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Related Experiment Videos

Barium activates rat cerebellar nitric oxide synthase

J Yamazaki1, T Urushidani, T Nagao

  • 1Department of Toxicology and Pharmacology, Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.

Japanese Journal of Pharmacology
|April 1, 1996
PubMed
Summary

Barium ions (Ba2+) activate rat cerebellar nitric oxide synthase (NOS) via a calmodulin-dependent pathway, similar to calcium ions (Ca2+). This finding suggests Ba2+ may influence cellular signaling through NOS activation.

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Enzymology

Background:

  • Barium ions (Ba2+) are known to permeate N-methyl-D-aspartate receptor channels.
  • Ba2+ can elevate cyclic guanosine monophosphate (cGMP) levels in rat cerebella.
  • Nitric oxide synthase (NOS) is a key enzyme in nitric oxide production.

Purpose of the Study:

  • To compare the activation of rat cerebellar nitric oxide synthase (NOS) by Ba2+ versus Ca2+.
  • To investigate the mechanism by which Ba2+ activates NOS.

Main Methods:

  • Enzyme activity assay measuring L-citrulline formation.
  • Use of rat cerebellar fractions eluted from an anion exchange column.
  • Calmodulin-dependent activation assay.
  • Determination of EC50 for Ca2+ and Ba2+.

Related Experiment Videos

  • Determination of IC50 for NG-monomethyl-L-arginine.

    • Main Results:

    • Both Ca2+ and Ba2+ stimulated L-citrulline formation in the presence of calmodulin.
    • The EC50 for Ca2+ was 200 nM, and for Ba2+ was 50 microM.
    • The IC50 for NG-monomethyl-L-arginine was consistent for both cations (200 nM).

    Conclusions:

    • Ba2+ activates rat cerebellar NOS through a calmodulin-dependent pathway.
    • The activation mechanism of NOS by Ba2+ is comparable to that of Ca2+.
    • These findings suggest a potential role for Ba2+ in modulating cellular signaling via NOS.