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Article: Alteration in Phosphorylation of P20 Is Associated with Insulin Resistance

TitleAlteration in Phosphorylation of P20 Is Associated with Insulin Resistance
Authors
Issue Date2001
PublisherAmerican Diabetes Association. The Journal's web site is located at http://diabetes.diabetesjournals.org/
Citation
Diabetes, 2001, v. 50 n. 8, p. 1821-1827 How to Cite?
AbstractWe have recently identified a small phosphoprotein, P20, as a common intracellular target for insulin and several of its antagonists, including amylin, epinephrine, and calcitonin gene-related peptide. These hormones elicit phosphorylation of P20 at its different sites, producing three phosphorylated isoforms: S1 with an isoelectric point (pI) value of 6.0, S2 with a pI value of 5.9, and S3 with a pI value of 5.6 (FEBS Letters 457:149-152 and 462:25-30, 1999). In the current study, we showed that P20 is one of the most abundant phosphoproteins in rat extensor digitorum longus (EDL) muscle. Insulin and amylin antagonize each other's actions in the phosphorylation of this protein in rat EDL muscle. Insulin inhibits amylin-evoked phosphorylation of S2 and S3, whereas amylin decreases insulin-induced phosphorylation of S1. In rats made insulin resistant by dexamethasone treatment, levels of the phosphoisoforms S2 and S3, which were barely detectable in healthy rats in the absence of hormone stimulation, were significantly increased. Moreover, the ability of insulin to inhibit amylin-evoked phosphorylation of these two isoforms was greatly attenuated. These results suggested that alterations in the phosphorylation of P20 might be associated with insulin resistance and that P20 could serve as a useful marker to dissect the cellular mechanisms of this disease.
Persistent Identifierhttp://hdl.handle.net/10722/162531
ISSN
2015 Impact Factor: 8.784
2015 SCImago Journal Rankings: 5.185
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWang, Yen_HK
dc.contributor.authorXu, Aen_HK
dc.contributor.authorYe, Jen_HK
dc.contributor.authorKraegen, EWen_HK
dc.contributor.authorTse, CAen_HK
dc.contributor.authorCooper, GJSen_HK
dc.date.accessioned2012-09-05T05:20:49Z-
dc.date.available2012-09-05T05:20:49Z-
dc.date.issued2001en_HK
dc.identifier.citationDiabetes, 2001, v. 50 n. 8, p. 1821-1827en_HK
dc.identifier.issn0012-1797en_HK
dc.identifier.urihttp://hdl.handle.net/10722/162531-
dc.description.abstractWe have recently identified a small phosphoprotein, P20, as a common intracellular target for insulin and several of its antagonists, including amylin, epinephrine, and calcitonin gene-related peptide. These hormones elicit phosphorylation of P20 at its different sites, producing three phosphorylated isoforms: S1 with an isoelectric point (pI) value of 6.0, S2 with a pI value of 5.9, and S3 with a pI value of 5.6 (FEBS Letters 457:149-152 and 462:25-30, 1999). In the current study, we showed that P20 is one of the most abundant phosphoproteins in rat extensor digitorum longus (EDL) muscle. Insulin and amylin antagonize each other's actions in the phosphorylation of this protein in rat EDL muscle. Insulin inhibits amylin-evoked phosphorylation of S2 and S3, whereas amylin decreases insulin-induced phosphorylation of S1. In rats made insulin resistant by dexamethasone treatment, levels of the phosphoisoforms S2 and S3, which were barely detectable in healthy rats in the absence of hormone stimulation, were significantly increased. Moreover, the ability of insulin to inhibit amylin-evoked phosphorylation of these two isoforms was greatly attenuated. These results suggested that alterations in the phosphorylation of P20 might be associated with insulin resistance and that P20 could serve as a useful marker to dissect the cellular mechanisms of this disease.en_HK
dc.languageengen_US
dc.publisherAmerican Diabetes Association. The Journal's web site is located at http://diabetes.diabetesjournals.org/en_HK
dc.relation.ispartofDiabetesen_HK
dc.subject.meshAdipose Tissue - Metabolismen_US
dc.subject.meshAmyloid - Pharmacologyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAorta - Metabolismen_US
dc.subject.meshCalcitonin Gene-Related Peptide - Pharmacologyen_US
dc.subject.meshCell Lineen_US
dc.subject.meshDexamethasone - Pharmacologyen_US
dc.subject.meshDietary Fats - Pharmacologyen_US
dc.subject.meshElectrophoresis, Gel, Two-Dimensionalen_US
dc.subject.meshElectrophoresis, Polyacrylamide Gelen_US
dc.subject.meshEpinephrine - Pharmacologyen_US
dc.subject.meshHsp20 Heat-Shock Proteinsen_US
dc.subject.meshHeat-Shock Proteins - Metabolismen_US
dc.subject.meshInsulin - Pharmacologyen_US
dc.subject.meshInsulin Resistance - Physiologyen_US
dc.subject.meshIslet Amyloid Polypeptideen_US
dc.subject.meshLiver - Metabolismen_US
dc.subject.meshMaleen_US
dc.subject.meshModels, Animalen_US
dc.subject.meshMuscle Proteins - Genetics - Isolation & Purification - Metabolismen_US
dc.subject.meshMuscle, Skeletal - Drug Effects - Metabolismen_US
dc.subject.meshMuscle, Smooth, Vascular - Metabolismen_US
dc.subject.meshMyocardium - Metabolismen_US
dc.subject.meshPhosphoproteins - Genetics - Isolation & Purification - Metabolismen_US
dc.subject.meshPhosphorylationen_US
dc.subject.meshRatsen_US
dc.subject.meshRats, Wistaren_US
dc.subject.meshRecombinant Proteins - Metabolismen_US
dc.subject.meshReference Valuesen_US
dc.subject.meshTransfectionen_US
dc.titleAlteration in Phosphorylation of P20 Is Associated with Insulin Resistanceen_HK
dc.typeArticleen_HK
dc.identifier.emailWang, Y: yuwanghk@hku.hken_HK
dc.identifier.emailXu, A: amxu@hkucc.hku.hken_HK
dc.identifier.authorityWang, Y=rp00239en_HK
dc.identifier.authorityXu, A=rp00485en_HK
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.doi10.2337/diabetes.50.8.1821-
dc.identifier.pmid11473044-
dc.identifier.scopuseid_2-s2.0-0035433960en_HK
dc.identifier.hkuros114924-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0035433960&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume50en_HK
dc.identifier.issue8en_HK
dc.identifier.spage1821en_HK
dc.identifier.epage1827en_HK
dc.identifier.isiWOS:000170096700020-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridWang, Y=34973733700en_HK
dc.identifier.scopusauthoridXu, A=7202655409en_HK
dc.identifier.scopusauthoridYe, J=7403237496en_HK
dc.identifier.scopusauthoridKraegen, EW=7006873142en_HK
dc.identifier.scopusauthoridTse, CA=7103295215en_HK
dc.identifier.scopusauthoridCooper, GJS=7402355946en_HK

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