File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Hydroxylation and glycosylation of the four conserved lysine residues in the collagenous domain of adiponectin. Potential role in the modulation of its insulin-sensitizing activity

TitleHydroxylation and glycosylation of the four conserved lysine residues in the collagenous domain of adiponectin. Potential role in the modulation of its insulin-sensitizing activity
Authors
Issue Date2002
PublisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/
Citation
Journal Of Biological Chemistry, 2002, v. 277 n. 22, p. 19521-19529 How to Cite?
AbstractIt has recently been shown that the fat-derived hormone adiponectin has the ability to decrease hyperglycemia and to reverse insulin resistance. However, bacterially produced full-length adiponectin is functionally inactive. Here, we show that endogenous adiponectin secreted by adipocytes is post-translationally modified into eight different isoforms, as shown by two-dimensional gel electrophoresis. Carbohydrate detection revealed that six of the adiponectin isoforms are glycosylated. The glycosylation sites were mapped to several lysines (residues 68, 71, 80, and 104) located in the collagenous domain of adiponectin, each having the surrounding motif of GXKGE(D). These four lysines were found to be hydroxylated and subsequently glycosylated. The glycosides attached to each of these four hydroxylated lysines are possibly glucosylgalactosyl groups. Functional analysis revealed that full-length adiponectin produced by mammalian cells is much more potent than bacterially generated adiponectin in enhancing the ability of subphysiological concentrations of insulin to inhibit gluconeogenesis in primary rat hepatocytes, whereas this insulin-sensitizing ability was significantly attenuated when the four glycosylated lysines were substituted with arginines. These results indicate that full-length adiponectin produced by mammalian cells is functionally active as an insulin sensitizer and that hydroxylation and glycosylation of the four lysines in the collagenous domain might contribute to this activity.
Persistent Identifierhttp://hdl.handle.net/10722/162664
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWang, Yen_US
dc.contributor.authorXu, Aen_US
dc.contributor.authorKnight, Cen_US
dc.contributor.authorXu, LYen_US
dc.contributor.authorCooper, GJSen_US
dc.date.accessioned2012-09-05T05:22:11Z-
dc.date.available2012-09-05T05:22:11Z-
dc.date.issued2002en_US
dc.identifier.citationJournal Of Biological Chemistry, 2002, v. 277 n. 22, p. 19521-19529en_US
dc.identifier.issn0021-9258en_US
dc.identifier.urihttp://hdl.handle.net/10722/162664-
dc.description.abstractIt has recently been shown that the fat-derived hormone adiponectin has the ability to decrease hyperglycemia and to reverse insulin resistance. However, bacterially produced full-length adiponectin is functionally inactive. Here, we show that endogenous adiponectin secreted by adipocytes is post-translationally modified into eight different isoforms, as shown by two-dimensional gel electrophoresis. Carbohydrate detection revealed that six of the adiponectin isoforms are glycosylated. The glycosylation sites were mapped to several lysines (residues 68, 71, 80, and 104) located in the collagenous domain of adiponectin, each having the surrounding motif of GXKGE(D). These four lysines were found to be hydroxylated and subsequently glycosylated. The glycosides attached to each of these four hydroxylated lysines are possibly glucosylgalactosyl groups. Functional analysis revealed that full-length adiponectin produced by mammalian cells is much more potent than bacterially generated adiponectin in enhancing the ability of subphysiological concentrations of insulin to inhibit gluconeogenesis in primary rat hepatocytes, whereas this insulin-sensitizing ability was significantly attenuated when the four glycosylated lysines were substituted with arginines. These results indicate that full-length adiponectin produced by mammalian cells is functionally active as an insulin sensitizer and that hydroxylation and glycosylation of the four lysines in the collagenous domain might contribute to this activity.en_US
dc.languageengen_US
dc.publisherAmerican Society for Biochemistry and Molecular Biology, Inc. The Journal's web site is located at http://www.jbc.org/en_US
dc.relation.ispartofJournal of Biological Chemistryen_US
dc.rightsJournal of Biological Chemistry. Copyright © American Society for Biochemistry and Molecular Biology, Inc.-
dc.subject.mesh3T3 Cellsen_US
dc.subject.meshAdipocytes - Metabolismen_US
dc.subject.meshAdiponectinen_US
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCos Cellsen_US
dc.subject.meshCell Differentiationen_US
dc.subject.meshChromatography, High Pressure Liquiden_US
dc.subject.meshDose-Response Relationship, Drugen_US
dc.subject.meshElectrophoresis, Gel, Two-Dimensionalen_US
dc.subject.meshGlucose - Metabolismen_US
dc.subject.meshGlycosylationen_US
dc.subject.meshHepatocytes - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshInsulin - Metabolismen_US
dc.subject.meshIntercellular Signaling Peptides And Proteinsen_US
dc.subject.meshLysine - Chemistryen_US
dc.subject.meshMaleen_US
dc.subject.meshMiceen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshPeptides - Chemistryen_US
dc.subject.meshProtein Bindingen_US
dc.subject.meshProtein Isoformsen_US
dc.subject.meshProtein Processing, Post-Translationalen_US
dc.subject.meshProtein Structure, Tertiaryen_US
dc.subject.meshProteins - Chemistry - Metabolismen_US
dc.subject.meshRatsen_US
dc.subject.meshRats, Wistaren_US
dc.subject.meshRecombinant Proteins - Metabolismen_US
dc.subject.meshSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionizationen_US
dc.subject.meshTransfectionen_US
dc.subject.meshTrypsin - Metabolism - Pharmacologyen_US
dc.titleHydroxylation and glycosylation of the four conserved lysine residues in the collagenous domain of adiponectin. Potential role in the modulation of its insulin-sensitizing activityen_US
dc.typeArticleen_US
dc.identifier.emailXu, A:amxu@hkucc.hku.hken_US
dc.identifier.authorityXu, A=rp00485en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1074/jbc.M200601200en_US
dc.identifier.pmid11912203-
dc.identifier.scopuseid_2-s2.0-0037205414en_US
dc.identifier.hkuros114926-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0037205414&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume277en_US
dc.identifier.issue22en_US
dc.identifier.spage19521en_US
dc.identifier.epage19529en_US
dc.identifier.isiWOS:000175894800039-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridWang, Y=34973748100en_US
dc.identifier.scopusauthoridXu, A=7202655409en_US
dc.identifier.scopusauthoridKnight, C=7202380957en_US
dc.identifier.scopusauthoridXu, LY=7404744252en_US
dc.identifier.scopusauthoridCooper, GJS=7402355946en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats