The enzymatic sulfation of glycoprotein carbohydrate units: blood group T-hapten specific and two other distinct Gal:3-O-sulfotransferases as evident from specificities and kinetics and the influence of sulfate and fucose residues occurring in the carbohydrate chain on C-3 sulfation of terminal Gal

Enzymatic 3-O-sulfation of terminal β-Gal residues was investigated by screening sulfotransferase activity present in 37 human tissue specimens toward the following synthesized acceptor moieties: Galβ1,3GalNAcα-O-Al, Galβ1,4GlcNAcβ-O-Al, Galβ1,3GlcNAcβ-O-Al, and mucin-type Galβ1,4GlcNAcβ1,6(Galβ1,3)...

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Veröffentlicht in:Glycobiology (Oxford) 1997-09, Vol.7 (6), p.753-767
Hauptverfasser: Chandrasekaran, E.V., Jain, Rakesh K., Vig, Rakesh, Matta, Khushi L.
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creator Chandrasekaran, E.V.
Jain, Rakesh K.
Vig, Rakesh
Matta, Khushi L.
description Enzymatic 3-O-sulfation of terminal β-Gal residues was investigated by screening sulfotransferase activity present in 37 human tissue specimens toward the following synthesized acceptor moieties: Galβ1,3GalNAcα-O-Al, Galβ1,4GlcNAcβ-O-Al, Galβ1,3GlcNAcβ-O-Al, and mucin-type Galβ1,4GlcNAcβ1,6(Galβ1,3)GalNAcα-O-Bn structures containing a C-3 methyl substituent on either Gal. Two distinct types of Gal: 3-O-sulfotransferases were revealed. One (Group A) was specific for the Galβ1, 3GalNAcα- linkage and the other (Group B) was directed toward the Galβ1,4GlcNAc branch β1,6 linked to the blood group T hapten. Enzyme activities found in breast tissues were unique in showing a strict specificity for the T-hapten. Galβ-O-allyl or benzyl did not serve as acceptors for Group A but were very active with Group B. An exainination of activity present in six human sera revealed a specificity of the serum enzyme toward β1,3 linked Gal, particularly, the T-hapten without β1,6 branching. Group A was highly active toward T-haptenlacrylamide copolymer, anti-freeze glycoprotein, and fetuin O-glycosidic asialo glycopeptide; less active toward fetuin triantennary asialo glycopeptide; and least active toward bovine IgG diantennary glycopeptide. Group B was moderately and highly active, respectively, with the latter two glycopeptides noted and least active with the first two. Competition experiments performed with Galβ1,3GaLNAcα-O-Al and Galβ1,4GlcNAcβ1,6(Galβ1,3)GalNAcα-O-Bn having a C-3 substituent (methyl or sulfate) on either Gal reinforced earlier findings on the specificity characteristics of Group A and Group B. Group A displayed a wider range of optimal activity (pH 6.0–7.4), whereas Group B possessed a peak of activity at pH 7.2. Mg2+ stimulated Group A 55% and Group B 150%, whereas Mn+2 stimulated Group B 130% but inhibited Group A 75%. Ca2+ stimulated Group B 100% but inhibited Group A 35%. Group A and Group B enzymes appeared to be of the same molecular size (
doi_str_mv 10.1093/glycob/7.6.753
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Two distinct types of Gal: 3-O-sulfotransferases were revealed. One (Group A) was specific for the Galβ1, 3GalNAcα- linkage and the other (Group B) was directed toward the Galβ1,4GlcNAc branch β1,6 linked to the blood group T hapten. Enzyme activities found in breast tissues were unique in showing a strict specificity for the T-hapten. Galβ-O-allyl or benzyl did not serve as acceptors for Group A but were very active with Group B. An exainination of activity present in six human sera revealed a specificity of the serum enzyme toward β1,3 linked Gal, particularly, the T-hapten without β1,6 branching. Group A was highly active toward T-haptenlacrylamide copolymer, anti-freeze glycoprotein, and fetuin O-glycosidic asialo glycopeptide; less active toward fetuin triantennary asialo glycopeptide; and least active toward bovine IgG diantennary glycopeptide. Group B was moderately and highly active, respectively, with the latter two glycopeptides noted and least active with the first two. Competition experiments performed with Galβ1,3GaLNAcα-O-Al and Galβ1,4GlcNAcβ1,6(Galβ1,3)GalNAcα-O-Bn having a C-3 substituent (methyl or sulfate) on either Gal reinforced earlier findings on the specificity characteristics of Group A and Group B. Group A displayed a wider range of optimal activity (pH 6.0–7.4), whereas Group B possessed a peak of activity at pH 7.2. Mg2+ stimulated Group A 55% and Group B 150%, whereas Mn+2 stimulated Group B 130% but inhibited Group A 75%. Ca2+ stimulated Group B 100% but inhibited Group A 35%. Group A and Group B enzymes appeared to be of the same molecular size (&lt;100,000 Da) as observed by Sephacryl S-100 HR column chromatography. The following effects upon Gal: 3-O- sulfotransferase activities by fucose, sulfate, and other substituents on the carbohydrate chains were noted. (1) A methyl or GlcNAc substituent on C-6 of GalNAc diminished the ability of Galβ1,3GalNAcα-O-Al to act as an acceptor for Group A. (2) An α1,3-fucosyl residue on the β1,6 branch in the mucin core structure did not affect the activity of Group A toward Gal linked β1,3 to GalNAcα-. (3) Lewis x and Lewis a terminals did not serve as acceptors for either Group A or B enzymes. (4) Elimination of Group B activity on Gal in the β1,6 branch owing to the presence of a 3-fucosyl or 6-sulfo group on GlcNAc did not hinder any action toward Gal linked β1,3 to GalNAcα. (5) Group A activity on Gal linked β1,3 to GalNAc remained imaffected by 3'-sulfation of the β1,6 branch. The reverse was true for Group B. (6) The acceptor activity of the T-hapten was increased somewhat upon C-6 sulfation of GalNAc, whereas, C-6 slalylation resulted in an 85% loss of activity. (7) A novel finding was that Galβ1,4GlcNAcβ-O-Al and Galβ1,3GlcNAcβ-O-M, upon C-6 sulfation of the GlcNAc moiety, became 100% inactive and 5- to 7-fold active, respectively, in their ability to serve as acceptors for Group B.</description><identifier>ISSN: 0959-6658</identifier><identifier>EISSN: 1460-2423</identifier><identifier>DOI: 10.1093/glycob/7.6.753</identifier><identifier>PMID: 9376678</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Animals ; Carbohydrate Sequence ; Cations, Divalent ; Cattle ; Chromatography, Thin Layer ; Fucose - metabolism ; Galactose - metabolism ; galactose:sulfotransferase ; Glycoconjugates - chemistry ; Glycoconjugates - metabolism ; glycoprotein ; Glycoproteins - metabolism ; Glycosides - metabolism ; human tissues ; Humans ; Hydrogen-Ion Concentration ; kinetic properties ; Kinetics ; Molecular Sequence Data ; Molecular Weight ; specificities ; Substrate Specificity ; Sulfates - metabolism ; Sulfotransferases - metabolism</subject><ispartof>Glycobiology (Oxford), 1997-09, Vol.7 (6), p.753-767</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c368t-99e83a1bc64877502e845af93aedd078d3b31be01904b94428a6023a9c9f60493</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9376678$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chandrasekaran, E.V.</creatorcontrib><creatorcontrib>Jain, Rakesh K.</creatorcontrib><creatorcontrib>Vig, Rakesh</creatorcontrib><creatorcontrib>Matta, Khushi L.</creatorcontrib><title>The enzymatic sulfation of glycoprotein carbohydrate units: blood group T-hapten specific and two other distinct Gal:3-O-sulfotransferases as evident from specificities and kinetics and the influence of sulfate and fucose residues occurring in the carbohydrate chain on C-3 sulfation of terminal Gal</title><title>Glycobiology (Oxford)</title><addtitle>Glycobiology</addtitle><description>Enzymatic 3-O-sulfation of terminal β-Gal residues was investigated by screening sulfotransferase activity present in 37 human tissue specimens toward the following synthesized acceptor moieties: Galβ1,3GalNAcα-O-Al, Galβ1,4GlcNAcβ-O-Al, Galβ1,3GlcNAcβ-O-Al, and mucin-type Galβ1,4GlcNAcβ1,6(Galβ1,3)GalNAcα-O-Bn structures containing a C-3 methyl substituent on either Gal. Two distinct types of Gal: 3-O-sulfotransferases were revealed. One (Group A) was specific for the Galβ1, 3GalNAcα- linkage and the other (Group B) was directed toward the Galβ1,4GlcNAc branch β1,6 linked to the blood group T hapten. Enzyme activities found in breast tissues were unique in showing a strict specificity for the T-hapten. Galβ-O-allyl or benzyl did not serve as acceptors for Group A but were very active with Group B. An exainination of activity present in six human sera revealed a specificity of the serum enzyme toward β1,3 linked Gal, particularly, the T-hapten without β1,6 branching. Group A was highly active toward T-haptenlacrylamide copolymer, anti-freeze glycoprotein, and fetuin O-glycosidic asialo glycopeptide; less active toward fetuin triantennary asialo glycopeptide; and least active toward bovine IgG diantennary glycopeptide. Group B was moderately and highly active, respectively, with the latter two glycopeptides noted and least active with the first two. Competition experiments performed with Galβ1,3GaLNAcα-O-Al and Galβ1,4GlcNAcβ1,6(Galβ1,3)GalNAcα-O-Bn having a C-3 substituent (methyl or sulfate) on either Gal reinforced earlier findings on the specificity characteristics of Group A and Group B. Group A displayed a wider range of optimal activity (pH 6.0–7.4), whereas Group B possessed a peak of activity at pH 7.2. Mg2+ stimulated Group A 55% and Group B 150%, whereas Mn+2 stimulated Group B 130% but inhibited Group A 75%. Ca2+ stimulated Group B 100% but inhibited Group A 35%. Group A and Group B enzymes appeared to be of the same molecular size (&lt;100,000 Da) as observed by Sephacryl S-100 HR column chromatography. The following effects upon Gal: 3-O- sulfotransferase activities by fucose, sulfate, and other substituents on the carbohydrate chains were noted. (1) A methyl or GlcNAc substituent on C-6 of GalNAc diminished the ability of Galβ1,3GalNAcα-O-Al to act as an acceptor for Group A. (2) An α1,3-fucosyl residue on the β1,6 branch in the mucin core structure did not affect the activity of Group A toward Gal linked β1,3 to GalNAcα-. (3) Lewis x and Lewis a terminals did not serve as acceptors for either Group A or B enzymes. (4) Elimination of Group B activity on Gal in the β1,6 branch owing to the presence of a 3-fucosyl or 6-sulfo group on GlcNAc did not hinder any action toward Gal linked β1,3 to GalNAcα. (5) Group A activity on Gal linked β1,3 to GalNAc remained imaffected by 3'-sulfation of the β1,6 branch. The reverse was true for Group B. (6) The acceptor activity of the T-hapten was increased somewhat upon C-6 sulfation of GalNAc, whereas, C-6 slalylation resulted in an 85% loss of activity. (7) A novel finding was that Galβ1,4GlcNAcβ-O-Al and Galβ1,3GlcNAcβ-O-M, upon C-6 sulfation of the GlcNAc moiety, became 100% inactive and 5- to 7-fold active, respectively, in their ability to serve as acceptors for Group B.</description><subject>Animals</subject><subject>Carbohydrate Sequence</subject><subject>Cations, Divalent</subject><subject>Cattle</subject><subject>Chromatography, Thin Layer</subject><subject>Fucose - metabolism</subject><subject>Galactose - metabolism</subject><subject>galactose:sulfotransferase</subject><subject>Glycoconjugates - chemistry</subject><subject>Glycoconjugates - metabolism</subject><subject>glycoprotein</subject><subject>Glycoproteins - metabolism</subject><subject>Glycosides - metabolism</subject><subject>human tissues</subject><subject>Humans</subject><subject>Hydrogen-Ion Concentration</subject><subject>kinetic properties</subject><subject>Kinetics</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>specificities</subject><subject>Substrate Specificity</subject><subject>Sulfates - metabolism</subject><subject>Sulfotransferases - metabolism</subject><issn>0959-6658</issn><issn>1460-2423</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUk2P0zAUDAi0lIUrNySfuKB0nTjxx95QBbtIK1ZCRUJcLMd5bs0mdrEdoPx63KaqtCd_zJvxvOcpijcVXlZYkKvNsNe-u2JLumQteVosqobism5q8qxYYNGKktKWvyhexvgT44pWvL0oLgRhlDK-ePJ-vQUE7t9-VMlqFKfB5I13yBt0lN4Fn8A6pFXo_HbfB5UATc6meI26wfsebYKfdmhdbtUugUNxB9qarKVcj9Ifj3zaQkC9jck6ndCNGq5JeV8envIpKBcNBBUhIhUR_LY9uIRM8ONZySZ7QLPcg3WQbc6HLIusM8METsPB72wejqCZtI-AAkTbT5nttZ5CsG6TKUfmo370VuXr3PWqJI9nkCCM1qnhYPtV8dyoIcLr03pZfPv0cb26Le_ubz6vPtyVmlCeSiGAE1V1mjacsRbXwJtWGUEU9D1mvCcdqTrAlcBNJ5qm5orimiihhaG4EeSyeDfr5tn_yuaTHG3UMAzKgZ-iZIJwjts2Fy7nQh18jAGM3AU7qrCXFZaHdMg5HZJJKnM6MuHtSXnqRujP5ac4ZLyc8fxZ8PcMq_AgKSOslbfff0ja1F9XzZe1rMh_pDDNvg</recordid><startdate>19970901</startdate><enddate>19970901</enddate><creator>Chandrasekaran, E.V.</creator><creator>Jain, Rakesh K.</creator><creator>Vig, Rakesh</creator><creator>Matta, Khushi L.</creator><general>Oxford University Press</general><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>19970901</creationdate><title>The enzymatic sulfation of glycoprotein carbohydrate units: blood group T-hapten specific and two other distinct Gal:3-O-sulfotransferases as evident from specificities and kinetics and the influence of sulfate and fucose residues occurring in the carbohydrate chain on C-3 sulfation of terminal Gal</title><author>Chandrasekaran, E.V. ; Jain, Rakesh K. ; Vig, Rakesh ; Matta, Khushi L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c368t-99e83a1bc64877502e845af93aedd078d3b31be01904b94428a6023a9c9f60493</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Animals</topic><topic>Carbohydrate Sequence</topic><topic>Cations, Divalent</topic><topic>Cattle</topic><topic>Chromatography, Thin Layer</topic><topic>Fucose - metabolism</topic><topic>Galactose - metabolism</topic><topic>galactose:sulfotransferase</topic><topic>Glycoconjugates - chemistry</topic><topic>Glycoconjugates - metabolism</topic><topic>glycoprotein</topic><topic>Glycoproteins - metabolism</topic><topic>Glycosides - metabolism</topic><topic>human tissues</topic><topic>Humans</topic><topic>Hydrogen-Ion Concentration</topic><topic>kinetic properties</topic><topic>Kinetics</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>specificities</topic><topic>Substrate Specificity</topic><topic>Sulfates - metabolism</topic><topic>Sulfotransferases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Chandrasekaran, E.V.</creatorcontrib><creatorcontrib>Jain, Rakesh K.</creatorcontrib><creatorcontrib>Vig, Rakesh</creatorcontrib><creatorcontrib>Matta, Khushi L.</creatorcontrib><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>Chandrasekaran, E.V.</au><au>Jain, Rakesh K.</au><au>Vig, Rakesh</au><au>Matta, Khushi L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The enzymatic sulfation of glycoprotein carbohydrate units: blood group T-hapten specific and two other distinct Gal:3-O-sulfotransferases as evident from specificities and kinetics and the influence of sulfate and fucose residues occurring in the carbohydrate chain on C-3 sulfation of terminal Gal</atitle><jtitle>Glycobiology (Oxford)</jtitle><addtitle>Glycobiology</addtitle><date>1997-09-01</date><risdate>1997</risdate><volume>7</volume><issue>6</issue><spage>753</spage><epage>767</epage><pages>753-767</pages><issn>0959-6658</issn><eissn>1460-2423</eissn><abstract>Enzymatic 3-O-sulfation of terminal β-Gal residues was investigated by screening sulfotransferase activity present in 37 human tissue specimens toward the following synthesized acceptor moieties: Galβ1,3GalNAcα-O-Al, Galβ1,4GlcNAcβ-O-Al, Galβ1,3GlcNAcβ-O-Al, and mucin-type Galβ1,4GlcNAcβ1,6(Galβ1,3)GalNAcα-O-Bn structures containing a C-3 methyl substituent on either Gal. Two distinct types of Gal: 3-O-sulfotransferases were revealed. One (Group A) was specific for the Galβ1, 3GalNAcα- linkage and the other (Group B) was directed toward the Galβ1,4GlcNAc branch β1,6 linked to the blood group T hapten. Enzyme activities found in breast tissues were unique in showing a strict specificity for the T-hapten. Galβ-O-allyl or benzyl did not serve as acceptors for Group A but were very active with Group B. An exainination of activity present in six human sera revealed a specificity of the serum enzyme toward β1,3 linked Gal, particularly, the T-hapten without β1,6 branching. Group A was highly active toward T-haptenlacrylamide copolymer, anti-freeze glycoprotein, and fetuin O-glycosidic asialo glycopeptide; less active toward fetuin triantennary asialo glycopeptide; and least active toward bovine IgG diantennary glycopeptide. Group B was moderately and highly active, respectively, with the latter two glycopeptides noted and least active with the first two. Competition experiments performed with Galβ1,3GaLNAcα-O-Al and Galβ1,4GlcNAcβ1,6(Galβ1,3)GalNAcα-O-Bn having a C-3 substituent (methyl or sulfate) on either Gal reinforced earlier findings on the specificity characteristics of Group A and Group B. Group A displayed a wider range of optimal activity (pH 6.0–7.4), whereas Group B possessed a peak of activity at pH 7.2. Mg2+ stimulated Group A 55% and Group B 150%, whereas Mn+2 stimulated Group B 130% but inhibited Group A 75%. Ca2+ stimulated Group B 100% but inhibited Group A 35%. Group A and Group B enzymes appeared to be of the same molecular size (&lt;100,000 Da) as observed by Sephacryl S-100 HR column chromatography. The following effects upon Gal: 3-O- sulfotransferase activities by fucose, sulfate, and other substituents on the carbohydrate chains were noted. (1) A methyl or GlcNAc substituent on C-6 of GalNAc diminished the ability of Galβ1,3GalNAcα-O-Al to act as an acceptor for Group A. (2) An α1,3-fucosyl residue on the β1,6 branch in the mucin core structure did not affect the activity of Group A toward Gal linked β1,3 to GalNAcα-. (3) Lewis x and Lewis a terminals did not serve as acceptors for either Group A or B enzymes. (4) Elimination of Group B activity on Gal in the β1,6 branch owing to the presence of a 3-fucosyl or 6-sulfo group on GlcNAc did not hinder any action toward Gal linked β1,3 to GalNAcα. (5) Group A activity on Gal linked β1,3 to GalNAc remained imaffected by 3'-sulfation of the β1,6 branch. The reverse was true for Group B. (6) The acceptor activity of the T-hapten was increased somewhat upon C-6 sulfation of GalNAc, whereas, C-6 slalylation resulted in an 85% loss of activity. (7) A novel finding was that Galβ1,4GlcNAcβ-O-Al and Galβ1,3GlcNAcβ-O-M, upon C-6 sulfation of the GlcNAc moiety, became 100% inactive and 5- to 7-fold active, respectively, in their ability to serve as acceptors for Group B.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>9376678</pmid><doi>10.1093/glycob/7.6.753</doi><tpages>15</tpages><oa>free_for_read</oa></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 Animals
Carbohydrate Sequence
Cations, Divalent
Cattle
Chromatography, Thin Layer
Fucose - metabolism
Galactose - metabolism
galactose:sulfotransferase
Glycoconjugates - chemistry
Glycoconjugates - metabolism
glycoprotein
Glycoproteins - metabolism
Glycosides - metabolism
human tissues
Humans
Hydrogen-Ion Concentration
kinetic properties
Kinetics
Molecular Sequence Data
Molecular Weight
specificities
Substrate Specificity
Sulfates - metabolism
Sulfotransferases - metabolism
title The enzymatic sulfation of glycoprotein carbohydrate units: blood group T-hapten specific and two other distinct Gal:3-O-sulfotransferases as evident from specificities and kinetics and the influence of sulfate and fucose residues occurring in the carbohydrate chain on C-3 sulfation of terminal Gal
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