Abstract 6868: Targeting glycolysis in cancer

Abstract The reprogramming of metabolism to increase reliance on glycolysis is a recognized phenomenon in tumors and is frequently driven by oncogenic mutations. In breast cancer, one of these genetic alterations, the increased activity of the human epidermal growth factor receptor 2 (HER2/ErbB2) is observed in ∼30% of tumors. HER2 activate a variety of downstream effectors (e.g. Ras, HIF-1α) that stimulate glycolysis, in part through the activity of a family of enzymes, the 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatases (PFKFB1-4). The PFKFBs produce fructose-2, 6-bisphosphate (F26BP) which activates a rate-limiting glycolytic enzyme, 6-phosphofructo-1-kinase (PFK-1) and therefore important regulators of glycolysis. Preliminary data from our laboratory have determined that the PFKFB4 enzyme was highly expressed in a series of patient - derived HER2+ breast tumors relative to normal breast and additionally found higher expression in paired metastases. We found that silencing PFKFB4 expression in HER2+ breast cancer cells caused a marked reduction in their glycolytic flux and survival. Through in silico screening and optimization, we have identified a small molecule inhibitor of PFKFB4 that selectively inhibits PFKFB4 activity with a resultant decrease in glycolysis and cancer cell growth. We have found that PFKFB4 inhibition also caused a significant decrease in the invasion and migration of HER2+ breast cancer cells in vitro, importantly at concentrations well below levels that affect cell viability. We have now examined the effects of PFKFB4 inhibition in a relevant transgenic model of HER2-driven spontaneous mammary tumor formation and have found that the inhibitor caused marked suppression in the growth of HER2+ mammary tumors without signs of systemic toxicity. We additionally have found in preliminary studies that PFKFB4 inhibition decreased the development of metastases in these mice. Taken together, our data strongly support the further evaluation of these inhibitors as a potential strategy for the successful treatment of HER2+ breast cancer. Citation Format: Sucheta Telang, Renita Ranjan, Joseph Burlison. Targeting glycolysis in cancer [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2025; Part 1 (Regular Abstracts); 2025 Apr 25-30; Chicago, IL. Philadelphia (PA): AACR; Cancer Res 2025;85(8_Suppl_1):Abstract nr 6868.

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Publication Details

Journal
Cancer Research
Published
2025-04-21
DOI
https://doi.org/10.1158/1538-7445.am2025-6868
Primary Topic
Cancer, Hypoxia, and Metabolism
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article
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article

Abstract 6868: Targeting glycolysis in cancer

Cancer Research
Cancer, Hypoxia, and Metabolism
article

Abstract 6868: Targeting glycolysis in cancer

article en

Abstract

Abstract The reprogramming of metabolism to increase reliance on glycolysis is a recognized phenomenon in tumors and is frequently driven by oncogenic mutations. In breast cancer, one of these genetic alterations, the increased activity of the human epidermal growth factor receptor 2 (HER2/ErbB2) is observed in ∼30% of tumors. HER2 activate a variety of downstream effectors (e.g. Ras, HIF-1α) that stimulate glycolysis, in part through the activity of a family of enzymes, the 6-phosphofructo-2-kinase/fructose-2, 6-bisphosphatases (PFKFB1-4). The PFKFBs produce fructose-2, 6-bisphosphate (F26BP) which activates a rate-limiting glycolytic enzyme, 6-phosphofructo-1-kinase (PFK-1) and therefore important regulators of glycolysis. Preliminary data from our laboratory have determined that the PFKFB4 enzyme was highly expressed in a series of patient - derived HER2+ breast tumors relative to normal breast and additionally found higher expression in paired metastases. We found that silencing PFKFB4 expression in HER2+ breast cancer cells caused a marked reduction in their glycolytic flux and survival. Through in silico screening and optimization, we have identified a small molecule inhibitor of PFKFB4 that selectively inhibits PFKFB4 activity with a resultant decrease in glycolysis and cancer cell growth. We have found that PFKFB4 inhibition also caused a significant decrease in the invasion and migration of HER2+ breast cancer cells in vitro, importantly at concentrations well below levels that affect cell viability. We have now examined the effects of PFKFB4 inhibition in a relevant transgenic model of HER2-driven spontaneous mammary tumor formation and have found that the inhibitor caused marked suppression in the growth of HER2+ mammary tumors without signs of systemic toxicity. We additionally have found in preliminary studies that PFKFB4 inhibition decreased the development of metastases in these mice. Taken together, our data strongly support the further evaluation of these inhibitors as a potential strategy for the successful treatment of HER2+ breast cancer. Citation Format: Sucheta Telang, Renita Ranjan, Joseph Burlison. Targeting glycolysis in cancer [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2025; Part 1 (Regular Abstracts); 2025 Apr 25-30; Chicago, IL. Philadelphia (PA): AACR; Cancer Res 2025;85(8_Suppl_1):Abstract nr 6868.

Cancer ResearchVol. 85(8_Supplement_1)
University of Louisville (US)
Good health and well-being
Openalex Percentile: Top 50%
Cancer, Hypoxia, and Metabolism
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