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Related Experiment Videos

Cholinergic function and alpha-bungarotoxin binding in PC12 cells.

G Kemp1, M Edge

  • 1Neuropsychiatry Research Program, University of Alabama at Birmingham 35294.

Molecular Pharmacology
|September 1, 1987
PubMed
Summary
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The PC12 cell line expresses nicotinic acetylcholine receptors (nAChRs) and an alpha-bungarotoxin (BGT) binding protein. Studies question if the BGT protein functions as a nAChR, as no BGT-sensitive Na+ flux was detected.

Area of Science:

  • Neuroscience
  • Cell Biology
  • Biochemistry

Background:

  • PC12 cells, derived from adrenal chromaffin tumors, possess both ganglionic nicotinic acetylcholine receptors (nAChRs) and an alpha-bungarotoxin (BGT) binding protein of unknown function.
  • Nicotinic Na+ fluxes and BGT binding sites were quantified, with a significant portion of BGT binding observed intracellularly.

Purpose of the Study:

  • To investigate the functional relationship between BGT binding protein and nAChR-mediated Na+ flux in PC12 cells.
  • To determine the synthesis and turnover rates of nAChRs and BGT binding protein.
  • To assess the impact of protein synthesis inhibition and agonist stimulation on these components.

Main Methods:

  • Measurement of nicotinic Na+ fluxes and [125I]BGT binding.
  • Inhibition of ganglionic Na+ fluxes and assessment of residual BGT-sensitive flux.

Related Experiment Videos

  • Irreversible inactivation of nAChRs and BGT binding protein using MBTA.
  • Monitoring of de novo synthesis and membrane insertion of nAChRs and BGT binding protein.
  • Effect of cycloheximide on protein synthesis and membrane insertion.
  • Carbamylcholine-induced changes in Na+ flux and BGT binding.

    • Main Results:

    • No detectable BGT-sensitive Na+ flux was found, suggesting the BGT binding protein may not function as a canonical nAChR.
    • New ganglionic nAChRs appeared with a half-life of 24 hours, while BGT binding protein was synthesized more rapidly (half-life of 6.5 hours).
    • Inhibition of protein synthesis significantly reduced BGT binding protein insertion into the plasma membrane.
    • Carbamylcholine treatment rapidly decreased Na+ flux activity by 30% without altering BGT binding protein concentration.

    Conclusions:

    • The BGT binding protein in PC12 cells likely represents a distinct entity from the functional ganglionic nAChR.
    • PC12 cells exhibit differential regulation of nAChR and BGT binding protein synthesis and turnover.
    • Agonist-induced desensitization primarily affects nAChR-mediated Na+ flux rather than the BGT binding protein levels.