Aging & Longevity

BMAL1 downregulation exacerbates age-related nonalcoholic steatohepatitis by promoting NLRP3 inflammasome activation via HIF-1ɑ-mediated glycolysis.

TL;DR

BMAL1 downregulation under aging and HFD conditions promotes NASH progression by binding to HIF-1α and modulating the glycolysis-NLRP3 inflammasome axis.

Key Findings

Aged HFD-fed mice exhibited more severe NASH phenotypes than young HFD-fed mice.

  • Aged mice were 18 months old and young mice were 6 weeks old; both groups were fed a high-fat diet (HFD) for 16 weeks to induce NASH.
  • Aged HFD-fed mice showed elevated NLRP3 inflammasome activity, enhanced glycolysis, and reduced BMAL1 expression compared to young HFD-fed mice.
  • Aged mice displayed more pronounced lipid accumulation, inflammation, oxidative stress, and fibrosis in liver tissue.

Transcriptomic analysis identified NLRP3-related signaling and circadian rhythm pathways as central contributors to age-specific NASH pathogenesis.

  • Gene expression profiling of liver tissue was performed using RNA sequencing to identify molecular signatures.
  • Both NLRP3-related signaling pathways and circadian rhythm pathways were highlighted as key differentially regulated pathways in aged versus young HFD-fed mice.
  • BMAL1, a core circadian rhythm gene, was identified as downregulated in aged HFD-fed mice.

BMAL1 directly bound to HIF-1α, thereby suppressing glycolysis in hepatocytes.

  • The interaction between BMAL1 and HIF-1α was validated using molecular docking and co-immunoprecipitation (Co-IP) assays.
  • BMAL1 overexpression in senescent NASH cells significantly downregulated HIF-1α-mediated glycolytic activity.
  • Treatment with the HIF-1α inhibitor 2-methoxyestradiol (2-ME2) phenocopied the effects of BMAL1 overexpression on glycolysis suppression.

BMAL1 overexpression combined with glycolysis or HIF-1α inhibition significantly attenuated NLRP3 inflammasome activation and NASH-related pathologies in senescent hepatocytes.

  • In vitro, BMAL1 overexpression plasmids were transfected into AML-12 cells co-treated with H2O2 and free fatty acid (FFA) to model senescent NASH.
  • Treatment with 2-deoxy-D-glucose (2-DG, a glycolysis inhibitor) or 2-methoxyestradiol (2-ME2, a HIF-1α inhibitor) alongside BMAL1 overexpression significantly downregulated NLRP3 expression.
  • Combined interventions attenuated lipid accumulation, inflammation, oxidative stress, and fibrosis in senescent NASH cells.

Hepatocyte-specific BMAL1 overexpression in aged HFD-fed mice inhibited glycolysis and NLRP3 activation, resulting in improvement of NASH-related pathologies.

  • Hepatocyte-specific BMAL1 overexpression was achieved in aged HFD-fed mice through adeno-associated virus serotype 8 (AAV8) delivery.
  • AAV8-mediated BMAL1 overexpression markedly inhibited glycolysis in liver tissue of aged HFD-fed mice.
  • NLRP3 inflammasome activation was reduced following hepatocyte-specific BMAL1 restoration, and NASH-related pathologies including lipid accumulation, inflammation, and fibrosis were improved.

A senescence-associated cellular model of NASH was established using co-treatment of murine hepatocyte AML-12 cells with H2O2 and free fatty acid (FFA).

  • AML-12 murine hepatocytes were used as the in vitro model.
  • H2O2 was used to induce cellular senescence and FFA was used to induce steatosis, together replicating an aged NASH cellular environment.
  • This model was used to test the effects of BMAL1 overexpression and pharmacological inhibition of glycolysis and HIF-1α.

Epidemiological evidence indicates higher incidence and mortality rate of NASH in the elderly population compared to younger groups.

  • The study cites epidemiological studies demonstrating age-related differences in NASH incidence and mortality.
  • The mechanisms underlying age-related exacerbation of NASH were described as poorly understood prior to this study.

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Citation

Ren Y, Lv D, Chen J, Chen W, Chen C, Zhang L, et al.. (2026). BMAL1 downregulation exacerbates age-related nonalcoholic steatohepatitis by promoting NLRP3 inflammasome activation via HIF-1ɑ-mediated glycolysis.. Free radical biology & medicine. https://doi.org/10.1016/j.freeradbiomed.2026.01.058