Version of Record online: 23 MAY 2013
Copyright © 2013 American Association for the Study of Liver Diseases
Volume 58, Issue 1, pages 239–250, July 2013
How to Cite
Wang, Y.-W., Lin, K.-T., Chen, S.-C., Gu, D.-L., Chen, C.-F., Tu, P.-H. and Jou, Y.-S. (2013), Overexpressed-eIF3I interacted and activated oncogenic Akt1 is a theranostic target in human hepatocellular carcinoma. Hepatology, 58: 239–250. doi: 10.1002/hep.26352
Potential conflict of interest: Nothing to report.
Supported by funding from the National Research Program for Biopharmaceuticals (NSC 101-2325-B-001-011) and the National Science Council (NSC101-2320-B-001-029-MY3) of Taiwan.
- Issue online: 24 JUN 2013
- Version of Record online: 23 MAY 2013
- Accepted manuscript online: 4 MAR 2013 12:25PM EST
- Manuscript Accepted: 19 FEB 2013
- Manuscript Received: 10 OCT 2012
Additional Supporting Information may be found in the online version of this article.
|HEP_26352_sm_SuppFig1.tif||205K||Supporting Information Figure 1. eIF3I and Akt1 interaction is phosphorylation-dependent. (A) Treatment of calf-intestinal alkaline phosphatase (CIP) reduced interaction of overexpressed- eIF3I and Akt1 in 293T cells. (B) Treatment of Insulin-like growth factor 1 (IGF-1) to 293T transfectants of eIF3I and Akt1 increased phosphorylation of Akt1 and its interaction with eIF3I.|
|HEP_26352_sm_SuppFig2.tif||126K||Supporting Information Figure 2. eIF3I interrupted Akt1 protein interactions with PP2A. Akt1 can interact with PP2A-B and PP2A-C in 293 cells but loss their protein interactions when co- transfection with eIF3I. Tubulin served as protein loading control.|
|HEP_26352_sm_SuppFig3.tif||231K||Supporting Information Figure 3. eIF3I is not an Akt1 substrate. (A) Autoradiography of in vitro 32P-labeled kinase assay: detection of phosphorylated protein in immunoprecipitated complex in 293 cells with constitutively active Akt1 (myr-Akt1). (B) Detection of Akt1 phospho-substrate signal in HA-precipitated immune-complexes in 293T cells. Western blotting analysis of abovementioned proteins and tubulin served as expression and internal controls in lower panels.|
|HEP_26352_sm_SuppFig4.tif||131K||Supporting Information Figure 4. The subcellular localization of eIF3I-activated Akt1. Akt1 and eIF3I proteins are mainly localized in cytoplasm fraction and detectable in fractions of plasma membrane and nucleus. Tubulin, E-cadherin and histone H3 protein expression served as localization controls of cytoplasm, membrane and nucleus respectively.|
|HEP_26352_sm_SuppFig5.tif||208K||Supporting Information Figure 5. Growth effect of sorafenib treatments on eIF3I-overexpressed HepG2 cells. Gray and full columns represent the cell proliferation activity of eIF3I-overexpressed and vector only HepG2 transfectants, respectively, treated with various doses (0∼10 μM) of sorafenib for 2 days.|
|HEP_26352_sm_SuppTab1.doc||105K||Supporting Information Table 1. Clinical features and immunohistochemistry results of eIF3I and pAKT1 antibodies of 59 HCC patients.|
|HEP_26352_sm_SuppInfo.doc||88K||Supporting Information Figure 1.|
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