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Authordc.contributor.authorDünner, Natalia 
Authordc.contributor.authorQuezada, Carolina es_CL
Authordc.contributor.authorBerndt, F. Andrés es_CL
Authordc.contributor.authorCánovas, José es_CL
Authordc.contributor.authorRojas Baechler, Cecilia es_CL
Admission datedc.date.accessioned2014-01-07T13:04:03Z
Available datedc.date.available2014-01-07T13:04:03Z
Publication datedc.date.issued2013-10
Cita de ítemdc.identifier.citationPLOS ONE, October 2013 | Volume 8 | Issue 10 | e75440en_US
Identifierdc.identifier.otherdoi: 10.1371/journal.pone.0075440
Identifierdc.identifier.urihttps://repositorio.uchile.cl/handle/2250/129097
General notedc.descriptionArtículo de publicación ISIen_US
Abstractdc.description.abstractThe renin-angiotensin system expressed in adipose tissue has been implicated in the modulation of adipocyte formation, glucose metabolism, triglyceride accumulation, lipolysis, and the onset of the adverse metabolic consequences of obesity. As we investigated angiotensin II signal transduction mechanisms in human preadipose cells, an interplay of extracellularsignal- regulated kinases 1 and 2 (ERK1,2) and Akt/PKB became evident. Angiotensin II caused attenuation of phosphorylated Akt (p-Akt), at serine 473; the p-Akt/Akt ratio decreased to 0.560.2-fold the control value without angiotensin II (p,0.001). Here we report that the reduction of phosphorylated Akt associates with ERK1,2 activities. In the absence of angiotensin II, inhibition of ERK1,2 activation with U0126 or PD98059 resulted in a 2.160.5 (p,0.001) and 1.460.2-fold (p,0.05) increase in the p-Akt/Akt ratio, respectively. In addition, partial knockdown of ERK1 protein expression by the short hairpin RNA technique also raised phosphorylated Akt in these cells (the p-Akt/Akt ratio was 1.560.1-fold the corresponding control; p,0.05). Furthermore, inhibition of ERK1,2 activation with U0126 prevented the reduction of p-Akt/Akt by angiotensin II. An analogous effect was found on the phosphorylation status of Akt downstream effectors, the forkhead box (Fox) proteins O1 and O4. Altogether, these results indicate that angiotensin II signaling in human preadipose cells involves an ERK1,2- dependent attenuation of Akt activity, whose impact on the biological functions under its regulation is not fully understood.en_US
Lenguagedc.language.isoenen_US
Type of licensedc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile*
Link to Licensedc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/cl/*
Títulodc.titleAngiotensin II Signaling in Human Preadipose Cells: Participation of ERK1,2-Dependent Modulation of Akten_US
Document typedc.typeArtículo de revista


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Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 3.0 Chile