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Article: Functional analysis of site-directed glycosylation mutants of the human equilibrative nucleoside transporter-2

TitleFunctional analysis of site-directed glycosylation mutants of the human equilibrative nucleoside transporter-2
Authors
Issue Date2003
PublisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yabbi
Citation
Archives Of Biochemistry And Biophysics, 2003, v. 411 n. 1, p. 19-26 How to Cite?
AbstractProtein glycosylation is important for nucleoside transport, and this has been demonstrated for the human equilibrative nucleoside transporter-1 (hENT1). It is not known whether glycosylation affects the functions of hENT2 or where hENT2 is glycosylated. We address these questions using N-glycosylation mutants (N48D, N57D, and N48/57D) and demonstrate that hENT2 is glycosylated at Asn48 and Asn57. Our results show that although the apparent affinities for [3H]uridine and [3H]cytidine of the mutants were indistinguishable from those of the wild-type protein, N-glycosylation was required for efficient targeting of hENT2 to the plasma membrane. All mutants had a two- to threefold increase in IC50 for dipyridamole. N57D and N48/57D, but not N48D, also had a twofold increase in IC50 for NBMPR. We conclude that the relative insensitivity of hENT2 to inhibitors is primarily due to its primary structure and not to glycosylation. Glycosylation modulates hENT1 function, but is not required for hENT2. © 2003 Elsevier Science (USA). All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/171290
ISSN
2015 Impact Factor: 2.807
2015 SCImago Journal Rankings: 1.478
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWard, JLen_US
dc.contributor.authorLeung, GPHen_US
dc.contributor.authorToan, SVen_US
dc.contributor.authorTse, CMen_US
dc.date.accessioned2012-10-30T06:13:13Z-
dc.date.available2012-10-30T06:13:13Z-
dc.date.issued2003en_US
dc.identifier.citationArchives Of Biochemistry And Biophysics, 2003, v. 411 n. 1, p. 19-26en_US
dc.identifier.issn0003-9861en_US
dc.identifier.urihttp://hdl.handle.net/10722/171290-
dc.description.abstractProtein glycosylation is important for nucleoside transport, and this has been demonstrated for the human equilibrative nucleoside transporter-1 (hENT1). It is not known whether glycosylation affects the functions of hENT2 or where hENT2 is glycosylated. We address these questions using N-glycosylation mutants (N48D, N57D, and N48/57D) and demonstrate that hENT2 is glycosylated at Asn48 and Asn57. Our results show that although the apparent affinities for [3H]uridine and [3H]cytidine of the mutants were indistinguishable from those of the wild-type protein, N-glycosylation was required for efficient targeting of hENT2 to the plasma membrane. All mutants had a two- to threefold increase in IC50 for dipyridamole. N57D and N48/57D, but not N48D, also had a twofold increase in IC50 for NBMPR. We conclude that the relative insensitivity of hENT2 to inhibitors is primarily due to its primary structure and not to glycosylation. Glycosylation modulates hENT1 function, but is not required for hENT2. © 2003 Elsevier Science (USA). All rights reserved.en_US
dc.languageengen_US
dc.publisherAcademic Press. The Journal's web site is located at http://www.elsevier.com/locate/yabbien_US
dc.relation.ispartofArchives of Biochemistry and Biophysicsen_US
dc.subject.meshAmino Acid Substitutionen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAsparagineen_US
dc.subject.meshBiological Transporten_US
dc.subject.meshCell Lineen_US
dc.subject.meshCloning, Molecularen_US
dc.subject.meshEquilibrative-Nucleoside Transporter 2 - Chemistry - Metabolismen_US
dc.subject.meshGlycosylationen_US
dc.subject.meshHumansen_US
dc.subject.meshKidneyen_US
dc.subject.meshKineticsen_US
dc.subject.meshMutagenesis, Site-Directeden_US
dc.subject.meshRecombinant Proteins - Chemistry - Metabolismen_US
dc.subject.meshSwineen_US
dc.subject.meshTransfectionen_US
dc.subject.meshUridine - Metabolismen_US
dc.titleFunctional analysis of site-directed glycosylation mutants of the human equilibrative nucleoside transporter-2en_US
dc.typeArticleen_US
dc.identifier.emailLeung, GPH:gphleung@hkucc.hku.hken_US
dc.identifier.authorityLeung, GPH=rp00234en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1016/S0003-9861(02)00718-Xen_US
dc.identifier.pmid12590919-
dc.identifier.scopuseid_2-s2.0-0037373166en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0037373166&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume411en_US
dc.identifier.issue1en_US
dc.identifier.spage19en_US
dc.identifier.epage26en_US
dc.identifier.isiWOS:000181291100002-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridWard, JL=7404119073en_US
dc.identifier.scopusauthoridLeung, GPH=35963668200en_US
dc.identifier.scopusauthoridToan, SV=6505873802en_US
dc.identifier.scopusauthoridTse, CM=7103295076en_US

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