Calcium/calmodulin-dependent protein kinase II increases glutamate and noradrenaline release from synaptosomes

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Abstract
A VARIETY of evidence indicates that calcium-dependent protein phosphorylation modulates the release of neurotransmitter from nerve terminals1–3. For instance, the injection of rat calcium/cal-modulin-dependent protein kinase II (Ca2+/CaM-dependent PK II) into the preterminal digit of the squid giant synapse leads to an increase in the release of a so-far unidentified neurotransmitter induced by presynaptic depolarization3,4. But until now, it has not been demonstrated that Ca2+/CaM-dependent PK II can also regulate neurotransmitter release in the vertebrate nervous system. Here we report that the introduction of Ca2+/CaM-depen-dent PK II, autoactivated5–8 by thiophosphorylation, into rat brain synaptosomes (isolated nerve terminals) increases the initial rate of induced release of two neurotransmitters, glutamate and noradrenaline. We also show that introduction of a selective peptidergic inhibitor of Ca2+/CaM-dependent PK II inhibits the initial rate of induced glutamate release. These results support the hypothesis3,9 that activation of Ca2+/CaM-dependent PK II in the nerve terminal removes a constraint on neurotransmitter release.