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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Huo, Xiaodong Kong, Qingbin Wang, Jiao Luo, Ting Shao, Ting Hua, Hui Liu, Shu Jiang, Yangfu |
| Description | Author Affiliation: Huo X ( From the State Key Laboratory of Biotherapy, Section of Oncogene, West China Hospital, Sichuan University, Chengdu 610041.); Liu S ( From the State Key Laboratory of Biotherapy, Section of Oncogene, West China Hospital, Sichuan University, Chengdu 610041.); Shao T ( From the State Key Laboratory of Biotherapy, Section of Oncogene, West China Hospital, Sichuan University, Chengdu 610041.); Hua H ( the Laboratory of Stem Cell Biology, West China Hospital, Chengdu 610041.); Kong Q ( From the State Key Laboratory of Biotherapy, Section of Oncogene, West China Hospital, Sichuan University, Chengdu 610041.); Wang J ( the School of Basic Medicine, Chengdu University of Traditional Chinese Medicine, Chengdu 610075, and.); Luo T ( the Cancer Center, West China Hospital, Chengdu 610041, China.); Jiang Y ( From the State Key Laboratory of Biotherapy, Section of Oncogene, West China Hospital, Sichuan University, Chengdu 610041, jyangfu@scu.edu.cn.) |
| Abstract | Glycogen synthase kinase-3 (GSK3) has either tumor-suppressive roles or pro-tumor roles in different types of human tumors. A number of GSK3 targets in diverse signaling pathways have been uncovered, such as tuberous sclerosis complex subunit 2 and ß-catenin. The O subfamily of forkhead/winged helix transcription factors (FOXO) is known as tumor suppressors that induce apoptosis. In this study, we find that FOXO binds to type I insulin-like growth factor receptor (IGF-IR) promoter and stimulates its transcription. GSK3 positively regulates the transactivation activity of FOXO and stimulates IGF-IR expression. Although kinase-dead GSK3ß cannot up-regulate IGF-IR, the constitutively active GSK3ß induces IGF-IR expression in a FOXO-dependent manner. Serum starvation or Akt inhibition leads to an increase in IGF-IR expression, which could be blunted by GSK3 inhibition. GSK3ß knockdown or GSK3 inhibitor suppresses IGF-I-induced IGF-IR, Akt, and ERK1/2 phosphorylation. Moreover, knockdown of GSK3ß or FOXO1/3/4 leads to a decrease in cellular proliferation and abrogates IGF-I-induced hepatoma cell proliferation. These results suggest that GSK3 and FOXO may positively regulate IGF-I signaling and hepatoma cell proliferation. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 36 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-09-05 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Forkhead Transcription Factors Genetics Glycogen Synthase Kinase 3 Receptor, IGF Type 1 Transcription Factors Blotting, Western Cell Line, Tumor Cell Proliferation Drug Effects Extracellular Signal-Regulated MAP Kinases Metabolism Gene Expression Regulation, Neoplastic Insulin-Like Growth Factor I Pharmacology Models, Genetic Phosphorylation Promoter Regions, Genetic Protein Binding Proto-Oncogene Proteins C-akt RNA Interference Reverse Transcriptase Polymerase Chain Reaction Transcriptional Activation Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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