Molecular Cloning of Squid N-Acetylgalactosamine 4-Sulfate 6-O-Sulfotransferase and Synthesis of a Unique Chondroitin Sulfate Containing E-D Hybrid Tetrasaccharide Structure by the Recombinant Enzyme
N-Acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) transfers sulfate to position 6 of GalNAc(4SO₄) residues in chondroitin sulfate (CS). We previously purified squid GalNAc4S-6ST and cloned a cDNA encoding the partial sequence of squid GalNAc4S-6ST. In this paper, we cloned squid Ga...
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| Veröffentlicht in: | Glycobiology (Oxford) 2007-12, Vol.17 (12), p.1365-1376 |
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| creator | Yamaguchi, Teruyoshi Ohtake, Shiori Kimata, Koji Habuchi, Osami |
| description | N-Acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) transfers sulfate to position 6 of GalNAc(4SO₄) residues in chondroitin sulfate (CS). We previously purified squid GalNAc4S-6ST and cloned a cDNA encoding the partial sequence of squid GalNAc4S-6ST. In this paper, we cloned squid GalNAc4S-6ST cDNA containing a full open reading frame and characterized the recombinant squid GalNAc4S-6ST. The cDNA predicts a Type II transmembrane protein composed of 425 amino acid residues. The recombinant squid GalNAc4S-6ST transferred sulfate preferentially to the internal GalNAc(4SO₄) residues of chondroitin sulfate A (CS-A); nevertheless, the nonreducing terminal GalNAc(4SO₄) could be sulfated efficiently when the GalNAc(4SO₄) residue was included in the unique nonreducing terminal structure, GalNAc(4SO₄)-GlcA(2SO₄)-GalNAc(6SO₄), which was previously found in CS-A. Shark cartilage chondroitin sulfate C (CS-C) and chondroitin sulfate D (CS-D), poor acceptors for human GalNAc4S-6ST, served as the good acceptors for the recombinant squid GalNAc4S-6ST. Analysis of the sulfated products formed from CS-C and CS-D revealed that GalNAc(4SO₄) residues included in a tetrasaccharide sequence, GlcA-GalNAc(4SO₄)-GlcA(2SO₄)-GalNAc(6SO₄), were sulfated efficiently by squid GalNAc4S-6ST, and the E-D hybrid tetrasaccharide sequence, GlcA-GalNAc(4,6-SO₄)-GlcA(2SO₄)-GalNAc(6SO₄) was generated in the resulting sulfated glycosaminoglycans. These observations indicate that the recombinant squid GalNAc4S-6ST is a useful enzyme for preparing a unique chondroitin sulfate containing the E-D hybrid tetrasaccharide structure. |
| doi_str_mv | 10.1093/glycob/cwm103 |
| format | Article |
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We previously purified squid GalNAc4S-6ST and cloned a cDNA encoding the partial sequence of squid GalNAc4S-6ST. In this paper, we cloned squid GalNAc4S-6ST cDNA containing a full open reading frame and characterized the recombinant squid GalNAc4S-6ST. The cDNA predicts a Type II transmembrane protein composed of 425 amino acid residues. The recombinant squid GalNAc4S-6ST transferred sulfate preferentially to the internal GalNAc(4SO₄) residues of chondroitin sulfate A (CS-A); nevertheless, the nonreducing terminal GalNAc(4SO₄) could be sulfated efficiently when the GalNAc(4SO₄) residue was included in the unique nonreducing terminal structure, GalNAc(4SO₄)-GlcA(2SO₄)-GalNAc(6SO₄), which was previously found in CS-A. Shark cartilage chondroitin sulfate C (CS-C) and chondroitin sulfate D (CS-D), poor acceptors for human GalNAc4S-6ST, served as the good acceptors for the recombinant squid GalNAc4S-6ST. Analysis of the sulfated products formed from CS-C and CS-D revealed that GalNAc(4SO₄) residues included in a tetrasaccharide sequence, GlcA-GalNAc(4SO₄)-GlcA(2SO₄)-GalNAc(6SO₄), were sulfated efficiently by squid GalNAc4S-6ST, and the E-D hybrid tetrasaccharide sequence, GlcA-GalNAc(4,6-SO₄)-GlcA(2SO₄)-GalNAc(6SO₄) was generated in the resulting sulfated glycosaminoglycans. These observations indicate that the recombinant squid GalNAc4S-6ST is a useful enzyme for preparing a unique chondroitin sulfate containing the E-D hybrid tetrasaccharide structure.</description><identifier>ISSN: 0959-6658</identifier><identifier>EISSN: 1460-2423</identifier><identifier>DOI: 10.1093/glycob/cwm103</identifier><identifier>PMID: 17893095</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; Cercopithecus aethiops ; chondroitin sulfate D ; chondroitin sulfate E ; Chondroitin Sulfates - chemistry ; Chromatography - methods ; Cloning, Molecular ; COS Cells ; Decapodiformes ; Enzymes - chemistry ; GalNAc4S-6ST ; Glycosaminoglycans - chemistry ; Molecular Sequence Data ; Open Reading Frames ; Polysaccharides - chemistry ; Recombinant Proteins - chemistry ; Sequence Homology, Amino Acid ; squid ; Substrate Specificity ; sulfotransferase ; Sulfotransferases - biosynthesis ; Sulfotransferases - chemistry ; Sulfotransferases - genetics</subject><ispartof>Glycobiology (Oxford), 2007-12, Vol.17 (12), p.1365-1376</ispartof><rights>Oxford University Press © The Author 2007. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org 2007</rights><rights>The Author 2007. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c479t-2e18ee435ab25c0463fb64f0b4bacef61dff5b5722441bd88807e476431c27d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,1578,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17893095$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yamaguchi, Teruyoshi</creatorcontrib><creatorcontrib>Ohtake, Shiori</creatorcontrib><creatorcontrib>Kimata, Koji</creatorcontrib><creatorcontrib>Habuchi, Osami</creatorcontrib><title>Molecular Cloning of Squid N-Acetylgalactosamine 4-Sulfate 6-O-Sulfotransferase and Synthesis of a Unique Chondroitin Sulfate Containing E-D Hybrid Tetrasaccharide Structure by the Recombinant Enzyme</title><title>Glycobiology (Oxford)</title><addtitle>Glycobiology</addtitle><description>N-Acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) transfers sulfate to position 6 of GalNAc(4SO₄) residues in chondroitin sulfate (CS). We previously purified squid GalNAc4S-6ST and cloned a cDNA encoding the partial sequence of squid GalNAc4S-6ST. In this paper, we cloned squid GalNAc4S-6ST cDNA containing a full open reading frame and characterized the recombinant squid GalNAc4S-6ST. The cDNA predicts a Type II transmembrane protein composed of 425 amino acid residues. The recombinant squid GalNAc4S-6ST transferred sulfate preferentially to the internal GalNAc(4SO₄) residues of chondroitin sulfate A (CS-A); nevertheless, the nonreducing terminal GalNAc(4SO₄) could be sulfated efficiently when the GalNAc(4SO₄) residue was included in the unique nonreducing terminal structure, GalNAc(4SO₄)-GlcA(2SO₄)-GalNAc(6SO₄), which was previously found in CS-A. Shark cartilage chondroitin sulfate C (CS-C) and chondroitin sulfate D (CS-D), poor acceptors for human GalNAc4S-6ST, served as the good acceptors for the recombinant squid GalNAc4S-6ST. Analysis of the sulfated products formed from CS-C and CS-D revealed that GalNAc(4SO₄) residues included in a tetrasaccharide sequence, GlcA-GalNAc(4SO₄)-GlcA(2SO₄)-GalNAc(6SO₄), were sulfated efficiently by squid GalNAc4S-6ST, and the E-D hybrid tetrasaccharide sequence, GlcA-GalNAc(4,6-SO₄)-GlcA(2SO₄)-GalNAc(6SO₄) was generated in the resulting sulfated glycosaminoglycans. These observations indicate that the recombinant squid GalNAc4S-6ST is a useful enzyme for preparing a unique chondroitin sulfate containing the E-D hybrid tetrasaccharide structure.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Cercopithecus aethiops</subject><subject>chondroitin sulfate D</subject><subject>chondroitin sulfate E</subject><subject>Chondroitin Sulfates - chemistry</subject><subject>Chromatography - methods</subject><subject>Cloning, Molecular</subject><subject>COS Cells</subject><subject>Decapodiformes</subject><subject>Enzymes - chemistry</subject><subject>GalNAc4S-6ST</subject><subject>Glycosaminoglycans - chemistry</subject><subject>Molecular Sequence Data</subject><subject>Open Reading Frames</subject><subject>Polysaccharides - chemistry</subject><subject>Recombinant Proteins - chemistry</subject><subject>Sequence Homology, Amino Acid</subject><subject>squid</subject><subject>Substrate Specificity</subject><subject>sulfotransferase</subject><subject>Sulfotransferases - biosynthesis</subject><subject>Sulfotransferases - chemistry</subject><subject>Sulfotransferases - genetics</subject><issn>0959-6658</issn><issn>1460-2423</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc1u1DAUhSMEokNhyRYsFohNqP_yt6yGoUPVoYiZShUby3FuZlwSe2o7gvCCvBZuM4DEhpWvdT99x9ZJkucEvyW4YifbblS2PlHfeoLZg2RGeI5Tyil7mMxwlVVpnmflUfLE-xuMSU7K7HFyRIqyYnE7S36ubAdq6KRD884abbbItmh9O-gGfUxPFYSx28pOqmC97LUBxNP10LUyAMrTy_vZBieNb8FJD0iaBq1HE3bgtb9zSXRl9O0AaL6zpnFWB23Qb8XcmiD1fewifYeWY-1i8Aai0UuldjJeAa2DG1QYHKB6RNGMPoOyfa2NNAEtzI-xh6fJo1Z2Hp4dzuNk836xmS_Ti8uzD_PTi1TxogopBVICcJbJmmYK85y1dc5bXPNaKmhz0rRtVmcFpZyTuinLEhfAi5wzomjRsOPk9aTdOxv_5IPotVfQddKAHbzIy4xQXNEIvvoHvLGDM_FpgsaieM5LEqF0gpSz3jtoxd7pXrpRECzu2hVTu2JqN_IvDtKh7qH5Sx_qjMCbCbDD_r-uQ7b2Ab7_gaX7KvKCFZlYXn8Ry_NPZ6vrFRPnkX858a20Qm6d9uJqTTFhGJe0JKRgvwDxCcwg</recordid><startdate>20071201</startdate><enddate>20071201</enddate><creator>Yamaguchi, Teruyoshi</creator><creator>Ohtake, Shiori</creator><creator>Kimata, Koji</creator><creator>Habuchi, Osami</creator><general>Oxford University Press</general><general>Oxford Publishing Limited (England)</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>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>20071201</creationdate><title>Molecular Cloning of Squid N-Acetylgalactosamine 4-Sulfate 6-O-Sulfotransferase and Synthesis of a Unique Chondroitin Sulfate Containing E-D Hybrid Tetrasaccharide Structure by the Recombinant Enzyme</title><author>Yamaguchi, Teruyoshi ; Ohtake, Shiori ; Kimata, Koji ; Habuchi, Osami</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c479t-2e18ee435ab25c0463fb64f0b4bacef61dff5b5722441bd88807e476431c27d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Cercopithecus aethiops</topic><topic>chondroitin sulfate D</topic><topic>chondroitin sulfate E</topic><topic>Chondroitin Sulfates - chemistry</topic><topic>Chromatography - methods</topic><topic>Cloning, Molecular</topic><topic>COS Cells</topic><topic>Decapodiformes</topic><topic>Enzymes - chemistry</topic><topic>GalNAc4S-6ST</topic><topic>Glycosaminoglycans - chemistry</topic><topic>Molecular Sequence Data</topic><topic>Open Reading Frames</topic><topic>Polysaccharides - chemistry</topic><topic>Recombinant Proteins - chemistry</topic><topic>Sequence Homology, Amino Acid</topic><topic>squid</topic><topic>Substrate Specificity</topic><topic>sulfotransferase</topic><topic>Sulfotransferases - biosynthesis</topic><topic>Sulfotransferases - chemistry</topic><topic>Sulfotransferases - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yamaguchi, Teruyoshi</creatorcontrib><creatorcontrib>Ohtake, Shiori</creatorcontrib><creatorcontrib>Kimata, Koji</creatorcontrib><creatorcontrib>Habuchi, Osami</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>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>Yamaguchi, Teruyoshi</au><au>Ohtake, Shiori</au><au>Kimata, Koji</au><au>Habuchi, Osami</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular Cloning of Squid N-Acetylgalactosamine 4-Sulfate 6-O-Sulfotransferase and Synthesis of a Unique Chondroitin Sulfate Containing E-D Hybrid Tetrasaccharide Structure by the Recombinant Enzyme</atitle><jtitle>Glycobiology (Oxford)</jtitle><addtitle>Glycobiology</addtitle><date>2007-12-01</date><risdate>2007</risdate><volume>17</volume><issue>12</issue><spage>1365</spage><epage>1376</epage><pages>1365-1376</pages><issn>0959-6658</issn><eissn>1460-2423</eissn><abstract>N-Acetylgalactosamine 4-sulfate 6-O-sulfotransferase (GalNAc4S-6ST) transfers sulfate to position 6 of GalNAc(4SO₄) residues in chondroitin sulfate (CS). We previously purified squid GalNAc4S-6ST and cloned a cDNA encoding the partial sequence of squid GalNAc4S-6ST. In this paper, we cloned squid GalNAc4S-6ST cDNA containing a full open reading frame and characterized the recombinant squid GalNAc4S-6ST. The cDNA predicts a Type II transmembrane protein composed of 425 amino acid residues. The recombinant squid GalNAc4S-6ST transferred sulfate preferentially to the internal GalNAc(4SO₄) residues of chondroitin sulfate A (CS-A); nevertheless, the nonreducing terminal GalNAc(4SO₄) could be sulfated efficiently when the GalNAc(4SO₄) residue was included in the unique nonreducing terminal structure, GalNAc(4SO₄)-GlcA(2SO₄)-GalNAc(6SO₄), which was previously found in CS-A. Shark cartilage chondroitin sulfate C (CS-C) and chondroitin sulfate D (CS-D), poor acceptors for human GalNAc4S-6ST, served as the good acceptors for the recombinant squid GalNAc4S-6ST. Analysis of the sulfated products formed from CS-C and CS-D revealed that GalNAc(4SO₄) residues included in a tetrasaccharide sequence, GlcA-GalNAc(4SO₄)-GlcA(2SO₄)-GalNAc(6SO₄), were sulfated efficiently by squid GalNAc4S-6ST, and the E-D hybrid tetrasaccharide sequence, GlcA-GalNAc(4,6-SO₄)-GlcA(2SO₄)-GalNAc(6SO₄) was generated in the resulting sulfated glycosaminoglycans. These observations indicate that the recombinant squid GalNAc4S-6ST is a useful enzyme for preparing a unique chondroitin sulfate containing the E-D hybrid tetrasaccharide structure.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>17893095</pmid><doi>10.1093/glycob/cwm103</doi><tpages>12</tpages></addata></record> |
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| source | Oxford University Press Journals All Titles (1996-Current); MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Animals Base Sequence Cercopithecus aethiops chondroitin sulfate D chondroitin sulfate E Chondroitin Sulfates - chemistry Chromatography - methods Cloning, Molecular COS Cells Decapodiformes Enzymes - chemistry GalNAc4S-6ST Glycosaminoglycans - chemistry Molecular Sequence Data Open Reading Frames Polysaccharides - chemistry Recombinant Proteins - chemistry Sequence Homology, Amino Acid squid Substrate Specificity sulfotransferase Sulfotransferases - biosynthesis Sulfotransferases - chemistry Sulfotransferases - genetics |
| title | Molecular Cloning of Squid N-Acetylgalactosamine 4-Sulfate 6-O-Sulfotransferase and Synthesis of a Unique Chondroitin Sulfate Containing E-D Hybrid Tetrasaccharide Structure by the Recombinant Enzyme |
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