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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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Quercetin Suppresses HeLa Cell Viability via AMPK-Induced HSP70 and EGFR Down-Regulation

Cited 32 times inthomson ciCited 34 times inthomson ci
Title
Quercetin Suppresses HeLa Cell Viability via AMPK-Induced HSP70 and EGFR Down-Regulation
Author
Jung, Jin HeeLee, Jeong OkKim, Ji HaeLee, Soo KyungYou, Ga YoungPark, Sun HwaPark, Ji ManKim, Eung-KyunSuh, Pann-GhillAn, Jin KyungKim, Hyeon Soo
Keywords
HEAT-SHOCK-PROTEIN; STRESS-INDUCED APOPTOSIS; PRIMARY COLORECTAL TUMORS; ESTROGEN-BINDING SITES; N-TERMINAL KINASE; BREAST-CANCER; CARCINOMA CELLS; ENERGY STATUS; KEY SENSOR; EXPRESSION
Issue Date
201005
Publisher
WILEY-BLACKWELL
Citation
JOURNAL OF CELLULAR PHYSIOLOGY, v.223, no.2, pp.408 - 414
Abstract
Quercetin, an anti-oxidant flavonoid that is widely distributed in the plant kingdom, has been suggested to have chemopreventive effects on cancer cells, although the mechanism is not completely understood. In this study, we found that quercetin increased the phosphorylation of AMP-activated protein kinase (AMPK) and downstream acetyl-CoA carboxylase (ACC) and suppressed the viability of HeLa cells. AICAR, an AMPK activator, and quercetin down-regulated heat shock protein (HSP)70 and increased the activity of the pro-apoptotic effector, caspase 3. Knock-down of AMPK blocked quercetin-mediated HSP70 down-regulation. Moreover, knock-down of HSP70 enhanced quercetin-mediated caspase 3 activation. Furthermore, quercetin sustained epidermal growth factor receptor (EGFR) activation by suppressing the phosphatases, PP2a and SHP-2. Finally, quercetin increased the interaction between EGFR and Cbl, and also induced the tyrosine phosphorylation of Cbl. Together, these results suggest that quercetin may have anti-tumor effects on HeLa cells via AMPK-induced HSP70 and down-regulation of EGFR.
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DOI
http://dx.doi.org/10.1002/jcp.22049
ISSN
0021-9541
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