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Cross-talk between second messengers.

M Bouvier1

  • 1Department of Biochemistry, University of Montreal, Quebec, Canada.

Annals of the New York Academy of Sciences
|January 1, 1990
PubMed
Summary
This summary is machine-generated.

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Cellular signaling pathways integrate diverse stimuli. Protein kinase C (PKC) phosphorylation of beta-adrenergic receptors or adenylyl cyclase mediates cross-talk, affecting cellular responses.

Area of Science:

  • Cellular Biology
  • Molecular Pharmacology
  • Signal Transduction

Background:

  • Cells integrate simultaneous stimulations via complex mechanisms.
  • Cross-talk between signaling pathways, like adenylyl cyclase and phosphatidyl-inositides hydrolysis, is crucial for cellular response.
  • Protein kinase C (PKC) activation by phorbol esters modulates beta-adrenergic-stimulated adenylyl cyclase activity.

Purpose of the Study:

  • To investigate the molecular basis of cross-talk between phosphatidyl-inositides turnover and beta-adrenergic-stimulated adenylyl cyclase activity.
  • To elucidate the role of protein kinase C (PKC) in modulating adenylyl cyclase activity.
  • To examine the differential effects of PKC on adenylyl cyclase regulation in different cell types.

Main Methods:

  • Experiments were conducted using avian and frog erythrocytes.

Related Experiment Videos

  • Cells were treated with phorbol esters to activate protein kinase C (PKC).
  • Beta-adrenergic receptor phosphorylation and adenylyl cyclase activity were measured. Purified proteins were used for in vitro phosphorylation assays.

    • Main Results:

    • In avian erythrocytes, phorbol ester treatment desensitized beta-adrenergic-stimulated adenylyl cyclase activity, associated with increased beta-adrenergic receptor phosphorylation by PKC.
    • In frog erythrocytes, phorbol ester treatment enhanced adenylyl cyclase activity, linked to increased phosphorylation of the adenylyl cyclase catalytic unit by PKC.
    • In vitro studies confirmed that PKC can phosphorylate both the beta 2-adrenergic receptor and the adenylyl cyclase catalytic unit.

    Conclusions:

    • Phosphatidyl-inositides turnover modulates beta-adrenergic-stimulated adenylyl cyclase activity through PKC-mediated phosphorylation.
    • PKC can phosphorylate distinct components of the cAMP production system, leading to either desensitization (receptor phosphorylation) or enhancement (cyclase phosphorylation) of adenylyl cyclase activity.
    • These findings highlight a conserved mechanism of signal integration with cell-specific outcomes.