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Article: Post-translational modifications of adiponectin: Mechanisms and functional implications

TitlePost-translational modifications of adiponectin: Mechanisms and functional implications
Authors
KeywordsAdipokine
Adiponectin
Insulin sensitivity
Metabolic syndrome
Obesity
Issue Date2008
PublisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.org
Citation
Biochemical Journal, 2008, v. 409 n. 3, p. 623-633 How to Cite?
AbstractAdiponectin is an insulin-sensitizing adipokine with anti-diabetic, anti-atherogenic, anti-inflammatory and cardioprotective properties. This adipokine is secreted from adipocytes into the circulation as three oligomeric isoforms, including trimeric, hexameric and the HMW (high-molecular-mass) oligomeric complex consisting of at least 18 protomers. Each oligomeric isoform of adiponectin exerts distinct biological properties in its various target tissues. The HMW oligomer is the major active form mediating the insulin-sensitizing effects of adiponectin, whereas the central actions of this adipokine are attributed primarily to the hexameric and trimeric oligomers. In patients with Type 2 diabetes and coronary heart disease, circulating levels of HMW adiponectin are selectively decreased due to an impaired secretion of this oligomer from adipocytes. The biosynthesis of the adiponectin oligomers is a complex process involving extensive post-translational modifications. Hydroxylation and glycosylation of several conserved lysine residues in the collagenous domain of adiponectin are necessary for the intracellular assembly and stabilization of its high-order oligomeric structures. Secretion of the adiponectin oligomers is tightly controlled by a pair of molecular chaperones in the ER (endoplasmic reticulum), including ERp44 (ER protein of 44 kDa) and Ero1-Lα (ER oxidoreductase 1-Lα). ERp44 inhibits the secretion of adiponectin oligomers through a thiol-mediated retention. In contrast, Ero1-Lα releases HMW adiponectin trapped by ERp44. The PPARγ (peroxisome-proliferator-activated receptor γ) agonists thiazolidinediones selectively enhance the secretion of HMW adiponectin through up-regulation of Ero1-Lα. In the present review, we discuss the recent advances in our understanding of the structural and biological properties of the adiponectin oligomeric isoforms and highlight the role of post-translational modifications in regulating the biosynthesis of HMW adiponectin. © The Authors.
Persistent Identifierhttp://hdl.handle.net/10722/76832
ISSN
2015 Impact Factor: 3.562
2015 SCImago Journal Rankings: 2.582
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWang, Yen_HK
dc.contributor.authorLam, KSLen_HK
dc.contributor.authorYau, MHen_HK
dc.contributor.authorXu, Aen_HK
dc.date.accessioned2010-09-06T07:25:23Z-
dc.date.available2010-09-06T07:25:23Z-
dc.date.issued2008en_HK
dc.identifier.citationBiochemical Journal, 2008, v. 409 n. 3, p. 623-633en_HK
dc.identifier.issn0264-6021en_HK
dc.identifier.urihttp://hdl.handle.net/10722/76832-
dc.description.abstractAdiponectin is an insulin-sensitizing adipokine with anti-diabetic, anti-atherogenic, anti-inflammatory and cardioprotective properties. This adipokine is secreted from adipocytes into the circulation as three oligomeric isoforms, including trimeric, hexameric and the HMW (high-molecular-mass) oligomeric complex consisting of at least 18 protomers. Each oligomeric isoform of adiponectin exerts distinct biological properties in its various target tissues. The HMW oligomer is the major active form mediating the insulin-sensitizing effects of adiponectin, whereas the central actions of this adipokine are attributed primarily to the hexameric and trimeric oligomers. In patients with Type 2 diabetes and coronary heart disease, circulating levels of HMW adiponectin are selectively decreased due to an impaired secretion of this oligomer from adipocytes. The biosynthesis of the adiponectin oligomers is a complex process involving extensive post-translational modifications. Hydroxylation and glycosylation of several conserved lysine residues in the collagenous domain of adiponectin are necessary for the intracellular assembly and stabilization of its high-order oligomeric structures. Secretion of the adiponectin oligomers is tightly controlled by a pair of molecular chaperones in the ER (endoplasmic reticulum), including ERp44 (ER protein of 44 kDa) and Ero1-Lα (ER oxidoreductase 1-Lα). ERp44 inhibits the secretion of adiponectin oligomers through a thiol-mediated retention. In contrast, Ero1-Lα releases HMW adiponectin trapped by ERp44. The PPARγ (peroxisome-proliferator-activated receptor γ) agonists thiazolidinediones selectively enhance the secretion of HMW adiponectin through up-regulation of Ero1-Lα. In the present review, we discuss the recent advances in our understanding of the structural and biological properties of the adiponectin oligomeric isoforms and highlight the role of post-translational modifications in regulating the biosynthesis of HMW adiponectin. © The Authors.en_HK
dc.languageengen_HK
dc.publisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.orgen_HK
dc.relation.ispartofBiochemical Journalen_HK
dc.subjectAdipokineen_HK
dc.subjectAdiponectinen_HK
dc.subjectInsulin sensitivityen_HK
dc.subjectMetabolic syndromeen_HK
dc.subjectObesityen_HK
dc.subject.meshAdiponectin - chemistry - genetics - metabolism - secretionen_HK
dc.subject.meshAnimalsen_HK
dc.subject.meshHumansen_HK
dc.subject.meshPPAR gamma - agonists - metabolismen_HK
dc.subject.meshProtein Bindingen_HK
dc.subject.meshProtein Processing, Post-Translational - drug effectsen_HK
dc.subject.meshSignal Transductionen_HK
dc.titlePost-translational modifications of adiponectin: Mechanisms and functional implicationsen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0264-6021&volume=409&spage=623&epage=33&date=2008&atitle=Post-translational+modifications+of+adiponectin:+mechanisms+and+functional+implications.en_HK
dc.identifier.emailWang, Y: yuwanghk@hku.hken_HK
dc.identifier.emailLam, KSL: ksllam@hku.hken_HK
dc.identifier.emailXu, A: amxu@hkucc.hku.hken_HK
dc.identifier.authorityWang, Y=rp00239en_HK
dc.identifier.authorityLam, KSL=rp00343en_HK
dc.identifier.authorityXu, A=rp00485en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1042/BJ20071492en_HK
dc.identifier.pmid18177270-
dc.identifier.scopuseid_2-s2.0-38949125405en_HK
dc.identifier.hkuros140347en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-38949125405&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume409en_HK
dc.identifier.issue3en_HK
dc.identifier.spage623en_HK
dc.identifier.epage633en_HK
dc.identifier.isiWOS:000253013900001-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridWang, Y=34973733700en_HK
dc.identifier.scopusauthoridLam, KSL=8082870600en_HK
dc.identifier.scopusauthoridYau, MH=9233223900en_HK
dc.identifier.scopusauthoridXu, A=7202655409en_HK

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