Glycolytic Suppression: How PTEN Tames the Progression of Endometriosis

In: Discovery Medicine · 2026 · vol. 38(213) · doi:10.24976/discov.med.202638213.253 · W7223317542
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PTEN downregulation in endometriosis correlates with hyperactive glycolysis, as its loss promotes ectopic lesion growth and malignant cell behaviors via enhanced glycolytic metabolism.

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This study investigates the role of PTEN in regulating glycolysis and disease progression in endometriosis. Researchers found that PTEN is downregulated in ectopic lesions, where it inversely correlates with key glycolytic regulators like Glut1 and PDK1. Experimental models demonstrated that suppressing PTEN activity enhances cell proliferation, migration, invasion, and glycolytic metabolism both in vitro and in vivo. These findings suggest that PTEN loss drives endometriotic lesion growth by promoting hyperactive glycolysis. This paper is centrally about endometriosis — specifically exploring the molecular mechanisms linking PTEN suppression to enhanced glycolytic activity in ectopic lesions.

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Abstract

Background: Endometriosis (EMs) is a common benign gynecological disorder affecting women of reproductive age, characterized by ectopic endometrial growth, invasion, and periodic bleeding. Mounting evidence indicates that metabolic reprogramming, particularly hyperactive glycolysis, critically promotes the pathological progression of EMs. Phosphatase and tensin homolog (PTEN), a pivotal tumor suppressor and endometrial housekeeping gene, is frequently downregulated in EMs; however, its precise regulatory mechanism linking glycolysis and EMs pathogenesis remains largely unexplored.Methods: Bioinformatics analysis was applied to characterize PTEN expression and its correlation with glycolysis-associated genes in EMs. In vitro, PTEN was knocked down in human normal endometrial stromal cells (NESC) and overexpressed in human endometriotic epithelial cells (12Z), while both cell types were treated with the PTEN inhibitor SF1670, followed by phenotypic and glycolytic assessments. In vivo, an EMs mouse model was used to verify the effects of PTEN inhibition on ectopic lesion development and glycolytic metabolism by pathological and molecular detection.Results: PTEN expression was significantly downregulated in ectopic lesions compared with normal and eutopic counterparts, and exhibited an opposite expression trend to the core glycolytic regulators glucose transporter type 1 (Glut1) and pyruvate dehydrogenase kinase 1 (PDK1). In cellular experiments, endogenous PTEN protein levels were also markedly lower in 12Z cells than in NESC cells. Functional experiments demonstrated that loss of PTEN via knockdown or pharmacological inhibition with SF1670 markedly reinforced cell proliferation, migration, invasion, and glycolytic metabolism, whereas PTEN overexpression effectively alleviated these malignant biological behaviors. In line with in vitro observations, in vivo studies further demonstrated that SF1670-mediated PTEN inhibition significantly promoted ectopic lesion growth, primarily by suppressing PTEN expression, and this effect was accompanied by enhanced glycolytic activity in lesion tissues.Conclusion: This study reveals that PTEN expression correlates with EMs progression and is inversely associated with glycolytic activity, suggesting a potential PTEN-glycolysis association that may serve as a target for diagnosis and therapy.
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Abstract

Background: Endometriosis (EMs) is a common benign gynecological disorder affecting women of reproductive age, characterized by ectopic endometrial growth, invasion, and periodic bleeding. Mounting evidence indicates that metabolic reprogramming, particularly hyperactive glycolysis, critically promotes the pathological progression of EMs. Phosphatase and tensin homolog (PTEN), a pivotal tumor suppressor and endometrial housekeeping gene, is frequently downregulated in EMs; however, its precise regulatory mechanism linking glycolysis and EMs pathogenesis remains largely unexplored.

Methods

Bioinformatics analysis was applied to characterize PTEN expression and its correlation with glycolysis-associated genes in EMs. In vitro, PTEN was knocked down in human normal endometrial stromal cells (NESC) and overexpressed in human endometriotic epithelial cells (12Z), while both cell types were treated with the PTEN inhibitor SF1670, followed by phenotypic and glycolytic assessments. In vivo, an EMs mouse model was used to verify the effects of PTEN inhibition on ectopic lesion development and glycolytic metabolism by pathological and molecular detection.

Results

PTEN expression was significantly downregulated in ectopic lesions compared with normal and eutopic counterparts, and exhibited an opposite expression trend to the core glycolytic regulators glucose transporter type 1 (Glut1) and pyruvate dehydrogenase kinase 1 (PDK1). In cellular experiments, endogenous PTEN protein levels were also markedly lower in 12Z cells than in NESC cells. Functional experiments demonstrated that loss of PTEN via knockdown or pharmacological inhibition with SF1670 markedly reinforced cell proliferation, migration, invasion, and glycolytic metabolism, whereas PTEN overexpression effectively alleviated these malignant biological behaviors. In line with in vitro observations, in vivo studies further demonstrated that SF1670-mediated PTEN inhibition significantly promoted ectopic lesion growth, primarily by suppressing PTEN expression, and this effect was accompanied by enhanced glycolytic activity in lesion tissues.

Conclusion

This study reveals that PTEN expression correlates with EMs progression and is inversely associated with glycolytic activity, suggesting a potential PTEN-glycolysis association that may serve as a target for diagnosis and therapy.

Keywords

- endometriosis - phosphatase and tensin homolog - glycolysis - lactate dehydrogenase - proliferation - migration - invasion

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