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Alcohols increase calmodulin affinity for Ca2+ and decrease target affinity for calmodulin.

Ichiro Ohashi1, Roman Pohoreki, Kiyoshi Morita

  • 1Department of Anesthesiology and Resuscitology, Okayama University Medical School, Okayama, Japan.

Biochimica Et Biophysica Acta
|April 28, 2004
PubMed
Summary
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Alcohols affect protein function by altering enzyme activity and calcium binding. This study shows alpha-helices are not reliable indicators of alcohol potency, challenging previous theories on anesthetic mechanisms.

Area of Science:

  • Biochemistry
  • Molecular Pharmacology

Background:

  • Alcohols and anesthetics are thought to inhibit proteins with easily disrupted structures like alpha-helices.
  • The calcineurin/calmodulin/Ca(2+) system provides a model to study alcohol effects on protein function.

Purpose of the Study:

  • To investigate the effects of alcohols on calmodulin, a protein rich in alpha-helical structures.
  • To determine if alpha-helical content reliably predicts alcohol or anesthetic potency.

Main Methods:

  • Monitored calcineurin phosphatase activity and Ca(2+) binding to assess calmodulin function.
  • Utilized flow dialysis to directly measure Ca(2+) binding to calmodulin.
  • Employed a binding domain peptide to study calmodulin-target interactions.

Main Results:

Related Experiment Videos

  • Alcohols inhibited calcineurin activity in a concentration-dependent manner.
  • Ethanol increased calmodulin's affinity for Ca(2+), stabilizing its bound form.
  • Calmodulin's affinity for calcineurin decreased at saturating Ca(2+) levels.

Conclusions:

  • Alcohol effects on protein function are complex and not solely dependent on alpha-helical content.
  • Alpha-helices are unlikely to be a reliable predictor of alcohol or anesthetic potency.