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Open Access Research article

Notch1 binds and induces degradation of Snail in hepatocellular carcinoma

Seung-Oe Lim1, Hyeon Seop Kim1, Xiaoyuan Quan1, Sun-Min Ahn1, Hongtae Kim2, David Hsieh1, Je Kyung Seong3 and Guhung Jung1*

Author Affiliations

1 Department of Biological Sciences, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul, 151-747, Korea

2 Department of Biological Science, Sungkyunkwan University, Seobu-ro, Jangan-gu, Suwon, Gyeonggi-do, 110-745, Korea

3 Laboratory of Developmental Biology and Genomics, College of Veterinary Medicine, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul, 151-747, Korea

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BMC Biology 2011, 9:83  doi:10.1186/1741-7007-9-83

Published: 30 November 2011

Additional files

Additional file 1:

Peptides sequence of identified Snail-bound proteins including Snail by mass spectrometry analysis.

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Additional file 2:

Notch1 interacts with Snail. HT-29, Panc-1, or MDA-MB-231 cells were immunostained with anti-Snail and/or anti-Notch1 antibodies and assessed by the Duolink® II assay. Red spots indicate the interaction between the endogenous Snail and Notch1 proteins.

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Additional file 3:

Snail and NICD regulate invasion. (A-C) MEFs (A), Huh7 (B), and Hep3B (C) were infected by MSCV-NICD and/or MSCV-Snail, selected in puromycin, and analyzed for Notch1 and Snail expression by immunoblot with the indicated antibodies. β-actin served as an internal control. (D) Hep3B cells were transfected by Notch1 and/or Snail siRNA, treated with 300 μM H2O2 for 72 h, and analyzed for Notch1 and Snail expression by immunoblot with the indicated antibodies. E-cadherin, which is a Snail target gene, served as a marker of Snail activity. β-actin served as an internal control. (E) Hep3B cells were transfected by Notch1 and/or Snail siRNA, treated with 300 μM H2O2 for 72 h, and analyzed for Notch1 and Snail expression by immunoblot with the indicated antibodies. β-actin served as an internal control.

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