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Hou J.-K.,Shanghai JiaoTong University | Huang Y.,Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education | He W.,Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education | Yan Z.-W.,Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education | And 7 more authors.
Cell Death and Disease | Year: 2014

Adenanthin, a natural diterpenoid isolated from the leaves of Isodon adenanthus, has recently been reported to induce leukemic cell differentiation by targeting peroxiredoxins (Prx) I and II. On the other hand, increasing lines of evidence propose that these Prx proteins would become potential targets to screen drugs for the prevention and treatment of solid tumors. Therefore, it is of significance to explore the potential activities of adenanthin on solid tumor cells. Here, we demonstrate that Prx I protein is essential for the survival of hepatocellular carcinoma (HCC) cells, and adenanthin can kill these malignant liver cells in vitro and xenografts. We also show that the cell death-inducing activity of adenanthin on HCC cells is mediated by the increased reactive oxygen species (ROS) levels. Furthermore, the silencing of Prx I or Prx II significantly enhances the cytotoxic activity of adenanthin on HCC, whereas the ectopic expression of Prx I and Prx II but not their mutants of adenanthin-bound cysteines can rescue adenanthin-induced cytotoxicity in Prxs-silenced HCC cells. Taken together, our results propose that adenanthin targets Prx I/II to kill HCC cells and its therapeutic significance warrants to be further explored in HCC patients. © 2014 Macmillan Publishers Limited. All rights reserved.


Wei Y.,CAS Shanghai Institute of Organic Chemistry | Wang T.,Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education | Liu C.,CAS Shanghai Institute of Organic Chemistry | Zhang Q.,CAS Shanghai Institute of Organic Chemistry | And 4 more authors.
Chinese Journal of Chemistry | Year: 2013

Affinity core-shell magnetic nanoparticles (MNPs) were prepared for identifying the target proteins of drugs in the cell lysate when used in combination with nano-high-performance liquid chromatography tandem mass spectrometry (HPLC-MS/MS)-based shotgun proteomic analysis. A number of new potential targets of cyclosporine A (CsA) could be identified, owing to the high efficacy of the affinity MNPs in drug target identification. To the best of our knowledge, this is the first time to reveal such an abundant target spectrum of CsA. Copyright © 2013 SIOC, CAS, Shanghai & WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.


Xu Y.,CAS Shanghai Institutes for Biological Sciences | Xu Y.,Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education | Li J.,Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education | Zuo Y.,Key Laboratory of Cell Differentiation and Apoptosis of Chinese Ministry of Education | And 4 more authors.
Cancer Letters | Year: 2011

SUMO conjugation emerges as an important mechanism in regulating protein localization, stability and activity. SUMOylation is a dynamic process and can be reversed by a family of sentrin/SUMO-specific proteases (SENPs). However, the biological roles of SENPs in cellular processes are largely unknown. Here, we show that SENP1, a member of SENP family, is overexpressed in most of colon cancer tissues. Silencing of SENP1 expression inhibits cell growth with G1 arrest in vitro and in nude mice and colony formation in colon cancer cell line DLD-1, suggesting that SENP1 is essential for cell growth in the colon cancer cell line. Accordingly, silencing of SENP1 results in upregulation of CDK inhibitors such as p16, p19, p21 and p27. These results suggest that SENP1 might play a role in cell cycle regulation of colon cancer cells. © 2011 Elsevier Ireland Ltd.

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