Production and characterization of monoclonal antibodies specific to lactotriaosylceramide
We have established hybridoma cell lines producing monoclonal antibodies (mAbs) directed to N-acetylglucosaminylβ1-3galactose (GlcNAcβ1-3Gal) residue by immunizing BALB/c mice with lactotriaosylceramide (Lc₃Cer). These obtained hybridoma cells, specific to Lc₃Cer, were dual immunoglobulin (Ig)-produ...
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| Veröffentlicht in: | Glycobiology (Oxford) 2010-12, Vol.20 (12), p.1631-1642 |
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| creator | Nozaki, Hirofumi Yanagida, Mayumi Koide, Ken-ichi Shiotani, Kazusa Kinoshita, Mikio Kobayashi, Yoshiyasu Watarai, Shinobu Nakamura, Kazuo Suzuki, Akemi Ariga, Toshio Kushi, Yasunori |
| description | We have established hybridoma cell lines producing monoclonal antibodies (mAbs) directed to N-acetylglucosaminylβ1-3galactose (GlcNAcβ1-3Gal) residue by immunizing BALB/c mice with lactotriaosylceramide (Lc₃Cer). These obtained hybridoma cells, specific to Lc₃Cer, were dual immunoglobulin (Ig)-producing cells which secreted both IgM and IgG molecules as antibodies. The established mAbs are able to react with not only Lc₃Cer but also GlcNAcβ1-3-terminal glycosphingolipids (GSLs) despite branching or lactosamine chain lengths and human transferrin with terminal GlcNAc residues. Comparison of the variable regions of the cloned IgM and IgG by reversed transcription-polymerase chain reaction analysis confirmed that the variable regions determine the specificity, the other amino acids are conserved, and these mAbs are encoded by J558 and Vκ-21family genes. Furthermore, we have analyzed the expression of GSLs with GlcNAcβ1-3 epitope in acute leukemia cell lines and mouse fetal tissues using these mAbs, in which antigens were distributed comparatively. These mAbs are useful for studying the precise distribution of GlcNAcβ1-3Gal-terminating GSL expression in tissues as well as for detecting GSLs carrying terminal GlcNAcβ1-3Gal carbohydrate structure. |
| doi_str_mv | 10.1093/glycob/cwq117 |
| format | Article |
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These obtained hybridoma cells, specific to Lc₃Cer, were dual immunoglobulin (Ig)-producing cells which secreted both IgM and IgG molecules as antibodies. The established mAbs are able to react with not only Lc₃Cer but also GlcNAcβ1-3-terminal glycosphingolipids (GSLs) despite branching or lactosamine chain lengths and human transferrin with terminal GlcNAc residues. Comparison of the variable regions of the cloned IgM and IgG by reversed transcription-polymerase chain reaction analysis confirmed that the variable regions determine the specificity, the other amino acids are conserved, and these mAbs are encoded by J558 and Vκ-21family genes. Furthermore, we have analyzed the expression of GSLs with GlcNAcβ1-3 epitope in acute leukemia cell lines and mouse fetal tissues using these mAbs, in which antigens were distributed comparatively. These mAbs are useful for studying the precise distribution of GlcNAcβ1-3Gal-terminating GSL expression in tissues as well as for detecting GSLs carrying terminal GlcNAcβ1-3Gal carbohydrate structure.</description><identifier>ISSN: 0959-6658</identifier><identifier>EISSN: 1460-2423</identifier><identifier>DOI: 10.1093/glycob/cwq117</identifier><identifier>PMID: 20693232</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>amino-CTH ; Animals ; Antibodies, Monoclonal, Murine-Derived - biosynthesis ; Antibodies, Monoclonal, Murine-Derived - genetics ; Antibodies, Monoclonal, Murine-Derived - immunology ; Antibody Specificity - genetics ; Antibody Specificity - immunology ; characteristic amino acid sequences ; Female ; HL-60 Cells ; Humans ; hybridoma cells ; IgM subclass ; Immunoglobulin G - biosynthesis ; Immunoglobulin G - genetics ; Immunoglobulin G - immunology ; Immunoglobulin M - biosynthesis ; Immunoglobulin M - genetics ; Immunoglobulin M - immunology ; Immunoglobulin Variable Region - biosynthesis ; Immunoglobulin Variable Region - genetics ; Immunoglobulin Variable Region - immunology ; K562 Cells ; Lactosylceramides - biosynthesis ; Lactosylceramides - genetics ; Lactosylceramides - immunology ; lactotriaosylceramide ; Mice ; Mice, Inbred BALB C ; monoclonal antibodies ; nLc5Cer ; transferrin ; U937 Cells ; variable regions</subject><ispartof>Glycobiology (Oxford), 2010-12, Vol.20 (12), p.1631-1642</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c393t-78404a82e96c4d69f2f42f0a6a125fa58a23203abba8cb8fb8a3bd468887bfaa3</citedby><cites>FETCH-LOGICAL-c393t-78404a82e96c4d69f2f42f0a6a125fa58a23203abba8cb8fb8a3bd468887bfaa3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20693232$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nozaki, Hirofumi</creatorcontrib><creatorcontrib>Yanagida, Mayumi</creatorcontrib><creatorcontrib>Koide, Ken-ichi</creatorcontrib><creatorcontrib>Shiotani, Kazusa</creatorcontrib><creatorcontrib>Kinoshita, Mikio</creatorcontrib><creatorcontrib>Kobayashi, Yoshiyasu</creatorcontrib><creatorcontrib>Watarai, Shinobu</creatorcontrib><creatorcontrib>Nakamura, Kazuo</creatorcontrib><creatorcontrib>Suzuki, Akemi</creatorcontrib><creatorcontrib>Ariga, Toshio</creatorcontrib><creatorcontrib>Kushi, Yasunori</creatorcontrib><title>Production and characterization of monoclonal antibodies specific to lactotriaosylceramide</title><title>Glycobiology (Oxford)</title><addtitle>Glycobiology</addtitle><description>We have established hybridoma cell lines producing monoclonal antibodies (mAbs) directed to N-acetylglucosaminylβ1-3galactose (GlcNAcβ1-3Gal) residue by immunizing BALB/c mice with lactotriaosylceramide (Lc₃Cer). These obtained hybridoma cells, specific to Lc₃Cer, were dual immunoglobulin (Ig)-producing cells which secreted both IgM and IgG molecules as antibodies. The established mAbs are able to react with not only Lc₃Cer but also GlcNAcβ1-3-terminal glycosphingolipids (GSLs) despite branching or lactosamine chain lengths and human transferrin with terminal GlcNAc residues. Comparison of the variable regions of the cloned IgM and IgG by reversed transcription-polymerase chain reaction analysis confirmed that the variable regions determine the specificity, the other amino acids are conserved, and these mAbs are encoded by J558 and Vκ-21family genes. Furthermore, we have analyzed the expression of GSLs with GlcNAcβ1-3 epitope in acute leukemia cell lines and mouse fetal tissues using these mAbs, in which antigens were distributed comparatively. These mAbs are useful for studying the precise distribution of GlcNAcβ1-3Gal-terminating GSL expression in tissues as well as for detecting GSLs carrying terminal GlcNAcβ1-3Gal carbohydrate structure.</description><subject>amino-CTH</subject><subject>Animals</subject><subject>Antibodies, Monoclonal, Murine-Derived - biosynthesis</subject><subject>Antibodies, Monoclonal, Murine-Derived - genetics</subject><subject>Antibodies, Monoclonal, Murine-Derived - immunology</subject><subject>Antibody Specificity - genetics</subject><subject>Antibody Specificity - immunology</subject><subject>characteristic amino acid sequences</subject><subject>Female</subject><subject>HL-60 Cells</subject><subject>Humans</subject><subject>hybridoma cells</subject><subject>IgM subclass</subject><subject>Immunoglobulin G - biosynthesis</subject><subject>Immunoglobulin G - genetics</subject><subject>Immunoglobulin G - immunology</subject><subject>Immunoglobulin M - biosynthesis</subject><subject>Immunoglobulin M - genetics</subject><subject>Immunoglobulin M - immunology</subject><subject>Immunoglobulin Variable Region - biosynthesis</subject><subject>Immunoglobulin Variable Region - genetics</subject><subject>Immunoglobulin Variable Region - immunology</subject><subject>K562 Cells</subject><subject>Lactosylceramides - biosynthesis</subject><subject>Lactosylceramides - genetics</subject><subject>Lactosylceramides - immunology</subject><subject>lactotriaosylceramide</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>monoclonal antibodies</subject><subject>nLc5Cer</subject><subject>transferrin</subject><subject>U937 Cells</subject><subject>variable regions</subject><issn>0959-6658</issn><issn>1460-2423</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkE1P3DAQhq2qFWwXjr2W3Dil-CuOfawQsK1QqbQFIS7W2LGpSxLv2lnB8usJhMJppJnnfTV6EPpC8DeCFTu6bbc2miN7vyak_oBmhAtcUk7ZRzTDqlKlEJXcRZ9z_ocxEURWO2iXYqEYZXSGbn6n2GzsEGJfQN8U9i8ksINL4RFeltEXXeyjbWMP7YgMwcQmuFzklbPBB1sMsWjHSBxSgJi3rXUJutC4PfTJQ5vd_uuco8vTkz_Hi_L84uzH8ffz0jLFhrKWHHOQ1ClheSOUp55Tj0EAoZWHSsL4KGZgDEhrpDcSmGm4kFLWxgOwOTqcelcprjcuD7oL2bq2hd7FTda1oKIWUvGRLCfSpphzcl6vUuggbTXB-tmmnmzqyebIf31t3pjONW_0f33vhSEP7uHtDulOi5rVlV5c3-irn-yULK6X-tfIH0y8h6jhNoWsL5cUE4aJwjXnnD0BWIWNng</recordid><startdate>20101201</startdate><enddate>20101201</enddate><creator>Nozaki, Hirofumi</creator><creator>Yanagida, Mayumi</creator><creator>Koide, Ken-ichi</creator><creator>Shiotani, Kazusa</creator><creator>Kinoshita, Mikio</creator><creator>Kobayashi, Yoshiyasu</creator><creator>Watarai, Shinobu</creator><creator>Nakamura, Kazuo</creator><creator>Suzuki, Akemi</creator><creator>Ariga, Toshio</creator><creator>Kushi, Yasunori</creator><general>Oxford University Press</general><scope>FBQ</scope><scope>BSCLL</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>7X8</scope></search><sort><creationdate>20101201</creationdate><title>Production and characterization of monoclonal antibodies specific to lactotriaosylceramide</title><author>Nozaki, Hirofumi ; Yanagida, Mayumi ; Koide, Ken-ichi ; Shiotani, Kazusa ; Kinoshita, Mikio ; Kobayashi, Yoshiyasu ; Watarai, Shinobu ; Nakamura, Kazuo ; Suzuki, Akemi ; Ariga, Toshio ; Kushi, Yasunori</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c393t-78404a82e96c4d69f2f42f0a6a125fa58a23203abba8cb8fb8a3bd468887bfaa3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>amino-CTH</topic><topic>Animals</topic><topic>Antibodies, Monoclonal, Murine-Derived - biosynthesis</topic><topic>Antibodies, Monoclonal, Murine-Derived - genetics</topic><topic>Antibodies, Monoclonal, Murine-Derived - immunology</topic><topic>Antibody Specificity - genetics</topic><topic>Antibody Specificity - immunology</topic><topic>characteristic amino acid sequences</topic><topic>Female</topic><topic>HL-60 Cells</topic><topic>Humans</topic><topic>hybridoma cells</topic><topic>IgM subclass</topic><topic>Immunoglobulin G - biosynthesis</topic><topic>Immunoglobulin G - genetics</topic><topic>Immunoglobulin G - immunology</topic><topic>Immunoglobulin M - biosynthesis</topic><topic>Immunoglobulin M - genetics</topic><topic>Immunoglobulin M - immunology</topic><topic>Immunoglobulin Variable Region - biosynthesis</topic><topic>Immunoglobulin Variable Region - genetics</topic><topic>Immunoglobulin Variable Region - immunology</topic><topic>K562 Cells</topic><topic>Lactosylceramides - biosynthesis</topic><topic>Lactosylceramides - genetics</topic><topic>Lactosylceramides - immunology</topic><topic>lactotriaosylceramide</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>monoclonal antibodies</topic><topic>nLc5Cer</topic><topic>transferrin</topic><topic>U937 Cells</topic><topic>variable regions</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nozaki, Hirofumi</creatorcontrib><creatorcontrib>Yanagida, Mayumi</creatorcontrib><creatorcontrib>Koide, Ken-ichi</creatorcontrib><creatorcontrib>Shiotani, Kazusa</creatorcontrib><creatorcontrib>Kinoshita, Mikio</creatorcontrib><creatorcontrib>Kobayashi, Yoshiyasu</creatorcontrib><creatorcontrib>Watarai, Shinobu</creatorcontrib><creatorcontrib>Nakamura, Kazuo</creatorcontrib><creatorcontrib>Suzuki, Akemi</creatorcontrib><creatorcontrib>Ariga, Toshio</creatorcontrib><creatorcontrib>Kushi, Yasunori</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Glycobiology (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nozaki, Hirofumi</au><au>Yanagida, Mayumi</au><au>Koide, Ken-ichi</au><au>Shiotani, Kazusa</au><au>Kinoshita, Mikio</au><au>Kobayashi, Yoshiyasu</au><au>Watarai, Shinobu</au><au>Nakamura, Kazuo</au><au>Suzuki, Akemi</au><au>Ariga, Toshio</au><au>Kushi, Yasunori</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Production and characterization of monoclonal antibodies specific to lactotriaosylceramide</atitle><jtitle>Glycobiology (Oxford)</jtitle><addtitle>Glycobiology</addtitle><date>2010-12-01</date><risdate>2010</risdate><volume>20</volume><issue>12</issue><spage>1631</spage><epage>1642</epage><pages>1631-1642</pages><issn>0959-6658</issn><eissn>1460-2423</eissn><abstract>We have established hybridoma cell lines producing monoclonal antibodies (mAbs) directed to N-acetylglucosaminylβ1-3galactose (GlcNAcβ1-3Gal) residue by immunizing BALB/c mice with lactotriaosylceramide (Lc₃Cer). These obtained hybridoma cells, specific to Lc₃Cer, were dual immunoglobulin (Ig)-producing cells which secreted both IgM and IgG molecules as antibodies. The established mAbs are able to react with not only Lc₃Cer but also GlcNAcβ1-3-terminal glycosphingolipids (GSLs) despite branching or lactosamine chain lengths and human transferrin with terminal GlcNAc residues. Comparison of the variable regions of the cloned IgM and IgG by reversed transcription-polymerase chain reaction analysis confirmed that the variable regions determine the specificity, the other amino acids are conserved, and these mAbs are encoded by J558 and Vκ-21family genes. Furthermore, we have analyzed the expression of GSLs with GlcNAcβ1-3 epitope in acute leukemia cell lines and mouse fetal tissues using these mAbs, in which antigens were distributed comparatively. These mAbs are useful for studying the precise distribution of GlcNAcβ1-3Gal-terminating GSL expression in tissues as well as for detecting GSLs carrying terminal GlcNAcβ1-3Gal carbohydrate structure.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>20693232</pmid><doi>10.1093/glycob/cwq117</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | amino-CTH Animals Antibodies, Monoclonal, Murine-Derived - biosynthesis Antibodies, Monoclonal, Murine-Derived - genetics Antibodies, Monoclonal, Murine-Derived - immunology Antibody Specificity - genetics Antibody Specificity - immunology characteristic amino acid sequences Female HL-60 Cells Humans hybridoma cells IgM subclass Immunoglobulin G - biosynthesis Immunoglobulin G - genetics Immunoglobulin G - immunology Immunoglobulin M - biosynthesis Immunoglobulin M - genetics Immunoglobulin M - immunology Immunoglobulin Variable Region - biosynthesis Immunoglobulin Variable Region - genetics Immunoglobulin Variable Region - immunology K562 Cells Lactosylceramides - biosynthesis Lactosylceramides - genetics Lactosylceramides - immunology lactotriaosylceramide Mice Mice, Inbred BALB C monoclonal antibodies nLc5Cer transferrin U937 Cells variable regions |
| title | Production and characterization of monoclonal antibodies specific to lactotriaosylceramide |
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