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- Publisher Website: 10.1042/0264-6021:3460463
- Scopus: eid_2-s2.0-0034161982
- PMID: 10677367
- WOS: WOS:000085977300028
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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
Title | Expression of heparan sulphate L-iduronyl 2-O-sulphotransferase in human kidney 293 cells results in increased D-glucuronyl 2-O-sulphation |
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Authors | |
Keywords | 6-O-sulphation D-glucuronyl 2-O-sulphotransferase D-glucuronyl C-5 epimerization N-sulphation O-sulphation |
Issue Date | 2000 |
Publisher | Portland 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? |
Abstract | Functionally 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 Identifier | http://hdl.handle.net/10722/179407 |
ISSN | 2023 Impact Factor: 4.4 2023 SCImago Journal Rankings: 1.612 |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Rong, J | en_US |
dc.contributor.author | Habuchi, H | en_US |
dc.contributor.author | Kimata, K | en_US |
dc.contributor.author | Lindahl, U | en_US |
dc.contributor.author | KuscheGullberg, M | en_US |
dc.date.accessioned | 2012-12-19T09:56:14Z | - |
dc.date.available | 2012-12-19T09:56:14Z | - |
dc.date.issued | 2000 | en_US |
dc.identifier.citation | Biochemical Journal, 2000, v. 346 n. 2, p. 463-468 | en_US |
dc.identifier.issn | 0264-6021 | en_US |
dc.identifier.uri | http://hdl.handle.net/10722/179407 | - |
dc.description.abstract | Functionally 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.language | eng | en_US |
dc.publisher | Portland Press Ltd. The Journal's web site is located at http://www.biochemj.org | en_US |
dc.relation.ispartof | Biochemical Journal | en_US |
dc.subject | 6-O-sulphation | - |
dc.subject | D-glucuronyl 2-O-sulphotransferase | - |
dc.subject | D-glucuronyl C-5 epimerization | - |
dc.subject | N-sulphation | - |
dc.subject | O-sulphation | - |
dc.subject.mesh | Animals | en_US |
dc.subject.mesh | Carbohydrate Epimerases - Metabolism | en_US |
dc.subject.mesh | Cell Line | en_US |
dc.subject.mesh | Glucuronates - Metabolism | en_US |
dc.subject.mesh | Heparan Sulfate Proteoglycans - Metabolism | en_US |
dc.subject.mesh | Humans | en_US |
dc.subject.mesh | Kidney - Metabolism | en_US |
dc.subject.mesh | Mice | en_US |
dc.subject.mesh | Molecular Sequence Data | en_US |
dc.subject.mesh | Sulfotransferases - Metabolism | en_US |
dc.title | Expression of heparan sulphate L-iduronyl 2-O-sulphotransferase in human kidney 293 cells results in increased D-glucuronyl 2-O-sulphation | en_US |
dc.type | Article | en_US |
dc.identifier.email | Rong, J: jrong@hku.hk | en_US |
dc.identifier.authority | Rong, J=rp00515 | en_US |
dc.description.nature | link_to_subscribed_fulltext | en_US |
dc.identifier.doi | 10.1042/0264-6021:3460463 | en_US |
dc.identifier.pmid | 10677367 | - |
dc.identifier.scopus | eid_2-s2.0-0034161982 | en_US |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0034161982&selection=ref&src=s&origin=recordpage | en_US |
dc.identifier.volume | 346 | en_US |
dc.identifier.issue | 2 | en_US |
dc.identifier.spage | 463 | en_US |
dc.identifier.epage | 468 | en_US |
dc.identifier.isi | WOS:000085977300028 | - |
dc.publisher.place | United Kingdom | en_US |
dc.identifier.scopusauthorid | Rong, J=7005980047 | en_US |
dc.identifier.scopusauthorid | Habuchi, H=7005543543 | en_US |
dc.identifier.scopusauthorid | Kimata, K=35280139000 | en_US |
dc.identifier.scopusauthorid | Lindahl, U=35473807100 | en_US |
dc.identifier.scopusauthorid | KuscheGullberg, M=7004251579 | en_US |
dc.identifier.issnl | 0264-6021 | - |