International Journal of Oncology · 2010 · 56 citations · 44 references
MedicineOncologyPharmacologyMolecular OncologyOncogenesProteomicsCancer BiomarkersCancer ProgressionCancer ProteomicsMalignant NeoplasmsOncogene ActivationTumor BiologyAnchorage-independent SurvivalAnticancer ActivityCancer Proteome ProfilingMass Spectrometry ProteomicsProteomic AlterationsProteomic IdentificationTumor Cell Survival PathwaysTumor Proteomics
Triterpenoids are implicated in the chemoprevention of various cancers. Current challenge is to define the molecular mechanism underlying the chemopreventive activity of triterpenoids. This study was designed to characterize the intracellular proteins regulated by astragaloside IV, the major active triterpenoid in Radix Astragali. Upon the treatment with astragaloside IV, human hepatocellular carcinoma HepG2 cells were evaluated for the colonogenic survival and anchorage-independent growth. The cellular proteins of treated and untreated cells were resolved by 2-D polyacrylamide gel electrophoresis. The protein spots mostly altered by drug treatment were identified by mass spectrometry and subsequently verified by Western blotting using specific antibodies and RT-PCR technique using specific DNA primers. We found that astragaloside IV attenuated the colonogenic survival and anchorage-independent growth of cancer cells. Based on the proteomic profiles, top 14 upregulated and 13 down-regulated protein spots were subjected to mass spectrometric analysis. As an example, Vav3.1 belongs to the oncogene Vav family, which is implicated in tumorigenesis. Vav3.1 expression was down-regulated by astragaloside IV in a dose- and time-dependent manner. Down-regulation of Vav3.1 was highly correlated with the suppression of cell malignant transform. Thus, astragaloside IV may elicit anticancer activity via down-regulating the expression of oncogenes such as Vav3.1.
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Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks
Jesper V. Olsen, Blagoy Blagoev, Florian Gnad et al. · Cell · 2006 · 3.6K citations · Full text
LTRPC7 is a Mg·ATP-regulated divalent cation channel required for cell viability
Monica J. S. Nadler, Meredith C. Hermosura, Kazunori Inabe et al. · Nature · 2001 · 931 citations
The TRPM7 channel is inactivated by PIP2 hydrolysis
Loren W. Runnels, Lixia Yue, David E. Clapham · Nature Cell Biology · 2002 · 517 citations