Glycomic Analyses of Glycoproteins in Bile and Serum during Rat Hepatocarcinogenesis
Fucosylated alpha-fetoprotein (AFP) is a specific tumor marker for hepatocellular carcinomas (HCC). However, the mechanisms underlying the increase in fucosylated AFP in serum of patients with HCC are largely unknown. Recently, we reported that fucosylation is a possible signal for the secretion of...
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| Veröffentlicht in: | Journal of proteome research 2010-10, Vol.9 (10), p.4888-4896 |
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| creator | Nakagawa, Tsutomu Takeishi, Shunsaku Kameyama, Akihiko Yagi, Hirokazu Yoshioka, Tomoko Moriwaki, Kenta Masuda, Tomomi Matsumoto, Hitoshi Kato, Koichi Narimatsu, Hisashi Taniguchi, Naoyuki Miyoshi, Eiji |
| description | Fucosylated alpha-fetoprotein (AFP) is a specific tumor marker for hepatocellular carcinomas (HCC). However, the mechanisms underlying the increase in fucosylated AFP in serum of patients with HCC are largely unknown. Recently, we reported that fucosylation is a possible signal for the secretion of glycoproteins into bile in the liver. This finding might lead to the selective secretion of fucosylated AFP into bile and the selective secretion might be disrupted in hepatocarcinogenesis. In this study, therefore, we analyzed the oligosaccharide structures of glycoproteins in bile and serum of LEC rats, which are a rat model of spontaneous hepatocarcinogenesis. Lectin microarraying showed enhanced binding of 13 lectins to bile, compared with in serum from normal LEC rats, and the binding of these lectins to serum of LEC rats bearing HCC was higher than in normal rats. Structural analyses involving HPLC and mass spectrometry showed that the fucosylation levels of serum glycoproteins were not increased in CH rats but were in HCC rats, although the fucosylation levels of biliary glycoproteins were increased in both CH and HCC rats. These results suggested that the sorting machinery through fucosylation might be disrupted in the liver with HCC. |
| doi_str_mv | 10.1021/pr100414r |
| format | Article |
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However, the mechanisms underlying the increase in fucosylated AFP in serum of patients with HCC are largely unknown. Recently, we reported that fucosylation is a possible signal for the secretion of glycoproteins into bile in the liver. This finding might lead to the selective secretion of fucosylated AFP into bile and the selective secretion might be disrupted in hepatocarcinogenesis. In this study, therefore, we analyzed the oligosaccharide structures of glycoproteins in bile and serum of LEC rats, which are a rat model of spontaneous hepatocarcinogenesis. Lectin microarraying showed enhanced binding of 13 lectins to bile, compared with in serum from normal LEC rats, and the binding of these lectins to serum of LEC rats bearing HCC was higher than in normal rats. Structural analyses involving HPLC and mass spectrometry showed that the fucosylation levels of serum glycoproteins were not increased in CH rats but were in HCC rats, although the fucosylation levels of biliary glycoproteins were increased in both CH and HCC rats. These results suggested that the sorting machinery through fucosylation might be disrupted in the liver with HCC.</description><identifier>ISSN: 1535-3893</identifier><identifier>EISSN: 1535-3907</identifier><identifier>DOI: 10.1021/pr100414r</identifier><identifier>PMID: 20731380</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Animals ; Bile - metabolism ; Carcinoma, Hepatocellular - metabolism ; Carcinoma, Hepatocellular - pathology ; Chromatography, High Pressure Liquid ; Fucose - analysis ; Glycomics - methods ; Glycoproteins - analysis ; Glycoproteins - blood ; Glycoproteins - metabolism ; Lectins - metabolism ; Liver Neoplasms - metabolism ; Liver Neoplasms - pathology ; Mass Spectrometry ; Oligosaccharides - analysis ; Polysaccharides - analysis ; Polysaccharides - metabolism ; Protein Array Analysis - methods ; Protein Binding ; Proteomics - methods ; Rats ; Rats, Inbred LEC</subject><ispartof>Journal of proteome research, 2010-10, Vol.9 (10), p.4888-4896</ispartof><rights>Copyright © 2010 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a314t-59e6c5d270471accf8a1f9c0240ebf95e4e418a9e9f43b5ea65d61352de715693</citedby><cites>FETCH-LOGICAL-a314t-59e6c5d270471accf8a1f9c0240ebf95e4e418a9e9f43b5ea65d61352de715693</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/pr100414r$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/pr100414r$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,27053,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20731380$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nakagawa, Tsutomu</creatorcontrib><creatorcontrib>Takeishi, Shunsaku</creatorcontrib><creatorcontrib>Kameyama, Akihiko</creatorcontrib><creatorcontrib>Yagi, Hirokazu</creatorcontrib><creatorcontrib>Yoshioka, Tomoko</creatorcontrib><creatorcontrib>Moriwaki, Kenta</creatorcontrib><creatorcontrib>Masuda, Tomomi</creatorcontrib><creatorcontrib>Matsumoto, Hitoshi</creatorcontrib><creatorcontrib>Kato, Koichi</creatorcontrib><creatorcontrib>Narimatsu, Hisashi</creatorcontrib><creatorcontrib>Taniguchi, Naoyuki</creatorcontrib><creatorcontrib>Miyoshi, Eiji</creatorcontrib><title>Glycomic Analyses of Glycoproteins in Bile and Serum during Rat Hepatocarcinogenesis</title><title>Journal of proteome research</title><addtitle>J. Proteome Res</addtitle><description>Fucosylated alpha-fetoprotein (AFP) is a specific tumor marker for hepatocellular carcinomas (HCC). However, the mechanisms underlying the increase in fucosylated AFP in serum of patients with HCC are largely unknown. Recently, we reported that fucosylation is a possible signal for the secretion of glycoproteins into bile in the liver. This finding might lead to the selective secretion of fucosylated AFP into bile and the selective secretion might be disrupted in hepatocarcinogenesis. In this study, therefore, we analyzed the oligosaccharide structures of glycoproteins in bile and serum of LEC rats, which are a rat model of spontaneous hepatocarcinogenesis. Lectin microarraying showed enhanced binding of 13 lectins to bile, compared with in serum from normal LEC rats, and the binding of these lectins to serum of LEC rats bearing HCC was higher than in normal rats. Structural analyses involving HPLC and mass spectrometry showed that the fucosylation levels of serum glycoproteins were not increased in CH rats but were in HCC rats, although the fucosylation levels of biliary glycoproteins were increased in both CH and HCC rats. These results suggested that the sorting machinery through fucosylation might be disrupted in the liver with HCC.</description><subject>Animals</subject><subject>Bile - metabolism</subject><subject>Carcinoma, Hepatocellular - metabolism</subject><subject>Carcinoma, Hepatocellular - pathology</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Fucose - analysis</subject><subject>Glycomics - methods</subject><subject>Glycoproteins - analysis</subject><subject>Glycoproteins - blood</subject><subject>Glycoproteins - metabolism</subject><subject>Lectins - metabolism</subject><subject>Liver Neoplasms - metabolism</subject><subject>Liver Neoplasms - pathology</subject><subject>Mass Spectrometry</subject><subject>Oligosaccharides - analysis</subject><subject>Polysaccharides - analysis</subject><subject>Polysaccharides - metabolism</subject><subject>Protein Array Analysis - methods</subject><subject>Protein Binding</subject><subject>Proteomics - methods</subject><subject>Rats</subject><subject>Rats, Inbred LEC</subject><issn>1535-3893</issn><issn>1535-3907</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkM9LwzAUgIMobk4P_gOSi4iHatIkTXPUoZswEHSeS5a-jow2qUl72H9vdT9Ont7j8fHx-BC6puSBkpQ-toESwikPJ2hMBRMJU0SeHvZcsRG6iHFDCBWSsHM0SolklOVkjJazemt8Yw1-crreRojYV_jv2AbfgXURW4efbQ1YuxJ_QugbXPbBujX-0B2eQ6s7b3Qw1vk1OIg2XqKzStcRrvZzgr5eX5bTebJ4n71NnxaJZpR3iVCQGVGmknBJtTFVrmmlDEk5gVWlBHDgNNcKVMXZSoDORJlRJtISJBWZYhN0t_MOr373ELuisdFAXWsHvo-FFFmWSan4QN7vSBN8jAGqog220WFbUFL8NiyODQf2Zm_tVw2UR_IQbQBud4A2sdj4Pgzl4j-iH6A5eGM</recordid><startdate>20101001</startdate><enddate>20101001</enddate><creator>Nakagawa, Tsutomu</creator><creator>Takeishi, Shunsaku</creator><creator>Kameyama, Akihiko</creator><creator>Yagi, Hirokazu</creator><creator>Yoshioka, Tomoko</creator><creator>Moriwaki, Kenta</creator><creator>Masuda, Tomomi</creator><creator>Matsumoto, Hitoshi</creator><creator>Kato, Koichi</creator><creator>Narimatsu, Hisashi</creator><creator>Taniguchi, Naoyuki</creator><creator>Miyoshi, Eiji</creator><general>American Chemical Society</general><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>20101001</creationdate><title>Glycomic Analyses of Glycoproteins in Bile and Serum during Rat Hepatocarcinogenesis</title><author>Nakagawa, Tsutomu ; Takeishi, Shunsaku ; Kameyama, Akihiko ; Yagi, Hirokazu ; Yoshioka, Tomoko ; Moriwaki, Kenta ; Masuda, Tomomi ; Matsumoto, Hitoshi ; Kato, Koichi ; Narimatsu, Hisashi ; Taniguchi, Naoyuki ; Miyoshi, Eiji</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a314t-59e6c5d270471accf8a1f9c0240ebf95e4e418a9e9f43b5ea65d61352de715693</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Animals</topic><topic>Bile - metabolism</topic><topic>Carcinoma, Hepatocellular - metabolism</topic><topic>Carcinoma, Hepatocellular - pathology</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Fucose - analysis</topic><topic>Glycomics - methods</topic><topic>Glycoproteins - analysis</topic><topic>Glycoproteins - blood</topic><topic>Glycoproteins - metabolism</topic><topic>Lectins - metabolism</topic><topic>Liver Neoplasms - metabolism</topic><topic>Liver Neoplasms - pathology</topic><topic>Mass Spectrometry</topic><topic>Oligosaccharides - analysis</topic><topic>Polysaccharides - analysis</topic><topic>Polysaccharides - metabolism</topic><topic>Protein Array Analysis - methods</topic><topic>Protein Binding</topic><topic>Proteomics - methods</topic><topic>Rats</topic><topic>Rats, Inbred LEC</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nakagawa, Tsutomu</creatorcontrib><creatorcontrib>Takeishi, Shunsaku</creatorcontrib><creatorcontrib>Kameyama, Akihiko</creatorcontrib><creatorcontrib>Yagi, Hirokazu</creatorcontrib><creatorcontrib>Yoshioka, Tomoko</creatorcontrib><creatorcontrib>Moriwaki, Kenta</creatorcontrib><creatorcontrib>Masuda, Tomomi</creatorcontrib><creatorcontrib>Matsumoto, Hitoshi</creatorcontrib><creatorcontrib>Kato, Koichi</creatorcontrib><creatorcontrib>Narimatsu, Hisashi</creatorcontrib><creatorcontrib>Taniguchi, Naoyuki</creatorcontrib><creatorcontrib>Miyoshi, Eiji</creatorcontrib><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>Journal of proteome research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nakagawa, Tsutomu</au><au>Takeishi, Shunsaku</au><au>Kameyama, Akihiko</au><au>Yagi, Hirokazu</au><au>Yoshioka, Tomoko</au><au>Moriwaki, Kenta</au><au>Masuda, Tomomi</au><au>Matsumoto, Hitoshi</au><au>Kato, Koichi</au><au>Narimatsu, Hisashi</au><au>Taniguchi, Naoyuki</au><au>Miyoshi, Eiji</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Glycomic Analyses of Glycoproteins in Bile and Serum during Rat Hepatocarcinogenesis</atitle><jtitle>Journal of proteome research</jtitle><addtitle>J. Proteome Res</addtitle><date>2010-10-01</date><risdate>2010</risdate><volume>9</volume><issue>10</issue><spage>4888</spage><epage>4896</epage><pages>4888-4896</pages><issn>1535-3893</issn><eissn>1535-3907</eissn><abstract>Fucosylated alpha-fetoprotein (AFP) is a specific tumor marker for hepatocellular carcinomas (HCC). However, the mechanisms underlying the increase in fucosylated AFP in serum of patients with HCC are largely unknown. Recently, we reported that fucosylation is a possible signal for the secretion of glycoproteins into bile in the liver. This finding might lead to the selective secretion of fucosylated AFP into bile and the selective secretion might be disrupted in hepatocarcinogenesis. In this study, therefore, we analyzed the oligosaccharide structures of glycoproteins in bile and serum of LEC rats, which are a rat model of spontaneous hepatocarcinogenesis. Lectin microarraying showed enhanced binding of 13 lectins to bile, compared with in serum from normal LEC rats, and the binding of these lectins to serum of LEC rats bearing HCC was higher than in normal rats. Structural analyses involving HPLC and mass spectrometry showed that the fucosylation levels of serum glycoproteins were not increased in CH rats but were in HCC rats, although the fucosylation levels of biliary glycoproteins were increased in both CH and HCC rats. These results suggested that the sorting machinery through fucosylation might be disrupted in the liver with HCC.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>20731380</pmid><doi>10.1021/pr100414r</doi><tpages>9</tpages></addata></record> |
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| subjects | Animals Bile - metabolism Carcinoma, Hepatocellular - metabolism Carcinoma, Hepatocellular - pathology Chromatography, High Pressure Liquid Fucose - analysis Glycomics - methods Glycoproteins - analysis Glycoproteins - blood Glycoproteins - metabolism Lectins - metabolism Liver Neoplasms - metabolism Liver Neoplasms - pathology Mass Spectrometry Oligosaccharides - analysis Polysaccharides - analysis Polysaccharides - metabolism Protein Array Analysis - methods Protein Binding Proteomics - methods Rats Rats, Inbred LEC |
| title | Glycomic Analyses of Glycoproteins in Bile and Serum during Rat Hepatocarcinogenesis |
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