LTP induced by activation of voltage-dependent Ca²⁺ channels requires protein kinase activity

A VDCC-dependent component. The results herein demonstrate that both the NMDA and VDCC-dependent components of TEA-LTP are blocked by K-252a, a broad spectrum protein kinase inhibitor. Furthermore, VDCC-dependent TEA-LTP is attenuated by KN-62, a specific inhibitor of Ca²⁺/calmodulin dependent protein kinase II (CaM-KII). These results demonstrate that LTP induced by VDCC activation requires protein kinase activity and suggest that different routes of postsynaptic Ca²⁺ influx activate protein kinases to trigger the induction of LTP but that these enzyme systems may be contained in different cell compartments.