共 45 条
SIRT2 regulates tumour hypoxia response by promoting HIF-1α hydroxylation
被引:108
作者:

Seo, K-S
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Chungnam Natl Univ, Sch Med, Dept Biochem, Taejon 301747, South Korea Chungnam Natl Univ, Sch Med, Dept Biochem, Taejon 301747, South Korea

Park, J-H
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Chungnam Natl Univ, Sch Med, Dept Biochem, Taejon 301747, South Korea Chungnam Natl Univ, Sch Med, Dept Biochem, Taejon 301747, South Korea

Heo, J-Y
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机构:
Chungnam Natl Univ, Sch Med, Dept Biochem, Taejon 301747, South Korea
Chungnam Natl Univ, Sch Med, Infect Signaling Network Res Ctr, Taejon 301747, South Korea Chungnam Natl Univ, Sch Med, Dept Biochem, Taejon 301747, South Korea

Jing, K.
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Chungnam Natl Univ, Sch Med, Dept Biochem, Taejon 301747, South Korea
Chungnam Natl Univ, Sch Med, Infect Signaling Network Res Ctr, Taejon 301747, South Korea Chungnam Natl Univ, Sch Med, Dept Biochem, Taejon 301747, South Korea

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Min, K-N
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KT&G Life Sci Corp R&D Ctr, Suwon, South Korea Chungnam Natl Univ, Sch Med, Dept Biochem, Taejon 301747, South Korea

Kim, C.
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Korea Adv Inst Sci & Technol, Natl Res Lab Vasc Biol, Taejon 305701, South Korea
Korea Adv Inst Sci & Technol, Grad Sch Med Sci & Engn, Taejon 305701, South Korea Chungnam Natl Univ, Sch Med, Dept Biochem, Taejon 301747, South Korea

Koh, G. Y.
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Korea Adv Inst Sci & Technol, Natl Res Lab Vasc Biol, Taejon 305701, South Korea
Korea Adv Inst Sci & Technol, Grad Sch Med Sci & Engn, Taejon 305701, South Korea Chungnam Natl Univ, Sch Med, Dept Biochem, Taejon 301747, South Korea

Lim, K.
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Chungnam Natl Univ, Sch Med, Dept Biochem, Taejon 301747, South Korea
Chungnam Natl Univ, Sch Med, Infect Signaling Network Res Ctr, Taejon 301747, South Korea
Chungnam Natl Univ, Sch Med, Canc Res Inst, Taejon 301747, South Korea Chungnam Natl Univ, Sch Med, Dept Biochem, Taejon 301747, South Korea

Kang, G-Y
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Diatech Korea Co Ltd, Seoul, South Korea Chungnam Natl Univ, Sch Med, Dept Biochem, Taejon 301747, South Korea

Lee, J. Uee
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Catholic Univ, St Marys Hosp, Dept Pathol, Taejon, South Korea Chungnam Natl Univ, Sch Med, Dept Biochem, Taejon 301747, South Korea

Yim, Y-H
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Korea Res Inst Standard & Sci, Taejon, South Korea Chungnam Natl Univ, Sch Med, Dept Biochem, Taejon 301747, South Korea

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Kwak, T-H
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KT&G Life Sci Corp R&D Ctr, Suwon, South Korea Chungnam Natl Univ, Sch Med, Dept Biochem, Taejon 301747, South Korea

Kweon, G. R.
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机构:
Chungnam Natl Univ, Sch Med, Dept Biochem, Taejon 301747, South Korea Chungnam Natl Univ, Sch Med, Dept Biochem, Taejon 301747, South Korea
机构:
[1] Chungnam Natl Univ, Sch Med, Dept Biochem, Taejon 301747, South Korea
[2] Chungnam Natl Univ, Sch Med, Infect Signaling Network Res Ctr, Taejon 301747, South Korea
[3] KT&G Life Sci Corp R&D Ctr, Suwon, South Korea
[4] Korea Adv Inst Sci & Technol, Natl Res Lab Vasc Biol, Taejon 305701, South Korea
[5] Korea Adv Inst Sci & Technol, Grad Sch Med Sci & Engn, Taejon 305701, South Korea
[6] Chungnam Natl Univ, Sch Med, Canc Res Inst, Taejon 301747, South Korea
[7] Diatech Korea Co Ltd, Seoul, South Korea
[8] Catholic Univ, St Marys Hosp, Dept Pathol, Taejon, South Korea
[9] Korea Res Inst Standard & Sci, Taejon, South Korea
[10] Chungnam Natl Univ, Sch Med, Dept Internal Med, Taejon 301747, South Korea
来源:
基金:
新加坡国家研究基金会;
关键词:
INDUCIBLE FACTOR-1-ALPHA;
OXIDOREDUCTASE;
METABOLISM;
HIF1-ALPHA;
DEGRADATION;
ACTIVATION;
PROTEIN;
ACETYLATION;
SUPPRESSION;
OXIDATION;
D O I:
10.1038/onc.2014.76
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
Hypoxia-inducible factor-1 alpha (HIF-1 alpha) is a transcription factor that has a central role in the regulation of tumour metabolism under hypoxic conditions. HIF-1 alpha stimulates glycolytic energy production and promotes tumour growth. Sirtuins are NAD(+)-dependent protein deacetylases that regulate cellular metabolism in response to stress; however, their involvement in the hypoxic response remains unclear. In this study, it is shown that SIRT2-mediated deacetylation of HIF-1 alpha regulates its stability in tumour cells. SIRT2 overexpression destabilized HIF-1 alpha under hypoxic conditions, whereas HIF-1 alpha protein levels were high in SIRT2-deficient cells. SIRT2 directly interacted with HIF-1 alpha and deacetylated Lys709 of HIF-1 alpha. Deacetylation of HIF-1 alpha by SIRT2 resulted in increased binding affinity for prolyl hydroxylase 2, a key regulator of HIF-1a stability, and increased HIF-1 alpha hydroxylation and ubiquitination. Moreover, a pharmacological agent that increased the intracellular NAD(+)/NADH ratio led to the degradation of HIF-1 alpha by increasing SIRT2-mediated deacetylation and subsequent hydroxylation. These findings suggest that SIRT2-mediated HIF-1 alpha deacetylation is critical for the destablization of HIF-1 alpha and the hypoxic response of tumour cells.
引用
收藏
页码:1354 / 1362
页数:9
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Kimura, N
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Shirayoshi, Y
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Kamitani, H
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Watanabe, T
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Ohama, E
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Tahimic, CGT
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Kurimasa, A
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Oshimura, M
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