The changes in glycosylation after partial hepatectomy enhance collagen binding of vitronectin in plasma
Vitronectin is a multifunctional glycoprotein present in the extracellular matrix and plasma. Changes in rat vitronectin were studied during liver regeneration after partial hepatectomy. Carbohydrate concentrations of vitronectin decreased to 2/3 of sham-operated rats at 24 h after partial hepatecto...
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| Veröffentlicht in: | Glycobiology (Oxford) 2000-09, Vol.10 (9), p.865-874 |
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| creator | Uchibori-Iwaki, H Yoneda, A Oda-Tamai, S Kato, S Akamatsu, N Otsuka, M Murase, K Kojima, K Suzuki, R Maeya, Y Tanabe, M Ogawa, H |
| description | Vitronectin is a multifunctional glycoprotein present in the extracellular matrix and plasma. Changes in rat vitronectin were studied during liver regeneration after partial hepatectomy. Carbohydrate concentrations of vitronectin decreased to 2/3 of sham-operated rats at 24 h after partial hepatectomy. Carbohydrate composition and lectin reactivity indicated that N-glycosylation and sialylation of vitronectin changed markedly after partial hepatectomy, while amino acid composition did not change significantly. We previously showed that deN-glycosylation of vitronectin in vitro affects collagen binding among various ligands (Yoneda et al., Biochemistry (1998) 37, 6351-6360). Vitronectins from partially hepatectomized rats at 24 h were found to exhibit markedly enhanced binding to type I collagen. The effect of sialylation on collagen binding was further examined using enzymatically deglycosylated vitronectin of nonoperated rats. Collagen binding increased by 1.2 times after deN-glycosylation of vitronectin, while it increased more than 2.9 times after desialylation. Various glycosyltransferases in liver are known to change after partial hepatectomy, including the attenuation of N-oligosaccharide transferase. The findings therefore suggest that the collagen binding of vitronectin is modulated by the alteration of peptide glycosylation caused by postoperative physiological changes of glycosyltransferases and that the change may contribute to tissue remodeling processes. |
| doi_str_mv | 10.1093/glycob/10.9.865 |
| format | Article |
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Changes in rat vitronectin were studied during liver regeneration after partial hepatectomy. Carbohydrate concentrations of vitronectin decreased to 2/3 of sham-operated rats at 24 h after partial hepatectomy. Carbohydrate composition and lectin reactivity indicated that N-glycosylation and sialylation of vitronectin changed markedly after partial hepatectomy, while amino acid composition did not change significantly. We previously showed that deN-glycosylation of vitronectin in vitro affects collagen binding among various ligands (Yoneda et al., Biochemistry (1998) 37, 6351-6360). Vitronectins from partially hepatectomized rats at 24 h were found to exhibit markedly enhanced binding to type I collagen. The effect of sialylation on collagen binding was further examined using enzymatically deglycosylated vitronectin of nonoperated rats. Collagen binding increased by 1.2 times after deN-glycosylation of vitronectin, while it increased more than 2.9 times after desialylation. Various glycosyltransferases in liver are known to change after partial hepatectomy, including the attenuation of N-oligosaccharide transferase. The findings therefore suggest that the collagen binding of vitronectin is modulated by the alteration of peptide glycosylation caused by postoperative physiological changes of glycosyltransferases and that the change may contribute to tissue remodeling processes.</description><identifier>ISSN: 0959-6658</identifier><identifier>EISSN: 1460-2423</identifier><identifier>DOI: 10.1093/glycob/10.9.865</identifier><identifier>PMID: 10988248</identifier><language>eng</language><publisher>England: Oxford Publishing Limited (England)</publisher><subject>Amino Acids - analysis ; Animals ; Collagen - blood ; Collagen - chemistry ; Collagen - metabolism ; Glycoside Hydrolases - metabolism ; Glycosylation ; Glycosyltransferases - metabolism ; Hepatectomy ; Isoelectric Focusing ; Liver - enzymology ; Liver - metabolism ; Liver - surgery ; Liver Regeneration - physiology ; Male ; N-Acetylneuraminic Acid - metabolism ; Oligosaccharides - analysis ; Protein Binding ; Rats ; Rats, Wistar ; Vitronectin - blood ; Vitronectin - chemistry ; Vitronectin - metabolism</subject><ispartof>Glycobiology (Oxford), 2000-09, Vol.10 (9), p.865-874</ispartof><rights>Copyright Oxford University Press(England) Sep 1, 2000</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-62d86f6dfa7eaec6e8c2f0cf31148414d4ecf8ba66eaa430a1794e01e68f206b3</citedby><cites>FETCH-LOGICAL-c386t-62d86f6dfa7eaec6e8c2f0cf31148414d4ecf8ba66eaa430a1794e01e68f206b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,778,782,27911,27912</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10988248$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Uchibori-Iwaki, H</creatorcontrib><creatorcontrib>Yoneda, A</creatorcontrib><creatorcontrib>Oda-Tamai, S</creatorcontrib><creatorcontrib>Kato, S</creatorcontrib><creatorcontrib>Akamatsu, N</creatorcontrib><creatorcontrib>Otsuka, M</creatorcontrib><creatorcontrib>Murase, K</creatorcontrib><creatorcontrib>Kojima, K</creatorcontrib><creatorcontrib>Suzuki, R</creatorcontrib><creatorcontrib>Maeya, Y</creatorcontrib><creatorcontrib>Tanabe, M</creatorcontrib><creatorcontrib>Ogawa, H</creatorcontrib><title>The changes in glycosylation after partial hepatectomy enhance collagen binding of vitronectin in plasma</title><title>Glycobiology (Oxford)</title><addtitle>Glycobiology</addtitle><description>Vitronectin is a multifunctional glycoprotein present in the extracellular matrix and plasma. Changes in rat vitronectin were studied during liver regeneration after partial hepatectomy. Carbohydrate concentrations of vitronectin decreased to 2/3 of sham-operated rats at 24 h after partial hepatectomy. Carbohydrate composition and lectin reactivity indicated that N-glycosylation and sialylation of vitronectin changed markedly after partial hepatectomy, while amino acid composition did not change significantly. We previously showed that deN-glycosylation of vitronectin in vitro affects collagen binding among various ligands (Yoneda et al., Biochemistry (1998) 37, 6351-6360). Vitronectins from partially hepatectomized rats at 24 h were found to exhibit markedly enhanced binding to type I collagen. The effect of sialylation on collagen binding was further examined using enzymatically deglycosylated vitronectin of nonoperated rats. Collagen binding increased by 1.2 times after deN-glycosylation of vitronectin, while it increased more than 2.9 times after desialylation. Various glycosyltransferases in liver are known to change after partial hepatectomy, including the attenuation of N-oligosaccharide transferase. The findings therefore suggest that the collagen binding of vitronectin is modulated by the alteration of peptide glycosylation caused by postoperative physiological changes of glycosyltransferases and that the change may contribute to tissue remodeling processes.</description><subject>Amino Acids - analysis</subject><subject>Animals</subject><subject>Collagen - blood</subject><subject>Collagen - chemistry</subject><subject>Collagen - metabolism</subject><subject>Glycoside Hydrolases - metabolism</subject><subject>Glycosylation</subject><subject>Glycosyltransferases - metabolism</subject><subject>Hepatectomy</subject><subject>Isoelectric Focusing</subject><subject>Liver - enzymology</subject><subject>Liver - metabolism</subject><subject>Liver - surgery</subject><subject>Liver Regeneration - physiology</subject><subject>Male</subject><subject>N-Acetylneuraminic Acid - metabolism</subject><subject>Oligosaccharides - analysis</subject><subject>Protein Binding</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Vitronectin - blood</subject><subject>Vitronectin - chemistry</subject><subject>Vitronectin - metabolism</subject><issn>0959-6658</issn><issn>1460-2423</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkc1LxDAQxYMo7vpx9ibBg7fuJmmapkcRv2DBi57LNJ3sVtqkJl1h_3ujuwcRBoaB33s85hFyxdmCsypfrvud8c0yndVCq-KIzLlULBNS5MdkzqqiypQq9IycxfjBGFdcF6dklrRaC6nnZPO2QWo24NYYaefor2Hc9TB13lGwEwY6Qpg66OkGR5jQTH7YUXRJY5LU9z2s0dGmc23n1tRb-tVNwbsEJr80Yw9xgAtyYqGPeHnY5-T98eHt_jlbvT693N-tMpNrNWVKtFpZ1VooEdAo1EZYZmzOudSSy1aisboBpRBA5gx4WUlkHJW2gqkmPye3e98x-M8txqkeumgwpXTot7EuhSiVFFUCb_6BH34bXMpWC87ygrNSJWi5h0zwMQa09Ri6AcKu5qz-aaDeN_BzVnVqICmuD7bbZsD2D79_ef4NCwmFCw</recordid><startdate>20000901</startdate><enddate>20000901</enddate><creator>Uchibori-Iwaki, H</creator><creator>Yoneda, A</creator><creator>Oda-Tamai, S</creator><creator>Kato, S</creator><creator>Akamatsu, N</creator><creator>Otsuka, M</creator><creator>Murase, K</creator><creator>Kojima, K</creator><creator>Suzuki, R</creator><creator>Maeya, Y</creator><creator>Tanabe, M</creator><creator>Ogawa, H</creator><general>Oxford Publishing Limited (England)</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>7QL</scope><scope>7QO</scope><scope>7TK</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20000901</creationdate><title>The changes in glycosylation after partial hepatectomy enhance collagen binding of vitronectin in plasma</title><author>Uchibori-Iwaki, H ; Yoneda, A ; Oda-Tamai, S ; Kato, S ; Akamatsu, N ; Otsuka, M ; Murase, K ; Kojima, K ; Suzuki, R ; Maeya, Y ; Tanabe, M ; Ogawa, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-62d86f6dfa7eaec6e8c2f0cf31148414d4ecf8ba66eaa430a1794e01e68f206b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acids - analysis</topic><topic>Animals</topic><topic>Collagen - blood</topic><topic>Collagen - chemistry</topic><topic>Collagen - metabolism</topic><topic>Glycoside Hydrolases - metabolism</topic><topic>Glycosylation</topic><topic>Glycosyltransferases - metabolism</topic><topic>Hepatectomy</topic><topic>Isoelectric Focusing</topic><topic>Liver - enzymology</topic><topic>Liver - metabolism</topic><topic>Liver - surgery</topic><topic>Liver Regeneration - physiology</topic><topic>Male</topic><topic>N-Acetylneuraminic Acid - metabolism</topic><topic>Oligosaccharides - analysis</topic><topic>Protein Binding</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Vitronectin - blood</topic><topic>Vitronectin - chemistry</topic><topic>Vitronectin - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Uchibori-Iwaki, H</creatorcontrib><creatorcontrib>Yoneda, A</creatorcontrib><creatorcontrib>Oda-Tamai, S</creatorcontrib><creatorcontrib>Kato, S</creatorcontrib><creatorcontrib>Akamatsu, N</creatorcontrib><creatorcontrib>Otsuka, M</creatorcontrib><creatorcontrib>Murase, K</creatorcontrib><creatorcontrib>Kojima, K</creatorcontrib><creatorcontrib>Suzuki, R</creatorcontrib><creatorcontrib>Maeya, Y</creatorcontrib><creatorcontrib>Tanabe, M</creatorcontrib><creatorcontrib>Ogawa, H</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Glycobiology (Oxford)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Uchibori-Iwaki, H</au><au>Yoneda, A</au><au>Oda-Tamai, S</au><au>Kato, S</au><au>Akamatsu, N</au><au>Otsuka, M</au><au>Murase, K</au><au>Kojima, K</au><au>Suzuki, R</au><au>Maeya, Y</au><au>Tanabe, M</au><au>Ogawa, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The changes in glycosylation after partial hepatectomy enhance collagen binding of vitronectin in plasma</atitle><jtitle>Glycobiology (Oxford)</jtitle><addtitle>Glycobiology</addtitle><date>2000-09-01</date><risdate>2000</risdate><volume>10</volume><issue>9</issue><spage>865</spage><epage>874</epage><pages>865-874</pages><issn>0959-6658</issn><eissn>1460-2423</eissn><abstract>Vitronectin is a multifunctional glycoprotein present in the extracellular matrix and plasma. Changes in rat vitronectin were studied during liver regeneration after partial hepatectomy. Carbohydrate concentrations of vitronectin decreased to 2/3 of sham-operated rats at 24 h after partial hepatectomy. Carbohydrate composition and lectin reactivity indicated that N-glycosylation and sialylation of vitronectin changed markedly after partial hepatectomy, while amino acid composition did not change significantly. We previously showed that deN-glycosylation of vitronectin in vitro affects collagen binding among various ligands (Yoneda et al., Biochemistry (1998) 37, 6351-6360). Vitronectins from partially hepatectomized rats at 24 h were found to exhibit markedly enhanced binding to type I collagen. The effect of sialylation on collagen binding was further examined using enzymatically deglycosylated vitronectin of nonoperated rats. Collagen binding increased by 1.2 times after deN-glycosylation of vitronectin, while it increased more than 2.9 times after desialylation. Various glycosyltransferases in liver are known to change after partial hepatectomy, including the attenuation of N-oligosaccharide transferase. The findings therefore suggest that the collagen binding of vitronectin is modulated by the alteration of peptide glycosylation caused by postoperative physiological changes of glycosyltransferases and that the change may contribute to tissue remodeling processes.</abstract><cop>England</cop><pub>Oxford Publishing Limited (England)</pub><pmid>10988248</pmid><doi>10.1093/glycob/10.9.865</doi><tpages>10</tpages></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Oxford University Press Journals All Titles (1996-Current); Alma/SFX Local Collection |
| subjects | Amino Acids - analysis Animals Collagen - blood Collagen - chemistry Collagen - metabolism Glycoside Hydrolases - metabolism Glycosylation Glycosyltransferases - metabolism Hepatectomy Isoelectric Focusing Liver - enzymology Liver - metabolism Liver - surgery Liver Regeneration - physiology Male N-Acetylneuraminic Acid - metabolism Oligosaccharides - analysis Protein Binding Rats Rats, Wistar Vitronectin - blood Vitronectin - chemistry Vitronectin - metabolism |
| title | The changes in glycosylation after partial hepatectomy enhance collagen binding of vitronectin in plasma |
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