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Article: Insulin and insulin antagonists evoke phosphorylation of P20 at serine 157 and serine 16 respectively in rat skeletal muscle

TitleInsulin and insulin antagonists evoke phosphorylation of P20 at serine 157 and serine 16 respectively in rat skeletal muscle
Authors
KeywordsCalcitonin gene-related peptide
Epinephrine
Insulin
P20
Phosphorylation
Signal transduction
Issue Date1999
PublisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febslet
Citation
Febs Letters, 1999, v. 462 n. 1-2, p. 25-30 How to Cite?
AbstractWe show here that insulin and insulin antagonists differentially modify phosphorylation of three phospho-isoforms of P20 (termed S1, S2 and S3) in rat skeletal muscle. Precise phosphorylation sites of S1 and S2 were mapped to serine 157 and serine 16 respectively. Insulin evoked phosphorylation of P20 at serine 157 through the phosphatidylinositol (PI) 3-kinase pathway. Epinephrine and calcitonin gene-related peptide decreased phosphorylation at serine 157 and increased phosphorylation at serine 16 and other unidentified sites. These results demonstrate that the PI-3-kinase pathway of anabolic insulin and the cAMP pathway of catabolic hormones converge on P20 and suggest a potential role of this protein in regulating energy metabolism of skeletal muscle.
Persistent Identifierhttp://hdl.handle.net/10722/162279
ISSN
2015 Impact Factor: 3.519
2015 SCImago Journal Rankings: 2.026
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWang, Yen_HK
dc.contributor.authorXu, Aen_HK
dc.contributor.authorPearson, RBen_HK
dc.contributor.authorCooper, GJSen_HK
dc.date.accessioned2012-09-05T05:18:36Z-
dc.date.available2012-09-05T05:18:36Z-
dc.date.issued1999en_HK
dc.identifier.citationFebs Letters, 1999, v. 462 n. 1-2, p. 25-30en_HK
dc.identifier.issn0014-5793en_HK
dc.identifier.urihttp://hdl.handle.net/10722/162279-
dc.description.abstractWe show here that insulin and insulin antagonists differentially modify phosphorylation of three phospho-isoforms of P20 (termed S1, S2 and S3) in rat skeletal muscle. Precise phosphorylation sites of S1 and S2 were mapped to serine 157 and serine 16 respectively. Insulin evoked phosphorylation of P20 at serine 157 through the phosphatidylinositol (PI) 3-kinase pathway. Epinephrine and calcitonin gene-related peptide decreased phosphorylation at serine 157 and increased phosphorylation at serine 16 and other unidentified sites. These results demonstrate that the PI-3-kinase pathway of anabolic insulin and the cAMP pathway of catabolic hormones converge on P20 and suggest a potential role of this protein in regulating energy metabolism of skeletal muscle.en_HK
dc.languageengen_US
dc.publisherElsevier BV. The Journal's web site is located at http://www.elsevier.com/locate/febsleten_HK
dc.relation.ispartofFEBS Lettersen_HK
dc.subjectCalcitonin gene-related peptideen_HK
dc.subjectEpinephrineen_HK
dc.subjectInsulinen_HK
dc.subjectP20en_HK
dc.subjectPhosphorylationen_HK
dc.subjectSignal transductionen_HK
dc.subject.meshAmino Acid Sequenceen_US
dc.subject.meshAnimalsen_US
dc.subject.meshEnzyme Activationen_US
dc.subject.meshEpinephrine - Pharmacologyen_US
dc.subject.meshHsp20 Heat-Shock Proteinsen_US
dc.subject.meshHeat-Shock Proteinsen_US
dc.subject.meshHumansen_US
dc.subject.meshInsulin - Pharmacologyen_US
dc.subject.meshInsulin Antagonists - Pharmacologyen_US
dc.subject.meshMolecular Sequence Dataen_US
dc.subject.meshMuscle Proteins - Metabolismen_US
dc.subject.meshMuscle, Skeletal - Drug Effects - Metabolismen_US
dc.subject.meshPeptide Mappingen_US
dc.subject.meshPhosphatidylinositol 3-Kinases - Metabolismen_US
dc.subject.meshPhosphopeptides - Isolation & Purificationen_US
dc.subject.meshPhosphorylationen_US
dc.subject.meshProtein Isoforms - Metabolismen_US
dc.subject.meshRatsen_US
dc.subject.meshSerine - Metabolismen_US
dc.subject.meshSignal Transductionen_US
dc.titleInsulin and insulin antagonists evoke phosphorylation of P20 at serine 157 and serine 16 respectively in rat skeletal 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.doi10.1016/S0014-5793(99)01496-9en_HK
dc.identifier.pmid10580085-
dc.identifier.scopuseid_2-s2.0-0032712595en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0032712595&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume462en_HK
dc.identifier.issue1-2en_HK
dc.identifier.spage25en_HK
dc.identifier.epage30en_HK
dc.identifier.isiWOS:000083943300005-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridWang, Y=34973733700en_HK
dc.identifier.scopusauthoridXu, A=7202655409en_HK
dc.identifier.scopusauthoridPearson, RB=7401904914en_HK
dc.identifier.scopusauthoridCooper, GJS=7402355946en_HK

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