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Updated: Jul 29, 2026

Isolation and Time-Lapse Imaging of Primary Mouse Embryonic Palatal Mesenchyme Cells to Analyze Collective Movement Attributes
07:13

Isolation and Time-Lapse Imaging of Primary Mouse Embryonic Palatal Mesenchyme Cells to Analyze Collective Movement Attributes

Published on: February 13, 2021

Cyclic adenosine-3',5'-monophosphate alters hydrolysis of phospholipids by mouse embryo palate mesenchyme cells

M C Chabot, K P Chepenik

    Journal of Craniofacial Genetics and Developmental Biology
    |January 1, 1987
    PubMed

    Insights

    Cyclic AMP (cAMP) selectively inhibits arachidonic acid release from mouse embryo palate mesenchyme cells by modulating specific phospholipase A activities. This study clarifies the mechanism of arachidonic acid release inhibition.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Developmental Biology

    Background:

    • Arachidonic acid release is crucial for cellular signaling.
    • Understanding the regulation of arachidonic acid release is important for developmental processes.
    • Mouse embryo palate mesenchyme (MEPM) cells provide a model system to study these mechanisms.

    Purpose of the Study:

    • To investigate whether cyclic AMP (cAMP)-induced inhibition of arachidonic acid release from MEPM cells is selective or generalized.
    • To elucidate the specific phospholipid hydrolysis pathways affected by cAMP.

    Main Methods:

    • Utilized the calcium ionophore A23187 as a probe for phospholipid hydrolase activity.
    • Measured release of radiolabeled fatty acids from prelabeled MEPM cells.
    • Employed quantitative gas-liquid chromatography for substrate analysis.
    • Manipulated intracellular cAMP levels using (-) isoproterenol.

    Main Results:

    • A23187 stimulated the release of fatty acids from MEPM cell phospholipids in a dose- and time-dependent manner.
    • Elevated intracellular cAMP levels inhibited the A23187-stimulated release of arachidonic acid.
    • Gas-liquid chromatography identified 1,2-diradyl-sn-glycero-3-phosphoethanolamine as the primary source of ionophore-released arachidonic acid.
    • cAMP inhibited the hydrolysis of 1,2-diradyl-sn-glycero-3-phosphoethanolamine but potentially stimulated 1,2-diradyl-sn-glycero-3-phosphocholine hydrolysis.

    Conclusions:

    • The calcium ionophore A23187 selectively stimulates specific phospholipase A activities in MEPM cells.
    • Intracellular cAMP levels modulate these phospholipase A activities in a specific, non-generalized manner, impacting arachidonic acid release pathways.

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