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Article: Proteomic and functional characterization of endogenous adiponectin purified from fetal bovine serum

TitleProteomic and functional characterization of endogenous adiponectin purified from fetal bovine serum
Authors
KeywordsAdipokines
Adiponectin
Insulin resistance
Metabolic syndrome
Obesity
Type 2 diabetes
Issue Date2004
PublisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/proteomics
Citation
Proteomics, 2004, v. 4 n. 12, p. 3933-3942 How to Cite?
AbstractAdiponectin is a plasma protein exclusively secreted from fat tissue. Many recent pharmacological studies suggest that recombinant adiponectin has multiple therapeutic potentials for obesity-related metabolic disorders, including type 2 diabetes, dyslipidemia, insulin resistance and atherosclerosis. However, the physiological relevance of these findings remains to be further established. In the present study, we have purified endogenous adiponectin from fetal bovine serum and characterized its post-translational modifications and physiological functions in animal models. Endogenous bovine serum adiponectin consists predominantly of full-length proteins that form multiple oligomeric complexes, including trimers, hexamers and higher molecular species. Two-dimensional gel electrophoresis revealed that bovine serum adiponectin exists as multiple post-translationally modified isoforms with distinct molecular weight and isolectric point. Further analysis using mass spectrometry and Edman degradation sequencing demonstrated that five conserved lysine residues (Lys 28, 60, 63, 72 and 96) within the collagenous domain of bovine adiponectin are hydroxylated and glycosylated by a glucosyl╬▒(1-2)galactosyl group. Injection of endogenous bovine adiponectin into C57 mice potently decreased circulating glucose levels and enhanced lipid clearance after a high fat meal. Chronic administration of this protein for a period of two weeks significantly increased insulin sensitivity and glucose tolerance, and depleted hepatic lipid accumulation in high-fat fed mice. These results provide direct evidence that endogenous bovine adiponectin is a physiological hormone that can regulate lipid and glucose metabolism.
Persistent Identifierhttp://hdl.handle.net/10722/77337
ISSN
2015 Impact Factor: 4.079
2015 SCImago Journal Rankings: 1.476
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWang, Yen_HK
dc.contributor.authorLu, Gen_HK
dc.contributor.authorWong, WPSen_HK
dc.contributor.authorVliegenthart, JFGen_HK
dc.contributor.authorGerwig, GJen_HK
dc.contributor.authorLam, KSLen_HK
dc.contributor.authorCooper, GJSen_HK
dc.contributor.authorXu, Aen_HK
dc.date.accessioned2010-09-06T07:30:49Z-
dc.date.available2010-09-06T07:30:49Z-
dc.date.issued2004en_HK
dc.identifier.citationProteomics, 2004, v. 4 n. 12, p. 3933-3942en_HK
dc.identifier.issn1615-9853en_HK
dc.identifier.urihttp://hdl.handle.net/10722/77337-
dc.description.abstractAdiponectin is a plasma protein exclusively secreted from fat tissue. Many recent pharmacological studies suggest that recombinant adiponectin has multiple therapeutic potentials for obesity-related metabolic disorders, including type 2 diabetes, dyslipidemia, insulin resistance and atherosclerosis. However, the physiological relevance of these findings remains to be further established. In the present study, we have purified endogenous adiponectin from fetal bovine serum and characterized its post-translational modifications and physiological functions in animal models. Endogenous bovine serum adiponectin consists predominantly of full-length proteins that form multiple oligomeric complexes, including trimers, hexamers and higher molecular species. Two-dimensional gel electrophoresis revealed that bovine serum adiponectin exists as multiple post-translationally modified isoforms with distinct molecular weight and isolectric point. Further analysis using mass spectrometry and Edman degradation sequencing demonstrated that five conserved lysine residues (Lys 28, 60, 63, 72 and 96) within the collagenous domain of bovine adiponectin are hydroxylated and glycosylated by a glucosyl╬▒(1-2)galactosyl group. Injection of endogenous bovine adiponectin into C57 mice potently decreased circulating glucose levels and enhanced lipid clearance after a high fat meal. Chronic administration of this protein for a period of two weeks significantly increased insulin sensitivity and glucose tolerance, and depleted hepatic lipid accumulation in high-fat fed mice. These results provide direct evidence that endogenous bovine adiponectin is a physiological hormone that can regulate lipid and glucose metabolism.en_HK
dc.languageengen_HK
dc.publisherWiley - V C H Verlag GmbH & Co KGaA. The Journal's web site is located at http://www.wiley-vch.de/home/proteomicsen_HK
dc.relation.ispartofProteomicsen_HK
dc.subjectAdipokinesen_HK
dc.subjectAdiponectinen_HK
dc.subjectInsulin resistanceen_HK
dc.subjectMetabolic syndromeen_HK
dc.subjectObesityen_HK
dc.subjectType 2 diabetesen_HK
dc.subject.meshAdiponectinen_HK
dc.subject.meshAmino Acid Sequenceen_HK
dc.subject.meshAnimalsen_HK
dc.subject.meshBlotting, Westernen_HK
dc.subject.meshCattleen_HK
dc.subject.meshChromatography, High Pressure Liquiden_HK
dc.subject.meshElectrophoresis, Gel, Two-Dimensionalen_HK
dc.subject.meshEscherichia coli - metabolismen_HK
dc.subject.meshFatty Acids, Nonesterified - metabolismen_HK
dc.subject.meshGlucose - metabolismen_HK
dc.subject.meshGlucose Tolerance Testen_HK
dc.subject.meshGlycosylationen_HK
dc.subject.meshInsulin - metabolismen_HK
dc.subject.meshInsulin Resistanceen_HK
dc.subject.meshIntercellular Signaling Peptides and Proteins - blood - chemistry - isolation & purificationen_HK
dc.subject.meshIsoelectric Focusingen_HK
dc.subject.meshLipid Metabolismen_HK
dc.subject.meshLiver - metabolismen_HK
dc.subject.meshLysine - chemistryen_HK
dc.subject.meshMagnetic Resonance Spectroscopyen_HK
dc.subject.meshMaleen_HK
dc.subject.meshMass Spectrometry - methodsen_HK
dc.subject.meshMiceen_HK
dc.subject.meshMice, Inbred C57BLen_HK
dc.subject.meshMolecular Sequence Dataen_HK
dc.subject.meshProtein Processing, Post-Translationalen_HK
dc.subject.meshProtein Structure, Tertiaryen_HK
dc.subject.meshProteomics - methodsen_HK
dc.subject.meshRecombinant Proteins - chemistryen_HK
dc.subject.meshTime Factorsen_HK
dc.subject.meshTriglycerides - metabolismen_HK
dc.subject.meshTrypsin - chemistryen_HK
dc.titleProteomic and functional characterization of endogenous adiponectin purified from fetal bovine serumen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1615-9853&volume=4&spage=3933&epage=42&date=2004&atitle=Proteomic+and+functional+characterization+of+endogenous+adiponectin+purified+from+fetal+bovine+serum.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.doi10.1002/pmic.200400826en_HK
dc.identifier.pmid15378692-
dc.identifier.scopuseid_2-s2.0-10644228562en_HK
dc.identifier.hkuros120057en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-10644228562&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume4en_HK
dc.identifier.issue12en_HK
dc.identifier.spage3933en_HK
dc.identifier.epage3942en_HK
dc.identifier.isiWOS:000225801200022-
dc.publisher.placeGermanyen_HK
dc.identifier.scopusauthoridWang, Y=34973733700en_HK
dc.identifier.scopusauthoridLu, G=55197334400en_HK
dc.identifier.scopusauthoridWong, WPS=25947841100en_HK
dc.identifier.scopusauthoridVliegenthart, JFG=35473444200en_HK
dc.identifier.scopusauthoridGerwig, GJ=7003741811en_HK
dc.identifier.scopusauthoridLam, KSL=8082870600en_HK
dc.identifier.scopusauthoridCooper, GJS=7402355946en_HK
dc.identifier.scopusauthoridXu, A=7202655409en_HK

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