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Article: Substrate specificity of the heparan sulfate hexuronic acid 2-O-sulfotransferase

TitleSubstrate specificity of the heparan sulfate hexuronic acid 2-O-sulfotransferase
Authors
Issue Date2001
PublisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/biochemistry
Citation
Biochemistry, 2001, v. 40 n. 18, p. 5548-5555 How to Cite?
AbstractThe interaction of heparan sulfate with different ligand proteins depends on the precise location of O-sulfate groups in the polysaccharide chain. We have previously shown that overexpression in human kidney 293 cells of a mouse mastocytoma 2-O-sulfotransferase (2-OST), previously thought to catalyze the transfer of sulfate from 3′-phosphoadenosine 5′-phosphosulfate to C2 of L-iduronyl residues, preferentially increases the level of 2-O-sulfation of D-glucuronyl units [Rong, J., Habuchi, H., Kimata, K., Lindahl, U., and Kusche-Gullberg, M. (2000) Biochem. J. 346, 463-468]. In the study presented here, we further investigated the substrate specificity of the mouse mastocytoma 2-OST. Different polysaccharide acceptor substrates were incubated with cell extracts from 2-OST-transfected 293 cells together with the sulfate donor 3′-phosphoadenosine 5′-phospho[35S]sulfate. Incubations with O-desulfated heparin, predominantly composed of [(4)αIdoA(1)-(4)αGlcNSO3(1)-]n, resulted in 2-O-sulfation of iduronic acid. When, on the other hand, an N-sulfated capsular polysaccharide from Escherichia coli K5, with the structure [(4)βGlcA(1)-(4)αGlcNSO3(1)-]n, was used as an acceptor, sulfate was transferred almost exclusively to C2 of glucuronic acid. Substrates containing both iduronic and glucuronic acid residues in about equal proportions strongly favored sulfation of iduronic acid. In agreement with these results, the 2-OST was found to have a ∼5-fold higher affinity for iduronic acid-containing substrate disaccharide units (Km ∼ 3.7 μM) than for glucuronic acid-containing substrate disaccharide units (Km ∼ 19.3 μM).
Persistent Identifierhttp://hdl.handle.net/10722/179411
ISSN
2015 Impact Factor: 2.876
2015 SCImago Journal Rankings: 1.769
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.accessioned2012-12-19T09:56:15Z-
dc.date.available2012-12-19T09:56:15Z-
dc.date.issued2001en_US
dc.identifier.citationBiochemistry, 2001, v. 40 n. 18, p. 5548-5555en_US
dc.identifier.issn0006-2960en_US
dc.identifier.urihttp://hdl.handle.net/10722/179411-
dc.description.abstractThe interaction of heparan sulfate with different ligand proteins depends on the precise location of O-sulfate groups in the polysaccharide chain. We have previously shown that overexpression in human kidney 293 cells of a mouse mastocytoma 2-O-sulfotransferase (2-OST), previously thought to catalyze the transfer of sulfate from 3′-phosphoadenosine 5′-phosphosulfate to C2 of L-iduronyl residues, preferentially increases the level of 2-O-sulfation of D-glucuronyl units [Rong, J., Habuchi, H., Kimata, K., Lindahl, U., and Kusche-Gullberg, M. (2000) Biochem. J. 346, 463-468]. In the study presented here, we further investigated the substrate specificity of the mouse mastocytoma 2-OST. Different polysaccharide acceptor substrates were incubated with cell extracts from 2-OST-transfected 293 cells together with the sulfate donor 3′-phosphoadenosine 5′-phospho[35S]sulfate. Incubations with O-desulfated heparin, predominantly composed of [(4)αIdoA(1)-(4)αGlcNSO3(1)-]n, resulted in 2-O-sulfation of iduronic acid. When, on the other hand, an N-sulfated capsular polysaccharide from Escherichia coli K5, with the structure [(4)βGlcA(1)-(4)αGlcNSO3(1)-]n, was used as an acceptor, sulfate was transferred almost exclusively to C2 of glucuronic acid. Substrates containing both iduronic and glucuronic acid residues in about equal proportions strongly favored sulfation of iduronic acid. In agreement with these results, the 2-OST was found to have a ∼5-fold higher affinity for iduronic acid-containing substrate disaccharide units (Km ∼ 3.7 μM) than for glucuronic acid-containing substrate disaccharide units (Km ∼ 19.3 μM).en_US
dc.languageengen_US
dc.publisherAmerican Chemical Society. The Journal's web site is located at http://pubs.acs.org/biochemistryen_US
dc.relation.ispartofBiochemistryen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBrain - Enzymologyen_US
dc.subject.meshCell Lineen_US
dc.subject.meshGenetic Vectorsen_US
dc.subject.meshGlucuronic Acid - Metabolismen_US
dc.subject.meshHeparitin Sulfate - Metabolismen_US
dc.subject.meshHexuronic Acids - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshLung - Enzymologyen_US
dc.subject.meshMast-Cell Sarcoma - Enzymologyen_US
dc.subject.meshMiceen_US
dc.subject.meshOrgan Specificity - Geneticsen_US
dc.subject.meshRna, Messenger - Biosynthesisen_US
dc.subject.meshSubstrate Specificityen_US
dc.subject.meshSulfotransferases - Biosynthesis - Genetics - Metabolismen_US
dc.subject.meshTumor Cells, Cultureden_US
dc.titleSubstrate specificity of the heparan sulfate hexuronic acid 2-O-sulfotransferaseen_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.doi10.1021/bi002926pen_US
dc.identifier.pmid11331020-
dc.identifier.scopuseid_2-s2.0-0035826672en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0035826672&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume40en_US
dc.identifier.issue18en_US
dc.identifier.spage5548en_US
dc.identifier.epage5555en_US
dc.identifier.isiWOS:000168490400026-
dc.publisher.placeUnited Statesen_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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