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Article: Expression of heparan sulphate L-iduronyl 2-O-sulphotransferase in human kidney 293 cells results in increased D-glucuronyl 2-O-sulphation

TitleExpression of heparan sulphate L-iduronyl 2-O-sulphotransferase in human kidney 293 cells results in increased D-glucuronyl 2-O-sulphation
Authors
Issue Date2000
PublisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.org
Citation
Biochemical Journal, 2000, v. 346 n. 2, p. 463-468 How to Cite?
AbstractFunctionally important interactions between heparan sulphate and a variety of proteins depend on the precise location of O-sulphate groups. Such residues occur at C-2 of L-iduronic (IdoA) and D-glucuronic acid (GlcA) units, and at C-3 and C-6 of D-glucosamine (GlcN) units. Stable transfection of human embryonic kidney 293 cells with a cDNA encoding mouse mastocytoma IdoA 2-O-sulphotransferase resulted in an approx. 6-fold increase in O-sulphotransferase activity, compared with control cells, as determined using O-desulphated heparin as an acceptor. Structural analysis of endogenous heparan sulphate in the transfected cells, following metabolic labelling with either [ 3H]GlcN or [ 35S]sulphate, showed appreciable formation of -GlcA(2-OSO 3)-GlcNSO 3- disaccharide units (6% of total disaccharide units; 17% of total O-sulphated disaccharide units) that were essentially absent from heparan sulphate from control cells. The increase in GlcA 2-O-sulphation was accompanied by a decrease in the amount of IdoA formed, whereas overall 2-O-sulphation or 6-O-sulphation remained largely unaffected. These findings indicate that 2-O-sulphation of IdoA and GlcA residues is catalysed by the same enzyme in heparan sulphate biosynthesis.
Persistent Identifierhttp://hdl.handle.net/10722/179407
ISSN
2015 Impact Factor: 3.562
2015 SCImago Journal Rankings: 2.582
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorRong, Jen_US
dc.contributor.authorHabuchi, Hen_US
dc.contributor.authorKimata, Ken_US
dc.contributor.authorLindahl, Uen_US
dc.contributor.authorKuscheGullberg, Men_US
dc.date.accessioned2012-12-19T09:56:14Z-
dc.date.available2012-12-19T09:56:14Z-
dc.date.issued2000en_US
dc.identifier.citationBiochemical Journal, 2000, v. 346 n. 2, p. 463-468en_US
dc.identifier.issn0264-6021en_US
dc.identifier.urihttp://hdl.handle.net/10722/179407-
dc.description.abstractFunctionally important interactions between heparan sulphate and a variety of proteins depend on the precise location of O-sulphate groups. Such residues occur at C-2 of L-iduronic (IdoA) and D-glucuronic acid (GlcA) units, and at C-3 and C-6 of D-glucosamine (GlcN) units. Stable transfection of human embryonic kidney 293 cells with a cDNA encoding mouse mastocytoma IdoA 2-O-sulphotransferase resulted in an approx. 6-fold increase in O-sulphotransferase activity, compared with control cells, as determined using O-desulphated heparin as an acceptor. Structural analysis of endogenous heparan sulphate in the transfected cells, following metabolic labelling with either [ 3H]GlcN or [ 35S]sulphate, showed appreciable formation of -GlcA(2-OSO 3)-GlcNSO 3- disaccharide units (6% of total disaccharide units; 17% of total O-sulphated disaccharide units) that were essentially absent from heparan sulphate from control cells. The increase in GlcA 2-O-sulphation was accompanied by a decrease in the amount of IdoA formed, whereas overall 2-O-sulphation or 6-O-sulphation remained largely unaffected. These findings indicate that 2-O-sulphation of IdoA and GlcA residues is catalysed by the same enzyme in heparan sulphate biosynthesis.en_US
dc.languageengen_US
dc.publisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.orgen_US
dc.relation.ispartofBiochemical Journalen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCarbohydrate Epimerases - Metabolismen_US
dc.subject.meshCell Lineen_US
dc.subject.meshGlucuronates - Metabolismen_US
dc.subject.meshHeparan Sulfate Proteoglycans - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshKidney - Metabolismen_US
dc.subject.meshMiceen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshSulfotransferases - Metabolismen_US
dc.titleExpression of heparan sulphate L-iduronyl 2-O-sulphotransferase in human kidney 293 cells results in increased D-glucuronyl 2-O-sulphationen_US
dc.typeArticleen_US
dc.identifier.emailRong, J: jrong@hku.hken_US
dc.identifier.authorityRong, J=rp00515en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1042/0264-6021:3460463en_US
dc.identifier.pmid10677367-
dc.identifier.scopuseid_2-s2.0-0034161982en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0034161982&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume346en_US
dc.identifier.issue2en_US
dc.identifier.spage463en_US
dc.identifier.epage468en_US
dc.identifier.isiWOS:000085977300028-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridRong, J=7005980047en_US
dc.identifier.scopusauthoridHabuchi, H=7005543543en_US
dc.identifier.scopusauthoridKimata, K=35280139000en_US
dc.identifier.scopusauthoridLindahl, U=35473807100en_US
dc.identifier.scopusauthoridKuscheGullberg, M=7004251579en_US

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