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Decrease of cellular ATP by dihexanoylglycerol may limit responses to protein kinase C activation.

J Dawson, N T Thompson, R W Bonser

    FEBS Letters
    |April 6, 1987
    PubMed
    Summary
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    1,2-sn-Dihexanoylglycerol (HHG) significantly reduces ATP levels in HL-60 cells, impacting cellular responses. This effect is concentration-dependent, enantiomerically specific, and inhibits protein kinase C activation pathways.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Pharmacology

    Background:

    • Adenosine triphosphate (ATP) is crucial for cellular energy and function.
    • Protein kinase C (PKC) activation plays a key role in various cellular signaling pathways.
    • HL-60 cells are a human promyelocytic leukemia cell line widely used in cellular research.

    Purpose of the Study:

    • To investigate the effect of 1,2-sn-Dihexanoylglycerol (HHG) on ATP content in HL-60 cells.
    • To explore the relationship between HHG concentration and its impact on cellular energy levels.
    • To determine if HHG affects cellular responses mediated by protein kinase C (PKC).

    Main Methods:

    • Treatment of HL-60 cells with varying concentrations of HHG, oleoylacetylglycerols, and phorbol dibutyrate (PDBu).

    Related Experiment Videos

  • Measurement of intracellular ATP content using biochemical assays.
  • Assessment of lactate dehydrogenase release to evaluate cell viability.
  • Evaluation of PDBu-stimulated superoxide release and degranulation responses.

    • Main Results:

    • HHG significantly reduced HL-60 cell ATP content in a concentration-dependent manner (10-100 microM), with maximal reduction exceeding 90%.
    • The ATP-lowering effect of HHG was enantiomerically specific and did not induce lactate dehydrogenase release, indicating minimal cytotoxicity.
    • Higher HHG concentrations (above 10 microM) limited cellular responses, including PDBu-stimulated superoxide release, and exhibited a bell-shaped curve for degranulation.

    Conclusions:

    • HHG markedly depletes ATP levels in HL-60 cells via an enantiomerically specific mechanism.
    • The reduction in ATP content by HHG likely impairs cellular functions regulated by protein kinase C (PKC) activation.
    • HHG demonstrates complex concentration-dependent effects on cellular signaling, potentially by modulating energy availability.