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Ionic signalling by growth factor receptors.

W H Moolenaar, L H Defize, S W De Laat

    The Journal of Experimental Biology
    |September 1, 1986
    PubMed
    Summary
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    Cell proliferation relies on growth factors like EGF and PDGF binding to receptors, triggering ionic signals. These signals, including pH and calcium changes, are essential for DNA synthesis and cell division.

    Area of Science:

    • Cell biology
    • Molecular signaling

    Background:

    • Cell proliferation is regulated by polypeptide growth factors (e.g., epidermal growth factor [EGF], platelet-derived growth factor [PDGF]) binding to cell surface receptors.
    • Receptor activation initiates a cascade of events, including tyrosine-specific protein phosphorylations, increased cytoplasmic pH (pHi), and a rise in intracellular calcium (Ca2+).

    Purpose of the Study:

    • To investigate the role of ionic signals (pHi and Ca2+) in growth factor-induced cell proliferation.
    • To determine if tyrosine kinase activity alone is sufficient for stimulating cell division.

    Main Methods:

    • Utilized monoclonal antibodies against the human EGF receptor.
    • Assessed tyrosine kinase activity, cytoplasmic pH changes, intracellular Ca2+ transients, and DNA synthesis in quiescent fibroblasts.

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    Main Results:

    • Monoclonal antibodies activated EGF receptor tyrosine kinase but failed to induce ionic signals or DNA synthesis.
    • Phorbol esters, activating protein kinase C, inhibited growth factor-induced Ca2+ signals without affecting resting Ca2+ levels.
    • Ionic signals (Ca2+ and pHi) could be dissociated from tyrosine kinase activity.

    Conclusions:

    • Tyrosine kinase activity alone is insufficient for stimulating cell proliferation.
    • Ionic signals, specifically the rise in cytoplasmic pH and intracellular calcium, are indispensable for growth factor-induced cell proliferation.