immunology Dipeptidyl Peptidase 4 - metabolism Dipeptidyl-peptidase IV Displays (Marketing) EDTA Formaldehyde Glycoproteins Health aspects Humans Hybridomas - metabolism Immunization Immunoglobulins Immunohistochemistry Inflammation Kinases Lymphoma Medical schools Medicine Medicine and Health Sciences Mesothelioma Metastases Mice Monoclonal antibodies Paraffin Paraffin Embedding Paraffins Pathology Peptidase Prostate cancer Proteases Protein Engineering - methods Research and Analysis Methods Signal transduction Testing Therapeutic applications Thyroid cancer Tumor cell lines Tumors Urea |
| title | Development of novel monoclonal antibodies with specific binding affinity for denatured human CD26 in formalin-fixed paraffin-embedded and decalcified specimens |
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