Inactivation of the Ba2+ current in dissociated Helix neurons: voltage dependence and the role of phosphorylation.
The rate of inactivation of the voltage-dependent Ba2+ current in dissociated neurons from the snail Helix aspersa was found to be modulated by phosphorylation. Conditions were chosen such that the most likely mechanism of inactivation of the Ba2+ current was a voltage-dependent/calcium-independent inactivation process. If adenosine-triphosphate (ATP) was not included in the patch electrode filling solution, or if alkaline phosphatase was added, the Ba2+ current rapidly ran down and the rate of inactivation greatly increased with time. Dialysis with either ATP gamma S or the phosphatase inhibitor okadaic acid (OA) either enhanced the amplitude or greatly reduced the rate of run-down of the Ba2+ current (depending upon the presence of ATP), as well as reducing the rate of inactivation. However, dialysis with either the catalytic subunit of the cyclic-adenosine-mono-phosphate-dependent protein kinase (cAMP-PK), a synthetic peptide inhibitor of this enzyme, or staurosporine (a potent inhibitor of protein kinase C), did not have any significant effect on the amplitude or kinetics of the Ba2+ current. Surprisingly, dialysis with a peptide inhibitor (CKIP) of the Ca2+/calmodulin-dependent protein kinase II (Ca(2+)-CaM-PK) significantly reduced the rate of inactivation of this current. These results suggest that phosphorylation may exert its effect by modulating the gating properties of the Ca2+ channels.
Yakel
J L
JL
Laboratoire de Neurobiologie (URA 295 CNRS), Ecole Normale Supérieure, Paris, France.
D000255:Adenosine Triphosphate / Q000494:pharmacology; D000818:Animals; D001464:Barium / Q000502:physiology*; D006372:Helix, Snails; D009474:Neurons / Q000502:physiology*; D010766:Phosphorylation
D001464:Barium; D000255:Adenosine Triphosphate