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Nerve growth factor-induced decrease in the cell-free phosphorylation of a soluble protein in PC12 cells.

D End, N Tolson, S Hashimoto

    The Journal of Biological Chemistry
    |May 25, 1983
    PubMed
    Summary
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    Nerve growth factor (NGF) treatment significantly reduces the phosphorylation of a 100,000-dalton protein in PC12 cells. This suggests NGF may inhibit or remove the specific kinase responsible for this protein's phosphorylation.

    Area of Science:

    • Cellular signaling pathways
    • Neuroscience
    • Molecular biology

    Background:

    • PC12 cells are a model system for studying neuronal differentiation.
    • Protein phosphorylation is a key regulatory mechanism in cellular processes.
    • Nerve growth factor (NGF) plays a crucial role in neuronal development and survival.

    Purpose of the Study:

    • To investigate the effect of NGF on protein phosphorylation in PC12 cells.
    • To identify specific proteins affected by NGF treatment.
    • To elucidate the mechanism by which NGF modulates protein phosphorylation.

    Main Methods:

    • Cell-free extracts from PC12 cells were incubated with [32P]ATP.
    • Phosphorylation levels of proteins were analyzed using quantitative methods.

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  • PC12 cells were treated with NGF, epidermal growth factor, and other agents.

    • Main Results:

    • NGF treatment substantially and selectively reduced the phosphorylation of a 100,000-dalton protein by 30-50%.
    • This reduction was dose-dependent, rapid (within 15 min), and reversible upon NGF removal.
    • Other growth factors showed varied effects, while insulin had no effect.

    Conclusions:

    • NGF treatment leads to a specific decrease in the phosphorylation of a 100,000-dalton protein.
    • The data suggest NGF induces either covalent inhibition or physical removal of the responsible kinase.
    • This finding provides insights into NGF-mediated signaling pathways in neuronal cells.