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Author

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

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Activation of AMP-activated Protein Kinase Is Essential for Lysophosphatidic Acid-induced Cell Migration in Ovarian Cancer Cells

Cited 16 times inthomson ciCited 16 times inthomson ci
Title
Activation of AMP-activated Protein Kinase Is Essential for Lysophosphatidic Acid-induced Cell Migration in Ovarian Cancer Cells
Author
Kim, Eung-KyunPark, Ji-ManLim, SeyoungChoi, Jung WoongKim, Hyeon SooSeok, HeonSeo, Jeong KonOh, KeunheeLee, Dong-SupKim, Kyong TaiRyu, Sung HoSuh, Pann-Ghill
Keywords
AMP-activated protein kinase; Biological functions; Calcium/calmodulin-dependent protein kinase; Cancer cells; Cell migration; Cytoskeletal dynamics; Lung metastasis; Lysophosphatidic acid; Membrane dynamics; Ovarian cancer cells; Ovarian cancers; Phospholipase C; Signaling pathways; Stimulatory effects; Tumor metastasis
Issue Date
201107
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, v.286, no.27, pp.24036 - 24045
Abstract
Lysophosphatidic acid (LPA) is a bioactive phospholipid that affects various biological functions, such as cell proliferation, migration, and survival, through LPA receptors. Among them, the motility of cancer cells is an especially important activity for invasion and metastasis. Recently, AMP-activated protein kinase (AMPK), an energy-sensing kinase, was shown to regulate cell migration. However, the specific role of AMPK in cancer cell migration is unknown. The present study investigated whether LPA could induce AMPK activation and whether this process was associated with cell migration in ovarian cancer cells. We found that LPA led to a striking increase in AMPK phosphorylation in pathways involving the phospholipase C-beta 3 (PLC-beta 3) and calcium/calmodulin-dependent protein kinase kinase beta (CaMKK beta) in SKOV3 ovarian cancer cells. siRNA-mediated knockdown of AMPK beta 1, PLC-beta 3, or (CaMKK beta) impaired the stimulatory effects of LPA on cell migration. Furthermore, we found that knockdown of AMPK beta 1 abrogated LPA-induced activation of the small GTPase RhoA and ezrin/radixin/moesin proteins regulating membrane dynamics as membrane-cytoskeleton linkers. In ovarian cancer xenograft models, knockdown of AMPK significantly decreased peritoneal dissemination and lung metastasis. Taken together, our results suggest that activation of AMPK by LPA induces cell migration through the signaling pathway to cytoskeletal dynamics and increases tumor metastasis in ovarian cancer.
URI
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DOI
http://dx.doi.org/10.1074/jbc.M110.209908
ISSN
0021-9258
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