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Updated: Sep 11, 2025

Intracellular Phosphoflow Cytometry of Acute Myeloid Leukemia Patient-Derived Xenotransplants
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PRMT1-mediated metabolic reprogramming promotes leukemogenesis.

Hairui Su1, Yong Sun2,3, Han Guo4

  • 1Department of Biochemistry and Molecular Genetics, The University of Alabama at Birmingham, School of Medicine, Birmingham, United States.

Elife
|August 13, 2025
PubMed
Summary
This summary is machine-generated.

Protein arginine methyltransferase 1 (PRMT1) drives acute megakaryocytic leukemia (AMKL) by boosting glycolysis and hindering fatty acid oxidation. Inhibiting PRMT1 or targeting glucose metabolism offers therapeutic strategies for this cancer.

Keywords:
CPT1APRMT1cancer biologycell biologyfatty acidsglycolysisleukemiamitochondriamouse

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Area of Science:

  • Oncology
  • Cancer Metabolism
  • Molecular Biology

Background:

  • Protein arginine methyltransferase 1 (PRMT1) is frequently overexpressed in cancers, correlating with poor patient survival.
  • Acute megakaryocytic leukemia (AMKL) is a subtype of acute myeloid leukemia with specific molecular drivers.
  • Heterogeneity in PRMT1 expression within leukemia cell lines suggests distinct subpopulations may drive disease progression.

Purpose of the Study:

  • To investigate the role of PRMT1 in AMKL pathogenesis and its impact on cellular metabolism.
  • To evaluate the therapeutic potential of PRMT1 inhibition in a preclinical AMKL model.
  • To elucidate the metabolic pathways regulated by PRMT1 in leukemia cells.

Main Methods:

  • Utilized a murine AMKL cell line (6133) with heterogeneous Prmt1 expression.
  • Employed a PRMT1 inhibitor (MS023) for therapeutic intervention.
  • Conducted Seahorse analysis to assess cellular respiration and glycolysis.
  • Performed metabolomic and flow cytometry analyses to evaluate lipid metabolism.
  • Administered 2-deoxy-D-glucose and performed gene rescue experiments.

Main Results:

  • High PRMT1 expression in a subpopulation of AMKL cells was essential for leukemia development in vivo.
  • PRMT1 inhibition with MS023 effectively treated PRMT1-driven AMKL.
  • PRMT1 upregulated glycolysis (increased extracellular acidification rate, glucose consumption, lactate production) and downregulated fatty acid oxidation (decreased oxygen consumption rate, reduced CPT1A expression).
  • PRMT1 promoted intracellular lipid accumulation.
  • Glucose analog treatment delayed AMKL progression and induced differentiation; Cpt1a re-expression rescued proliferation.

Conclusions:

  • PRMT1 promotes AMKL proliferation by enhancing glycolysis and suppressing fatty acid oxidation.
  • Targeting PRMT1 or glucose metabolism represents a promising therapeutic strategy for AMKL.