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Adenylate cyclase stimulation by trypsin.

W L Ryan, N A Short, G L Curtis

    Proceedings of the Society for Experimental Biology and Medicine. Society for Experimental Biology and Medicine (New York, N.Y.)
    |December 1, 1975
    PubMed
    Summary
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    Trypsin treatment significantly boosts adenylate cyclase activity in rat embryo fibroblasts. This stimulation, blocked by soybean trypsin inhibitor, suggests trypsin targets the enzyme's catalytic unit.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Enzymology

    Background:

    • Adenylate cyclase is a crucial enzyme in cellular signaling pathways.
    • Understanding factors that regulate adenylate cyclase activity is vital for cell biology research.

    Purpose of the Study:

    • To investigate the effect of trypsin on adenylate cyclase activity in rat embryo fibroblast cells.
    • To determine the mechanism by which trypsin influences enzyme activity.

    Main Methods:

    • Treatment of rat embryo fibroblast cell line (F111) with varying concentrations and durations of trypsin.
    • Assay of adenylate cyclase activity.
    • Use of soybean trypsin inhibitor to block trypsin effects.
    • Assessment of enzyme response to PGE1 and fluoride stimulation.

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    Main Results:

    • Brief trypsin treatment markedly increased adenylate cyclase activity.
    • Stimulation was dependent on trypsin concentration and treatment duration.
    • Soybean trypsin inhibitor abolished the trypsin-induced stimulation.
    • Trypsin-treated enzyme showed response to PGE1 without further increase, but fluoride-stimulated activity increased.

    Conclusions:

    • Trypsin activates adenylate cyclase in F111 cells.
    • The findings suggest trypsin acts on the catalytic unit of adenylate cyclase.
    • This provides insights into the regulation of adenylate cyclase by proteases.