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Article: Phosphorylation of P20 is associated with the actions of insulin in rat skeletal and smooth muscle

TitlePhosphorylation of P20 is associated with the actions of insulin in rat skeletal and smooth muscle
Authors
KeywordsAdenylyl cyclase
Aorta
Phosphoprotein
Proteomics
Signal transduction
Issue Date1999
PublisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.org
Citation
Biochemical Journal, 1999, v. 344 n. 3, p. 971-976 How to Cite?
AbstractAlthough a large number of protein kinase/phosphatases involved in insulin's actions have been characterized recently, relatively few of the downstream phosphoproteins have been identified. We have employed two-dimensional gel electrophoresis-based proteome analysis to investigate the insulin-evoked phosphorylation cascade in rat soleus muscle. Insulin reproducibly increased phosphorylation of a 20-kDa protein with a pI value of 6.0, which was identified subsequently as a phospho-isoform of P20, a small heat-shock-related protein. The adenylyl cyclase activator, forskolin, decreased phosphorylation of this P20 isoform and increased phosphorylation of another two P20 isoforms, with pI values of 5.9 and 5.6. Two-dimensional peptide mapping revealed that the phospho-peptides of these three P20 isoforms are different. In contrast to its action in soleus muscle, insulin decreased phosphorylation of the P20 isoform with pI 6.0 and increased phosphorylation of the two isoforms with pI values of 5.9 and 5.6 in vascular smooth muscle. This effect is similar to that induced by vasodilatory stimuli, suggesting that insulin could exert its vasodilatory action by affecting phosphorylation of P20. In summary, these results demonstrate that insulin differently modulates phosphorylation of P20 in skeletal and smooth muscle, and suggest that P20 could be a potential modulator of insulin's functions in these tissues.
Persistent Identifierhttp://hdl.handle.net/10722/162364
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.authorXu, Aen_HK
dc.contributor.authorCooper, GJSen_HK
dc.date.accessioned2012-09-05T05:19:17Z-
dc.date.available2012-09-05T05:19:17Z-
dc.date.issued1999en_HK
dc.identifier.citationBiochemical Journal, 1999, v. 344 n. 3, p. 971-976en_HK
dc.identifier.issn0264-6021en_HK
dc.identifier.urihttp://hdl.handle.net/10722/162364-
dc.description.abstractAlthough a large number of protein kinase/phosphatases involved in insulin's actions have been characterized recently, relatively few of the downstream phosphoproteins have been identified. We have employed two-dimensional gel electrophoresis-based proteome analysis to investigate the insulin-evoked phosphorylation cascade in rat soleus muscle. Insulin reproducibly increased phosphorylation of a 20-kDa protein with a pI value of 6.0, which was identified subsequently as a phospho-isoform of P20, a small heat-shock-related protein. The adenylyl cyclase activator, forskolin, decreased phosphorylation of this P20 isoform and increased phosphorylation of another two P20 isoforms, with pI values of 5.9 and 5.6. Two-dimensional peptide mapping revealed that the phospho-peptides of these three P20 isoforms are different. In contrast to its action in soleus muscle, insulin decreased phosphorylation of the P20 isoform with pI 6.0 and increased phosphorylation of the two isoforms with pI values of 5.9 and 5.6 in vascular smooth muscle. This effect is similar to that induced by vasodilatory stimuli, suggesting that insulin could exert its vasodilatory action by affecting phosphorylation of P20. In summary, these results demonstrate that insulin differently modulates phosphorylation of P20 in skeletal and smooth muscle, and suggest that P20 could be a potential modulator of insulin's functions in these tissues.en_HK
dc.languageengen_US
dc.publisherPortland Press Ltd. The Journal's web site is located at http://www.biochemj.orgen_HK
dc.relation.ispartofBiochemical Journalen_HK
dc.subjectAdenylyl cyclaseen_HK
dc.subjectAortaen_HK
dc.subjectPhosphoproteinen_HK
dc.subjectProteomicsen_HK
dc.subjectSignal transductionen_HK
dc.subject.meshAnimalsen_US
dc.subject.meshElectrophoresis, Gel, Two-Dimensionalen_US
dc.subject.meshForskolin - Pharmacologyen_US
dc.subject.meshHsp20 Heat-Shock Proteinsen_US
dc.subject.meshHeat-Shock Proteinsen_US
dc.subject.meshInsulin - Pharmacologyen_US
dc.subject.meshIsoelectric Pointen_US
dc.subject.meshMaleen_US
dc.subject.meshMuscle Proteins - Chemistryen_US
dc.subject.meshMuscle, Skeletal - Metabolismen_US
dc.subject.meshMuscle, Smooth, Vascular - Metabolismen_US
dc.subject.meshPhosphopeptides - Chemistryen_US
dc.subject.meshPhosphoproteins - Chemistryen_US
dc.subject.meshPhosphorylationen_US
dc.subject.meshProtein Isoformsen_US
dc.subject.meshRatsen_US
dc.subject.meshRats, Wistaren_US
dc.titlePhosphorylation of P20 is associated with the actions of insulin in rat skeletal and smooth muscleen_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_subscribed_fulltexten_US
dc.identifier.doi10.1042/0264-6021:3440971en_HK
dc.identifier.pmid10585888-
dc.identifier.scopuseid_2-s2.0-0033572651en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0033572651&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume344en_HK
dc.identifier.issue3en_HK
dc.identifier.spage971en_HK
dc.identifier.epage976en_HK
dc.identifier.isiWOS:000084688200041-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridWang, Y=34973733700en_HK
dc.identifier.scopusauthoridXu, A=7202655409en_HK
dc.identifier.scopusauthoridCooper, GJS=7402355946en_HK

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