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Article: Amylin evokes phosphorylation of P20 in rat skeletal muscle

TitleAmylin evokes phosphorylation of P20 in rat skeletal muscle
Authors
KeywordsAmylin
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. 457 n. 1, p. 149-152 How to Cite?
AbstractTo investigate the signal transduction events underlying amylin's actions, the amylin-evoked protein phosphorylation cascade was analysed using two-dimensional gel electrophoresis. We found that phosphorylation of three isoelectric variants of P20 (termed ARPP1, ARPP2 and ARPP3) was associated with amylin's actions in rat skeletal muscle. Amylin decreased phosphorylation of ARPP1 and increased phosphorylation of ARPP2 and ARPP3 in a dose-dependent manner. Insulin inhibited amylin-evoked phosphorylation of ARPP2 and ARPP3. The amylin-selective antagonist rat amylin-(8-37) completely reversed amylin's action on ARPP3 and partially decreased phosphorylation of ARPP2. By contrast, the CGRP-selective antagonist, human CGRP-(8-37) blocked phosphorylation of ARPP2 but had little effect on ARPP3. These results suggest that amylin modifies phosphorylation of P20 via two independent mechanisms, and that P20 might be a molecule mediating amylin's biological functions. Copyright (C) 1999 Federation of European Biochemical Societies.
Persistent Identifierhttp://hdl.handle.net/10722/162294
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.authorCooper, GJSen_HK
dc.date.accessioned2012-09-05T05:18:43Z-
dc.date.available2012-09-05T05:18:43Z-
dc.date.issued1999en_HK
dc.identifier.citationFebs Letters, 1999, v. 457 n. 1, p. 149-152en_HK
dc.identifier.issn0014-5793en_HK
dc.identifier.urihttp://hdl.handle.net/10722/162294-
dc.description.abstractTo investigate the signal transduction events underlying amylin's actions, the amylin-evoked protein phosphorylation cascade was analysed using two-dimensional gel electrophoresis. We found that phosphorylation of three isoelectric variants of P20 (termed ARPP1, ARPP2 and ARPP3) was associated with amylin's actions in rat skeletal muscle. Amylin decreased phosphorylation of ARPP1 and increased phosphorylation of ARPP2 and ARPP3 in a dose-dependent manner. Insulin inhibited amylin-evoked phosphorylation of ARPP2 and ARPP3. The amylin-selective antagonist rat amylin-(8-37) completely reversed amylin's action on ARPP3 and partially decreased phosphorylation of ARPP2. By contrast, the CGRP-selective antagonist, human CGRP-(8-37) blocked phosphorylation of ARPP2 but had little effect on ARPP3. These results suggest that amylin modifies phosphorylation of P20 via two independent mechanisms, and that P20 might be a molecule mediating amylin's biological functions. Copyright (C) 1999 Federation of European Biochemical Societies.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.subjectAmylinen_HK
dc.subjectP20en_HK
dc.subjectPhosphorylationen_HK
dc.subjectSignal transductionen_HK
dc.subject.meshAmyloid - Antagonists & Inhibitors - Pharmacology - Physiologyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshDose-Response Relationship, Drugen_US
dc.subject.meshElectrophoresis, Gel, Two-Dimensionalen_US
dc.subject.meshHsp20 Heat-Shock Proteinsen_US
dc.subject.meshHeat-Shock Proteinsen_US
dc.subject.meshHindlimb - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshInsulin - Metabolismen_US
dc.subject.meshIslet Amyloid Polypeptideen_US
dc.subject.meshMaleen_US
dc.subject.meshMuscle Proteins - Metabolism - Physiologyen_US
dc.subject.meshMuscle, Skeletal - Metabolismen_US
dc.subject.meshPhosphorylationen_US
dc.subject.meshPrecipitin Testsen_US
dc.subject.meshRatsen_US
dc.subject.meshRats, Wistaren_US
dc.subject.meshSignal Transductionen_US
dc.titleAmylin evokes phosphorylation of P20 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)01029-7en_HK
dc.identifier.pmid10486583-
dc.identifier.scopuseid_2-s2.0-0032765124en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0032765124&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume457en_HK
dc.identifier.issue1en_HK
dc.identifier.spage149en_HK
dc.identifier.epage152en_HK
dc.identifier.isiWOS:000082228300033-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridWang, Y=34973733700en_HK
dc.identifier.scopusauthoridXu, A=7202655409en_HK
dc.identifier.scopusauthoridCooper, GJS=7402355946en_HK

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