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10.1158/0008-5472.CAN-16-0401

http://scihub22266oqcxt.onion/10.1158/0008-5472.CAN-16-0401
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C5082982!5082982!27261507
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suck abstract from ncbi


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pmid27261507      Cancer+Res 2016 ; 76 (14): 4259-69
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  • Definition of a novel feed-forward mechanism for glycolysis-HIF1? signaling in hypoxic tumors highlights adolase A as a therapeutic target #MMPMID27261507
  • Grandjean G; De Jong P; James B; Koh MY; Lemos R; Kingston J; Aleshin A; Bankston LA; Miller CP; Cho EJ; Edupuganti R; Devkota A; Stancu G; Liddington RC; Dalby K; Powis G
  • Cancer Res 2016[Jul]; 76 (14): 4259-69 PMID27261507show ga
  • The hypoxia-inducible transcription factor HIF1? drives expression of many glycolytic enzymes. Here we show that hypoxic glycolysis, in turn, increases HIF1? transcriptional activity and stimulates tumor growth, revealing a novel feed-forward mechanism of glycolysis-HIF1? signaling. Negative regulation of HIF1? by AMPK1 is bypassed in hypoxic cells, due to ATP elevation by increased glycolysis, thereby preventing phosphorylation and inactivation of the HIF1? transcriptional co-activator p300. Notably, of the HIF1? activated glycolytic enzymes we evaluated by gene silencing, aldolase A (ALDOA) blockade produced the most robust decrease in glycolysis, HIF-1 activity and cancer cell proliferation. Furthermore, either RNAi-mediated silencing of ALDOA or systemic treatment with a specific small molecule inhibitor of aldolase A was sufficient to increase overall survival in a xenograft model of metastatic breast cancer. In establishing a novel glycolysis-HIF-1? feed-forward mechanism in hypoxic tumor cell, our results also provide a preclinical rationale to develop aldolase A inhibitors as a generalized strategy to treat intractable hypoxic cancer cells found widely in most solid tumors.
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