Carcinoembryonic antigen as a specific glycoprotein ligand of rBC2LCN lectin on pancreatic ductal adenocarcinoma cells
The rBC2LCN lectin, known as a stem cell marker probe that binds to an H type 3 fucosylated trisaccharide motif, was recently revealed to also bind to pancreatic ductal adenocarcinoma (PDAC) cells. A lectin‐drug conjugate was generated by fusing rBC2LCN with a cytocidal toxin, and it showed a strong...
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| Veröffentlicht in: | Cancer science 2021-09, Vol.112 (9), p.3722-3731 |
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| creator | Furuta, Tomoaki Oda, Tatsuya Kiyoi, Kayo Yusuke, Ozawa Kimura, Sota Kurimori, Ko Miyazaki, Yoshihiro Yu, Yang Furuya, Kinji Akashi, Yoshimasa Shimomura, Osamu Tateno, Hiroaki |
| description | The rBC2LCN lectin, known as a stem cell marker probe that binds to an H type 3 fucosylated trisaccharide motif, was recently revealed to also bind to pancreatic ductal adenocarcinoma (PDAC) cells. A lectin‐drug conjugate was generated by fusing rBC2LCN with a cytocidal toxin, and it showed a strong anticancer effect in in vitro and in vivo PDAC models. However, it is unclear which molecules are carrier proteins of rBC2LCN on PDAC cells. In this study, we identified a rBC2LCN‐positive glycoprotein expressed in PDAC. Tumor lysates of PDAC patient‐derived xenografts (PDXs) were coprecipitated with rBC2LCN lectin and analyzed by liquid chromatography–mass spectrometry. A total of 343 proteins were initially identified. We used a web‐based database to select five glycoproteins and independently evaluated their expression in PDAC by immunohistochemistry (IHC). Among them, we focused on carcinoembryonic antigen 5 (CEA) as the most cancer‐specific carrier protein in PDAC, as it showed the most prominent difference in expression rate between PDAC cells (74%) and normal pancreatic duct cells (0%, P > .0001). rBC2LCN lectin and CEA colocalization in PDAC samples was confirmed by double‐staining analysis. Furthermore, rBC2LCN‐precipitated fractions were blotted with an anti‐CEA polyclonal antibody (pAb), and CEA pAb–precipitated fractions were blotted with rBC2LCN lectin. The results demonstrate that CEA is in fact a ligand of rBC2LCN lectin.
This study reports that carcinoembryonic antigen 5 (CEA) is a cancer‐specific rBC2LCN‐positive glycoprotein expressed in pancreatic ductal adenocarcinoma (PDAC). The rBC2LCN lectin, reported as a stem cell marker probe, has been detected in some cancers, and a glycan epitope of rBC2LCN, H type 3 fucosylated motif (Fucα1‐2Galβ1‐3GalNAc), could be a therapeutic target for cancers. This study showed for the first time that CEA is modified with α1‐2 fucose. |
| doi_str_mv | 10.1111/cas.15023 |
| format | Article |
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This study reports that carcinoembryonic antigen 5 (CEA) is a cancer‐specific rBC2LCN‐positive glycoprotein expressed in pancreatic ductal adenocarcinoma (PDAC). The rBC2LCN lectin, reported as a stem cell marker probe, has been detected in some cancers, and a glycan epitope of rBC2LCN, H type 3 fucosylated motif (Fucα1‐2Galβ1‐3GalNAc), could be a therapeutic target for cancers. This study showed for the first time that CEA is modified with α1‐2 fucose.</description><identifier>ISSN: 1347-9032</identifier><identifier>EISSN: 1349-7006</identifier><identifier>DOI: 10.1111/cas.15023</identifier><identifier>PMID: 34115906</identifier><language>eng</language><publisher>HOBOKEN: Wiley</publisher><subject>Adenocarcinoma ; Analysis ; Animals ; Antibodies - immunology ; Antigens ; Bioinformatics ; Cancer ; Carcinoembryonic antigen ; Carcinoembryonic Antigen - immunology ; Carcinoembryonic Antigen - metabolism ; Carcinoma, Pancreatic Ductal - metabolism ; Carcinoma, Pancreatic Ductal - pathology ; Care and treatment ; Carrier Proteins - metabolism ; CEA ; CEA (Oncology) ; Cell Line, Tumor ; Female ; glycoprotein ; Glycoproteins ; GPI-Linked Proteins - immunology ; GPI-Linked Proteins - metabolism ; Heterografts ; Humans ; Immunohistochemistry ; Immunohistochemistry - methods ; Immunoprecipitation - methods ; lectin ; Lectins ; Lectins - metabolism ; Life Sciences & Biomedicine ; Ligands ; Liquid chromatography ; Lysates ; Mass spectroscopy ; Mice ; Mice, Inbred ICR ; Mice, SCID ; Monoclonal antibodies ; Neoplasm Transplantation ; Oncology ; Original ; Pancreas ; Pancreatic cancer ; pancreatic ductal adenocarcinoma ; Pancreatic Neoplasms - metabolism ; Pancreatic Neoplasms - pathology ; Patients ; Polyclonal antibodies ; Prostate ; Proteins ; rBC2LCN ; Science & Technology ; Software ; Stem cells ; Xenografts</subject><ispartof>Cancer science, 2021-09, Vol.112 (9), p.3722-3731</ispartof><rights>2021 The Authors. published by John Wiley & Sons Australia, Ltd on behalf of Japanese Cancer Association.</rights><rights>2021 The Authors. Cancer Science published by John Wiley & Sons Australia, Ltd on behalf of Japanese Cancer Association.</rights><rights>COPYRIGHT 2021 John Wiley & Sons, Inc.</rights><rights>2021. This work is published under http://creativecommons.org/licenses/by-nc/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>10</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wos000667762200001</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c6443-ee1ff56de6b3b8f4fd8fe30fb7704d13c926b6162070627a15075a1950277d83</citedby><cites>FETCH-LOGICAL-c6443-ee1ff56de6b3b8f4fd8fe30fb7704d13c926b6162070627a15075a1950277d83</cites><orcidid>0000-0001-8843-9605 ; 0000-0001-6115-0158 ; 0000-0001-5878-4459 ; 0000-0002-1851-964X ; 0000-0003-3006-1659</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/PMC8409409/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8409409/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,865,886,1418,2115,11567,27929,27930,39263,45579,45580,46057,46481,53796,53798</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34115906$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Furuta, Tomoaki</creatorcontrib><creatorcontrib>Oda, Tatsuya</creatorcontrib><creatorcontrib>Kiyoi, Kayo</creatorcontrib><creatorcontrib>Yusuke, Ozawa</creatorcontrib><creatorcontrib>Kimura, Sota</creatorcontrib><creatorcontrib>Kurimori, Ko</creatorcontrib><creatorcontrib>Miyazaki, Yoshihiro</creatorcontrib><creatorcontrib>Yu, Yang</creatorcontrib><creatorcontrib>Furuya, Kinji</creatorcontrib><creatorcontrib>Akashi, Yoshimasa</creatorcontrib><creatorcontrib>Shimomura, Osamu</creatorcontrib><creatorcontrib>Tateno, Hiroaki</creatorcontrib><title>Carcinoembryonic antigen as a specific glycoprotein ligand of rBC2LCN lectin on pancreatic ductal adenocarcinoma cells</title><title>Cancer science</title><addtitle>CANCER SCI</addtitle><addtitle>Cancer Sci</addtitle><description>The rBC2LCN lectin, known as a stem cell marker probe that binds to an H type 3 fucosylated trisaccharide motif, was recently revealed to also bind to pancreatic ductal adenocarcinoma (PDAC) cells. A lectin‐drug conjugate was generated by fusing rBC2LCN with a cytocidal toxin, and it showed a strong anticancer effect in in vitro and in vivo PDAC models. However, it is unclear which molecules are carrier proteins of rBC2LCN on PDAC cells. In this study, we identified a rBC2LCN‐positive glycoprotein expressed in PDAC. Tumor lysates of PDAC patient‐derived xenografts (PDXs) were coprecipitated with rBC2LCN lectin and analyzed by liquid chromatography–mass spectrometry. A total of 343 proteins were initially identified. We used a web‐based database to select five glycoproteins and independently evaluated their expression in PDAC by immunohistochemistry (IHC). Among them, we focused on carcinoembryonic antigen 5 (CEA) as the most cancer‐specific carrier protein in PDAC, as it showed the most prominent difference in expression rate between PDAC cells (74%) and normal pancreatic duct cells (0%, P > .0001). rBC2LCN lectin and CEA colocalization in PDAC samples was confirmed by double‐staining analysis. Furthermore, rBC2LCN‐precipitated fractions were blotted with an anti‐CEA polyclonal antibody (pAb), and CEA pAb–precipitated fractions were blotted with rBC2LCN lectin. The results demonstrate that CEA is in fact a ligand of rBC2LCN lectin.
This study reports that carcinoembryonic antigen 5 (CEA) is a cancer‐specific rBC2LCN‐positive glycoprotein expressed in pancreatic ductal adenocarcinoma (PDAC). The rBC2LCN lectin, reported as a stem cell marker probe, has been detected in some cancers, and a glycan epitope of rBC2LCN, H type 3 fucosylated motif (Fucα1‐2Galβ1‐3GalNAc), could be a therapeutic target for cancers. This study showed for the first time that CEA is modified with α1‐2 fucose.</description><subject>Adenocarcinoma</subject><subject>Analysis</subject><subject>Animals</subject><subject>Antibodies - immunology</subject><subject>Antigens</subject><subject>Bioinformatics</subject><subject>Cancer</subject><subject>Carcinoembryonic antigen</subject><subject>Carcinoembryonic Antigen - immunology</subject><subject>Carcinoembryonic Antigen - metabolism</subject><subject>Carcinoma, Pancreatic Ductal - metabolism</subject><subject>Carcinoma, Pancreatic Ductal - pathology</subject><subject>Care and treatment</subject><subject>Carrier Proteins - metabolism</subject><subject>CEA</subject><subject>CEA (Oncology)</subject><subject>Cell Line, Tumor</subject><subject>Female</subject><subject>glycoprotein</subject><subject>Glycoproteins</subject><subject>GPI-Linked Proteins - immunology</subject><subject>GPI-Linked Proteins - metabolism</subject><subject>Heterografts</subject><subject>Humans</subject><subject>Immunohistochemistry</subject><subject>Immunohistochemistry - methods</subject><subject>Immunoprecipitation - methods</subject><subject>lectin</subject><subject>Lectins</subject><subject>Lectins - metabolism</subject><subject>Life Sciences & Biomedicine</subject><subject>Ligands</subject><subject>Liquid chromatography</subject><subject>Lysates</subject><subject>Mass spectroscopy</subject><subject>Mice</subject><subject>Mice, Inbred ICR</subject><subject>Mice, SCID</subject><subject>Monoclonal antibodies</subject><subject>Neoplasm Transplantation</subject><subject>Oncology</subject><subject>Original</subject><subject>Pancreas</subject><subject>Pancreatic cancer</subject><subject>pancreatic ductal adenocarcinoma</subject><subject>Pancreatic Neoplasms - metabolism</subject><subject>Pancreatic Neoplasms - pathology</subject><subject>Patients</subject><subject>Polyclonal antibodies</subject><subject>Prostate</subject><subject>Proteins</subject><subject>rBC2LCN</subject><subject>Science & Technology</subject><subject>Software</subject><subject>Stem cells</subject><subject>Xenografts</subject><issn>1347-9032</issn><issn>1349-7006</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>24P</sourceid><sourceid>WIN</sourceid><sourceid>HGBXW</sourceid><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqNkl2P1CAUhhujcdfVC_-AIfFGY2YWCoX2xmRs_EomeuHeE0oPI5sWRmjXzL_3zM44ukYTgQQCz3sO5-QtiqeMLhmOS2vyklW05PeKc8ZFs1CUyvu3Z7VoKC_Pikc5X1PKpWjEw-KMC8aqhsrz4qY1yfoQYezSLgZviQmT30AgJhND8hasd3i7GXY2blOcwAcy-I0JPYmOpDdtuW4_kQHshA8xkK0JNoGZUNPPdjIDMT2EaA9pRkMsDEN-XDxwZsjw5LhfFFfv3l61Hxbrz-8_tqv1wkoh-AKAOVfJHmTHu9oJ19cOOHWdUlT0jNumlJ1ksqSKylIZbIKqDGuwF0r1Nb8oXh_CbuduhN5CmJIZ9Db50aSdjsbruy_Bf9WbeKNrQRtcGODFMUCK32bIkx593ldgAsQ567IStCpprTiiz_9Ar-OcAlaHlFSNqmVZ_aI2ZgDtg4uY1-6D6pViVIlaKorU8i8Uzh5Gb2MA5_H-juDlQWBTzDmBO9XIqN57RKNH9K1HkH32e1NO5E9TIPDqAHyHLrpsPQQLJ4yit6RSsizxRBnS9f_TrZ_QGjG0cQ4TSi-PUixn9-8v63b15fD3H8dg5bE</recordid><startdate>202109</startdate><enddate>202109</enddate><creator>Furuta, Tomoaki</creator><creator>Oda, Tatsuya</creator><creator>Kiyoi, Kayo</creator><creator>Yusuke, Ozawa</creator><creator>Kimura, Sota</creator><creator>Kurimori, Ko</creator><creator>Miyazaki, Yoshihiro</creator><creator>Yu, Yang</creator><creator>Furuya, Kinji</creator><creator>Akashi, Yoshimasa</creator><creator>Shimomura, Osamu</creator><creator>Tateno, Hiroaki</creator><general>Wiley</general><general>John Wiley & Sons, Inc</general><general>John Wiley and Sons Inc</general><scope>24P</scope><scope>WIN</scope><scope>BLEPL</scope><scope>DTL</scope><scope>HGBXW</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>7X8</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-8843-9605</orcidid><orcidid>https://orcid.org/0000-0001-6115-0158</orcidid><orcidid>https://orcid.org/0000-0001-5878-4459</orcidid><orcidid>https://orcid.org/0000-0002-1851-964X</orcidid><orcidid>https://orcid.org/0000-0003-3006-1659</orcidid></search><sort><creationdate>202109</creationdate><title>Carcinoembryonic antigen as a specific glycoprotein ligand of rBC2LCN lectin on pancreatic ductal adenocarcinoma cells</title><author>Furuta, Tomoaki ; Oda, Tatsuya ; Kiyoi, Kayo ; Yusuke, Ozawa ; Kimura, Sota ; Kurimori, Ko ; Miyazaki, Yoshihiro ; Yu, Yang ; Furuya, Kinji ; Akashi, Yoshimasa ; Shimomura, Osamu ; Tateno, Hiroaki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6443-ee1ff56de6b3b8f4fd8fe30fb7704d13c926b6162070627a15075a1950277d83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>Adenocarcinoma</topic><topic>Analysis</topic><topic>Animals</topic><topic>Antibodies - 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metabolism</topic><topic>Pancreatic Neoplasms - pathology</topic><topic>Patients</topic><topic>Polyclonal antibodies</topic><topic>Prostate</topic><topic>Proteins</topic><topic>rBC2LCN</topic><topic>Science & Technology</topic><topic>Software</topic><topic>Stem cells</topic><topic>Xenografts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Furuta, Tomoaki</creatorcontrib><creatorcontrib>Oda, Tatsuya</creatorcontrib><creatorcontrib>Kiyoi, Kayo</creatorcontrib><creatorcontrib>Yusuke, Ozawa</creatorcontrib><creatorcontrib>Kimura, Sota</creatorcontrib><creatorcontrib>Kurimori, Ko</creatorcontrib><creatorcontrib>Miyazaki, Yoshihiro</creatorcontrib><creatorcontrib>Yu, Yang</creatorcontrib><creatorcontrib>Furuya, Kinji</creatorcontrib><creatorcontrib>Akashi, Yoshimasa</creatorcontrib><creatorcontrib>Shimomura, Osamu</creatorcontrib><creatorcontrib>Tateno, Hiroaki</creatorcontrib><collection>Wiley-Blackwell Open Access Titles</collection><collection>Wiley Free Content</collection><collection>Web of Science Core Collection</collection><collection>Science Citation Index Expanded</collection><collection>Web of Science - 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Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cancer science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Furuta, Tomoaki</au><au>Oda, Tatsuya</au><au>Kiyoi, Kayo</au><au>Yusuke, Ozawa</au><au>Kimura, Sota</au><au>Kurimori, Ko</au><au>Miyazaki, Yoshihiro</au><au>Yu, Yang</au><au>Furuya, Kinji</au><au>Akashi, Yoshimasa</au><au>Shimomura, Osamu</au><au>Tateno, Hiroaki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Carcinoembryonic antigen as a specific glycoprotein ligand of rBC2LCN lectin on pancreatic ductal adenocarcinoma cells</atitle><jtitle>Cancer science</jtitle><stitle>CANCER SCI</stitle><addtitle>Cancer Sci</addtitle><date>2021-09</date><risdate>2021</risdate><volume>112</volume><issue>9</issue><spage>3722</spage><epage>3731</epage><pages>3722-3731</pages><issn>1347-9032</issn><eissn>1349-7006</eissn><abstract>The rBC2LCN lectin, known as a stem cell marker probe that binds to an H type 3 fucosylated trisaccharide motif, was recently revealed to also bind to pancreatic ductal adenocarcinoma (PDAC) cells. A lectin‐drug conjugate was generated by fusing rBC2LCN with a cytocidal toxin, and it showed a strong anticancer effect in in vitro and in vivo PDAC models. However, it is unclear which molecules are carrier proteins of rBC2LCN on PDAC cells. In this study, we identified a rBC2LCN‐positive glycoprotein expressed in PDAC. Tumor lysates of PDAC patient‐derived xenografts (PDXs) were coprecipitated with rBC2LCN lectin and analyzed by liquid chromatography–mass spectrometry. A total of 343 proteins were initially identified. We used a web‐based database to select five glycoproteins and independently evaluated their expression in PDAC by immunohistochemistry (IHC). Among them, we focused on carcinoembryonic antigen 5 (CEA) as the most cancer‐specific carrier protein in PDAC, as it showed the most prominent difference in expression rate between PDAC cells (74%) and normal pancreatic duct cells (0%, P > .0001). rBC2LCN lectin and CEA colocalization in PDAC samples was confirmed by double‐staining analysis. Furthermore, rBC2LCN‐precipitated fractions were blotted with an anti‐CEA polyclonal antibody (pAb), and CEA pAb–precipitated fractions were blotted with rBC2LCN lectin. The results demonstrate that CEA is in fact a ligand of rBC2LCN lectin.
This study reports that carcinoembryonic antigen 5 (CEA) is a cancer‐specific rBC2LCN‐positive glycoprotein expressed in pancreatic ductal adenocarcinoma (PDAC). The rBC2LCN lectin, reported as a stem cell marker probe, has been detected in some cancers, and a glycan epitope of rBC2LCN, H type 3 fucosylated motif (Fucα1‐2Galβ1‐3GalNAc), could be a therapeutic target for cancers. This study showed for the first time that CEA is modified with α1‐2 fucose.</abstract><cop>HOBOKEN</cop><pub>Wiley</pub><pmid>34115906</pmid><doi>10.1111/cas.15023</doi><tpages>10</tpages><orcidid>https://orcid.org/0000-0001-8843-9605</orcidid><orcidid>https://orcid.org/0000-0001-6115-0158</orcidid><orcidid>https://orcid.org/0000-0001-5878-4459</orcidid><orcidid>https://orcid.org/0000-0002-1851-964X</orcidid><orcidid>https://orcid.org/0000-0003-3006-1659</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1347-9032 |
| ispartof | Cancer science, 2021-09, Vol.112 (9), p.3722-3731 |
| issn | 1347-9032 1349-7006 |
| language | eng |
| recordid | cdi_crossref_primary_10_1111_cas_15023 |
| source | MEDLINE; DOAJ Directory of Open Access Journals; Wiley-Blackwell Open Access Titles; Web of Science - Science Citation Index Expanded - 2021<img src="https://exlibris-pub.s3.amazonaws.com/fromwos-v2.jpg" />; Wiley Online Library All Journals; PubMed Central |
| subjects | Adenocarcinoma Analysis Animals Antibodies - immunology Antigens Bioinformatics Cancer Carcinoembryonic antigen Carcinoembryonic Antigen - immunology Carcinoembryonic Antigen - metabolism Carcinoma, Pancreatic Ductal - metabolism Carcinoma, Pancreatic Ductal - pathology Care and treatment Carrier Proteins - metabolism CEA CEA (Oncology) Cell Line, Tumor Female glycoprotein Glycoproteins GPI-Linked Proteins - immunology GPI-Linked Proteins - metabolism Heterografts Humans Immunohistochemistry Immunohistochemistry - methods Immunoprecipitation - methods lectin Lectins Lectins - metabolism Life Sciences & Biomedicine Ligands Liquid chromatography Lysates Mass spectroscopy Mice Mice, Inbred ICR Mice, SCID Monoclonal antibodies Neoplasm Transplantation Oncology Original Pancreas Pancreatic cancer pancreatic ductal adenocarcinoma Pancreatic Neoplasms - metabolism Pancreatic Neoplasms - pathology Patients Polyclonal antibodies Prostate Proteins rBC2LCN Science & Technology Software Stem cells Xenografts |
| title | Carcinoembryonic antigen as a specific glycoprotein ligand of rBC2LCN lectin on pancreatic ductal adenocarcinoma cells |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-14T06%3A14%3A57IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Carcinoembryonic%20antigen%20as%20a%20specific%20glycoprotein%20ligand%20of%20rBC2LCN%20lectin%20on%20pancreatic%20ductal%20adenocarcinoma%20cells&rft.jtitle=Cancer%20science&rft.au=Furuta,%20Tomoaki&rft.date=2021-09&rft.volume=112&rft.issue=9&rft.spage=3722&rft.epage=3731&rft.pages=3722-3731&rft.issn=1347-9032&rft.eissn=1349-7006&rft_id=info:doi/10.1111/cas.15023&rft_dat=%3Cgale_cross%3EA710748670%3C/gale_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2567978625&rft_id=info:pmid/34115906&rft_galeid=A710748670&rfr_iscdi=true |