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Activation of PI3K/Akt but not Jak2/STAT5 signaling in PDAC cells exposed to Epo.

By Thilo Welsch (346916), Stefanie Zschäbitz (346917), Verena Becker (86709), Thomas Giese (21715), Frank Bergmann (54891), Ulf Hinz (346918), Shereen Keleg (120586), Anette Heller (120583), Bence Sipos (161263), Ursula Klingmüller (86712), Markus W. Büchler (128674), Jens Werner (135131) and Nathalia A. Giese (85732)


<p>(A) Phosphorylation status of Stat5 was assessed in serum-starved pancreatic tumor cells and hEpoR-transduced NIH/3T3 cells stimulated with 50 U/ml erythropoietin (Epo) for 10 min. Clear accumulation of pSTAT5 was observed in hEpoR-NIH/3T3 but not in mock-transduced NIH/3T3 cells or in PDAC cells, independent of the level of constitutive pSTAT5 activation. (B) Phosphorylation status of Akt was assessed in serum-starved (left panel) or non-starved (right panel) PANC-1 cells consequently stimulated with Epo at 0–50 U/ml for 15 min. Epo-enhanced pAkt phosporylation was detected only under conditions of serum starvation and could be specifically inhibited by anti-EpoR antibody (+Ab) or phosphatidylinositol-3-OH kinase (PI3K) inhibitor LY2940020 (+LY). (C) Accumulation of mRNA coding for soluble EpoR isoform (upper panel; primers: EpoR_S5/6, <a href="" target="_blank">table 2</a>) as compared to mRNAs coding for full-length isoforms (two middle panels) and further related to expression of ß-actin (lower panel). 3′-end-based detection of EpoR mRNA was performed with antisense primers binding after (EpoR_FL1/2) or prior to a stop codon (EpoR_FL3/4) as visualized by a hEpoR plasmid carrying only the coding sequence for a full-length isoform.</p

Topics: Biochemistry, Cell Biology, Genetics, Molecular Biology, Chemistry, Immunology, Cancer, signaling, pdac, cells, exposed
Year: 2013
DOI identifier: 10.1371/journal.pone.0023151.g006
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Provided by: FigShare
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