VOLUME 283 (2008) PAGES 12446–12455
This article has been withdrawn by the authors. The Journal raised questions that the Akt immunoblot in Fig. 2B was reused in Fig. 6E, lanes 2 and 5 of the Akt immunoblot in Fig. 2C were duplicated, lanes 4 and 5 of the Akt immunoblot in Fig. 2C were reused in lanes 5 and 6 of the Akt immunoblot in Fig. 5C, lanes 2 and 5 of the Akt immunoblot were duplicated in Fig. 5C, the first lane of the PKCζ immunoblot in Fig. 4B was reused in Fig. 7A as Akt, and lanes 1 and 6 of the Akt immunoblot in Fig. 4C were duplicated. The authors were able to locate some of the original data and repeated experiments performed at the time of the original work, which the authors state support the conclusions of the paper. The authors state that the results of this paper are confirmed by the results of complementary experiments presented in the article, and some of the principal observations of this paper were further confirmed in publications from other laboratories (Elshaer, S. L. et al. (2018) Antioxidants 7, 47; Heo, K. S. et al. (2011) J. Cell Biol. 193, 867–884; Tommasini, I. et al. (2008) J. Immunol. 181, 5637–5645). The authors stand by the conclusions of the paper.
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- Protein Kinase Cζ-dependent LKB1 Serine 428 Phosphorylation Increases LKB1 Nucleus Export and Apoptosis in Endothelial CellsJournal of Biological ChemistryVol. 283Issue 18
- PreviewLKB1 is a serine-threonine protein kinase that, when inhibited, may result in unregulated cell growth and tumor formation. However, how LKB1 is regulated remains poorly understood. The aim of the present study was to define the upstream signaling events responsible for peroxynitrite (ONOO-)-induced LKB1 activation. Exposure of cultured human umbilical vein endothelial cells to a low concentration of ONOO- (5 μm) significantly increased the phosphorylation of LKB1 at Ser428 and protein kinase Cζ (PKCζ) at Thr410.
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