High endothelial cells synthesize and degrade sLex. Putative implications for L-selectin-dependent recognition
L-selectin guides lymphocytes into peripheral lymphoid tissues by recognizing glycoprotein ligands decorated with 6-sulfated sialyl Lewis x (sulfo sLex). Here we have used a rat peripheral lymph node high endothelial cell line (Ax) to study in detail the synthesis, expression and degradation of sLex...
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| Veröffentlicht in: | FEBS letters 1999-07, Vol.455 (1), p.97-100 |
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| creator | Majuri, Marja-Leena Räbinä, Jarkko Niittymäki, Jaana Tiisala, Sinikka Mattila, Pirkko Aavik, Einari Miyasaka, Masayuki Renkonen, Ossi Renkonen, Risto |
| description | L-selectin guides lymphocytes into peripheral lymphoid tissues by recognizing glycoprotein ligands decorated with 6-sulfated sialyl Lewis x (sulfo sLex). Here we have used a rat peripheral lymph node high endothelial cell line (Ax) to study in detail the synthesis, expression and degradation of sLex epitope. We show here that Ax cells possess active α(1,3)fucosyltransferase Fuc-TVII, the enzyme responsible for the final fucosylation of sialyl-
N-acetyllactosamine during sLex synthesis, and express sLex on the cell surface. Furthermore, these cells degrade sLex, primarily by desialylating it to neutral Lex epitopes by α(2,3)sialidase(s). |
| doi_str_mv | 10.1016/S0014-5793(99)00834-0 |
| format | Article |
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N-acetyllactosamine during sLex synthesis, and express sLex on the cell surface. Furthermore, these cells degrade sLex, primarily by desialylating it to neutral Lex epitopes by α(2,3)sialidase(s).</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(99)00834-0</identifier><identifier>PMID: 10428480</identifier><language>eng</language><publisher>England: Elsevier B.V</publisher><subject>Animals ; Base Sequence ; Carbohydrate Sequence ; Cell Line ; CHO Cells ; Cricetinae ; DNA ; Endothelium ; Endothelium - cytology ; Endothelium - metabolism ; Fuc, fucose ; Fuc-T, fucosyltransferase ; Fucosyltransferases - genetics ; Fucosyltransferases - metabolism ; Gal, galactose ; GlcNAc, N-acetylglucosamine ; HEV, high endothelial venule ; Inflammation ; L-Selectin - metabolism ; Lex, Lewis x ; Molecular Sequence Data ; NeuNAc, N-acetylneuraminic acid ; Oligosaccharides - biosynthesis ; Oligosaccharides - chemistry ; Oligosaccharides - metabolism ; Protein Binding ; Rats ; RNA, Messenger - genetics ; Sequence Homology, Nucleic Acid ; Sialyl Lewis x ; sLex, sialyl Lewis x ; α(1,3)fucosyltransferase ; α(2,3)sialidase</subject><ispartof>FEBS letters, 1999-07, Vol.455 (1), p.97-100</ispartof><rights>1999 Federation of European Biochemical Societies</rights><rights>FEBS Letters 455 (1999) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4730-ae482f97689f2c4956a440124e42f1153d41482b38b1fd9d9001a4385ad7f3e93</citedby><cites>FETCH-LOGICAL-c4730-ae482f97689f2c4956a440124e42f1153d41482b38b1fd9d9001a4385ad7f3e93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2899%2900834-0$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0014579399008340$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,1411,1427,3537,27901,27902,45550,45551,46384,46808,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10428480$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Majuri, Marja-Leena</creatorcontrib><creatorcontrib>Räbinä, Jarkko</creatorcontrib><creatorcontrib>Niittymäki, Jaana</creatorcontrib><creatorcontrib>Tiisala, Sinikka</creatorcontrib><creatorcontrib>Mattila, Pirkko</creatorcontrib><creatorcontrib>Aavik, Einari</creatorcontrib><creatorcontrib>Miyasaka, Masayuki</creatorcontrib><creatorcontrib>Renkonen, Ossi</creatorcontrib><creatorcontrib>Renkonen, Risto</creatorcontrib><title>High endothelial cells synthesize and degrade sLex. Putative implications for L-selectin-dependent recognition</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>L-selectin guides lymphocytes into peripheral lymphoid tissues by recognizing glycoprotein ligands decorated with 6-sulfated sialyl Lewis x (sulfo sLex). Here we have used a rat peripheral lymph node high endothelial cell line (Ax) to study in detail the synthesis, expression and degradation of sLex epitope. We show here that Ax cells possess active α(1,3)fucosyltransferase Fuc-TVII, the enzyme responsible for the final fucosylation of sialyl-
N-acetyllactosamine during sLex synthesis, and express sLex on the cell surface. Furthermore, these cells degrade sLex, primarily by desialylating it to neutral Lex epitopes by α(2,3)sialidase(s).</description><subject>Animals</subject><subject>Base Sequence</subject><subject>Carbohydrate Sequence</subject><subject>Cell Line</subject><subject>CHO Cells</subject><subject>Cricetinae</subject><subject>DNA</subject><subject>Endothelium</subject><subject>Endothelium - cytology</subject><subject>Endothelium - metabolism</subject><subject>Fuc, fucose</subject><subject>Fuc-T, fucosyltransferase</subject><subject>Fucosyltransferases - genetics</subject><subject>Fucosyltransferases - metabolism</subject><subject>Gal, galactose</subject><subject>GlcNAc, N-acetylglucosamine</subject><subject>HEV, high endothelial venule</subject><subject>Inflammation</subject><subject>L-Selectin - metabolism</subject><subject>Lex, Lewis x</subject><subject>Molecular Sequence Data</subject><subject>NeuNAc, N-acetylneuraminic acid</subject><subject>Oligosaccharides - biosynthesis</subject><subject>Oligosaccharides - chemistry</subject><subject>Oligosaccharides - metabolism</subject><subject>Protein Binding</subject><subject>Rats</subject><subject>RNA, Messenger - genetics</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Sialyl Lewis x</subject><subject>sLex, sialyl Lewis x</subject><subject>α(1,3)fucosyltransferase</subject><subject>α(2,3)sialidase</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkEFv2yAUx9HUasm6fYRWnKr24AwMtuFUtVXSTIq0St3OiMBzwuTgDJxu6acfjqNqt_YEvPfjD--H0DklE0po-fWJEMqzopLsSsprQgTjGfmAxlRULGO8FCdo_IqM0KcYf5F0FlR-RCNKeC64IGPk5261xuBt262hcbrBBpom4rj3qRDdC2DtLbawCtoCjgv4O8GPu0537hmw22wbZ9K-9RHXbcCLLEIDpnM-s7BNseA7HMC0K-966jM6rXUT4ctxPUM_Z9Mf9_Ns8f3h2_3tIjO8YiTTwEVey6oUss4Nl0WpOSc058DzmtKCWU4TsWRiSWsrrUyTac5EoW1VM5DsDF0OudvQ_t5B7NTGxX4y7aHdRVVKyZIpnsBiAE1oYwxQq21wGx32ihLVi1YH0aq3qKRUB9GKpHsXxwd2yw3Y_24NZhMwH4A_roH9-1LVbHqXHzp9Q8pDuY-6GaIgGXt2EFQ0DrwB65LaTtnWvfHbf0Eloe4</recordid><startdate>19990716</startdate><enddate>19990716</enddate><creator>Majuri, Marja-Leena</creator><creator>Räbinä, Jarkko</creator><creator>Niittymäki, Jaana</creator><creator>Tiisala, Sinikka</creator><creator>Mattila, Pirkko</creator><creator>Aavik, Einari</creator><creator>Miyasaka, Masayuki</creator><creator>Renkonen, Ossi</creator><creator>Renkonen, Risto</creator><general>Elsevier B.V</general><scope>6I.</scope><scope>AAFTH</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>19990716</creationdate><title>High endothelial cells synthesize and degrade sLex. Putative implications for L-selectin-dependent recognition</title><author>Majuri, Marja-Leena ; Räbinä, Jarkko ; Niittymäki, Jaana ; Tiisala, Sinikka ; Mattila, Pirkko ; Aavik, Einari ; Miyasaka, Masayuki ; Renkonen, Ossi ; Renkonen, Risto</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4730-ae482f97689f2c4956a440124e42f1153d41482b38b1fd9d9001a4385ad7f3e93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Animals</topic><topic>Base Sequence</topic><topic>Carbohydrate Sequence</topic><topic>Cell Line</topic><topic>CHO Cells</topic><topic>Cricetinae</topic><topic>DNA</topic><topic>Endothelium</topic><topic>Endothelium - cytology</topic><topic>Endothelium - metabolism</topic><topic>Fuc, fucose</topic><topic>Fuc-T, fucosyltransferase</topic><topic>Fucosyltransferases - genetics</topic><topic>Fucosyltransferases - metabolism</topic><topic>Gal, galactose</topic><topic>GlcNAc, N-acetylglucosamine</topic><topic>HEV, high endothelial venule</topic><topic>Inflammation</topic><topic>L-Selectin - metabolism</topic><topic>Lex, Lewis x</topic><topic>Molecular Sequence Data</topic><topic>NeuNAc, N-acetylneuraminic acid</topic><topic>Oligosaccharides - biosynthesis</topic><topic>Oligosaccharides - chemistry</topic><topic>Oligosaccharides - metabolism</topic><topic>Protein Binding</topic><topic>Rats</topic><topic>RNA, Messenger - genetics</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Sialyl Lewis x</topic><topic>sLex, sialyl Lewis x</topic><topic>α(1,3)fucosyltransferase</topic><topic>α(2,3)sialidase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Majuri, Marja-Leena</creatorcontrib><creatorcontrib>Räbinä, Jarkko</creatorcontrib><creatorcontrib>Niittymäki, Jaana</creatorcontrib><creatorcontrib>Tiisala, Sinikka</creatorcontrib><creatorcontrib>Mattila, Pirkko</creatorcontrib><creatorcontrib>Aavik, Einari</creatorcontrib><creatorcontrib>Miyasaka, Masayuki</creatorcontrib><creatorcontrib>Renkonen, Ossi</creatorcontrib><creatorcontrib>Renkonen, Risto</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Majuri, Marja-Leena</au><au>Räbinä, Jarkko</au><au>Niittymäki, Jaana</au><au>Tiisala, Sinikka</au><au>Mattila, Pirkko</au><au>Aavik, Einari</au><au>Miyasaka, Masayuki</au><au>Renkonen, Ossi</au><au>Renkonen, Risto</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>High endothelial cells synthesize and degrade sLex. Putative implications for L-selectin-dependent recognition</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1999-07-16</date><risdate>1999</risdate><volume>455</volume><issue>1</issue><spage>97</spage><epage>100</epage><pages>97-100</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>L-selectin guides lymphocytes into peripheral lymphoid tissues by recognizing glycoprotein ligands decorated with 6-sulfated sialyl Lewis x (sulfo sLex). Here we have used a rat peripheral lymph node high endothelial cell line (Ax) to study in detail the synthesis, expression and degradation of sLex epitope. We show here that Ax cells possess active α(1,3)fucosyltransferase Fuc-TVII, the enzyme responsible for the final fucosylation of sialyl-
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| ispartof | FEBS letters, 1999-07, Vol.455 (1), p.97-100 |
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| language | eng |
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| subjects | Animals Base Sequence Carbohydrate Sequence Cell Line CHO Cells Cricetinae DNA Endothelium Endothelium - cytology Endothelium - metabolism Fuc, fucose Fuc-T, fucosyltransferase Fucosyltransferases - genetics Fucosyltransferases - metabolism Gal, galactose GlcNAc, N-acetylglucosamine HEV, high endothelial venule Inflammation L-Selectin - metabolism Lex, Lewis x Molecular Sequence Data NeuNAc, N-acetylneuraminic acid Oligosaccharides - biosynthesis Oligosaccharides - chemistry Oligosaccharides - metabolism Protein Binding Rats RNA, Messenger - genetics Sequence Homology, Nucleic Acid Sialyl Lewis x sLex, sialyl Lewis x α(1,3)fucosyltransferase α(2,3)sialidase |
| title | High endothelial cells synthesize and degrade sLex. Putative implications for L-selectin-dependent recognition |
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