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Adiponectin-Activated AMPK Stimulates Dephosphorylation of AKT through Protein Phosphatase 2A Activation

Authors
Kim, Kun-yongBaek, AhmiHwang, Ji-EunChoi, Yeon A.Jeong, JoonLee, Myeong-SokCho, Dea HoLim, Jong-SeokKim, Keun IlYang, Young
Issue Date
May-2009
Publisher
AMER ASSOC CANCER RESEARCH
Citation
CANCER RESEARCH, v.69, no.9, pp 4018 - 4026
Pages
9
Journal Title
CANCER RESEARCH
Volume
69
Number
9
Start Page
4018
End Page
4026
URI
https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/13759
DOI
10.1158/0008-5472.CAN-08-2641
ISSN
0008-5472
1538-7445
Abstract
Low serum levels of adiponectin are a high risk factor for various types of cancer. Although adiponectin inhibits proliferation and metastasis of breast cancer cells, the underlying molecular mechanisms remain obscure. In this study, we show that adiponectin-activated AMPK reduces the invasiveness of MDA-MB-231 cells by stimulating dephosphorylation of AKT by increasing protein phosphatase 2A (PP2A) activity. Among the various regulatory B56 subunits, B56 gamma was directly phosphorylated by AMPK at Ser(298) and Ser(336), leading to an increase of PP2A activity through dephosphorylation of PP2Ac at Tyr(307). We also show that both the blood levels of adiponectin and the tissue levels of PP2A activity were decreased in breast cancer patients and that the direct administration of adiponectin into tumor tissues stimulates PP2A activity. Taken together, these findings show that adiponectin, derived from adipocytes, negatively regulates the invasiveness of breast cancer cells by activating the tumor suppressor PP2A. [Cancer Res 2009;69(9):4018-26]
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대학 > 기초교양대학 > 기초교양학부 > 1. Journal Articles
이과대학 > 생명시스템학부 > 1. Journal Articles

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