Impairment of HIF-1α-mediated metabolic adaption by NRF2-silencing in breast cancer cells
Identifieur interne : 000742 ( Main/Exploration ); précédent : 000741; suivant : 000743Impairment of HIF-1α-mediated metabolic adaption by NRF2-silencing in breast cancer cells
Auteurs : Sujin Lee [Corée du Sud] ; Steffanus Pranoto Hallis [Corée du Sud, Indonésie] ; Kyeong-Ah Jung [Corée du Sud] ; Dayoung Ryu [Corée du Sud] ; Mi-Kyoung Kwak [Corée du Sud]Source :
- Redox Biology [ 2213-2317 ] ; 2019.
Abstract
Hypoxia, a common element in the tumor environment, leads to Hypoxia-Inducible Factor-1α (HIF-1α) stabilization to modulate cellular metabolism as an adaptive response. In a previous study, we showed that inhibition of the nuclear factor erythroid 2-like-2 (NFE2L2; NRF2), a master regulator of many genes coping with electrophilic and oxidative stress, elevated the level of
Url:
DOI: 10.1016/j.redox.2019.101210
PubMed: 31078780
PubMed Central: 6514540
Affiliations:
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<front><div type="abstract" xml:lang="en"><p>Hypoxia, a common element in the tumor environment, leads to Hypoxia-Inducible Factor-1α (HIF-1α) stabilization to modulate cellular metabolism as an adaptive response. In a previous study, we showed that inhibition of the nuclear factor erythroid 2-like-2 (NFE2L2; NRF2), a master regulator of many genes coping with electrophilic and oxidative stress, elevated the level of <italic>miR-181c</italic>
and induced mitochondrial dysfunction in colon cancer cells. In this study, we demonstrate that <italic>NRF2</italic>
-silencing hindered HIF-1α accumulation in hypoxic breast cancer cells and subsequently suppressed hypoxia-inducible expression of glycolysis-associated glucose transporter-1, hexokinase-2, pyruvate dehydrogenase kinase-1, and lactate dehydrogenase A. HIF-1α dysregulation in <italic>NRF2</italic>
-silenced cancer cells was associated with <italic>miR-181c</italic>
elevation. Overexpression of <italic>miR-181c</italic>
in breast cancer cells blocked HIF-1α accumulation and diminished hypoxia-inducible levels of glycolysis enzymes, whereas the inhibition of <italic>miR-181c</italic>
in <italic>NRF2</italic>
-silenced cells restored HIF-1α accumulation. In a subsequent metabolomic analysis, hypoxic incubation increased the levels of metabolites involved in glycolysis and activated the pentose phosphate pathway (PPP) in control cells. However, these elevations were less pronounced in <italic>NRF2</italic>
-silenced cells. In particular, hypoxic incubation increased the levels of amino acids, which implies a shift to catabolic metabolism, and the increased levels were higher in control cells than in <italic>NRF2</italic>
-silenced cells. Concurrently, hypoxia activated BCL2 interacting protein 3 (BNIP3)-mediated autophagy in the control cells and <italic>miR-181c</italic>
was found to be involved in this autophagy activation. Taken together, these results show that hypoxia-induced metabolic changes to glycolysis, the PPP, and autophagy are inhibited by <italic>NRF2</italic>
-silencing through <italic>miR-181c</italic>
-mediated HIF-1α dysregulation. Therefore, targeting <italic>NRF2</italic>
/<italic>miR-181c</italic>
could be an effective strategy to counteract HIF-1α-orchestrated metabolic adaptation of hypoxic cancer cells.</p>
</div>
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