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. 2009 Jul 13;4(7):e6221. doi: 10.1371/journal.pone.0006221

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This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

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Islets were incubated for 30 min at 2.8 or 8.3 mM glucose in the presence or absence of 20 nM GLP-1. Activation of PKB by GLP-1 was assessed with antibodies specific for Ser⁴⁷³phospho-PKB and PKB, respectively. (A) Representative immunoblot of phospho- and total PKB in rat islets. (B) Quantitative measurement of PKB phosphorylation after 30 min treatment with GLP-1. Results are means±SE of 4 separate experiments. #p<0.05, when compared to the corresponding ‘minus GLP-1’ group.