Role of intracellular Zn2+ in translocation of protein kinase C in guinea pig cortical synaptoneurosomes

• Published in: Japanese Journal of Pharmacology 1990, Vol.52 (suppl-1.2), p.363-363
• Main Authors: Etoh, Susumu, Baba, Akemichi, Iwata, Heitaroh
• Format: Article
• Language: English
• ISSN: 0021-5198; 1347-3506
• DOI: 10.1016/S0021-5198(19)55911-X

Translocation of protein kinase C (PKC) seems to be involved in several physiological phenomena. It is reported that PKC contains cysteine-repeating sequence, as the 'zinc finger', and an activation of PKC may be influenced by Zn^2+ . The present study was undertaken to clarify the role of intracellular Zn^2+ in translocation of PKC in neurons. Like Ca^2+ , Zn^2+ induced a dose-dependent translocation of PKC from the cytosol to the membranes in the cerebral cortex homogenate. In the. guinea pig cortical synaptoneurosomes, either 10 μM A23187, 100 μM N-methyl-D-aspartate (NMDA) or 40 mM KCl resulted in the translocation of PKC (5-20 % of total PKC). N,N,N',N'-Tetrakis (2-pyridylmethyl) ethylene-diamine (TPEN) (100 μM), a heavy metal chelator, blocked the translocation of PKC induced by A23187 or NMDA. TPEN showed the inhibitory effect on the translocation even when it was treated together with CaCl_2 . On the other hand, TPEN pretreated with ZnCl_2 (Zn-TPEN complex formation) lost the inhibitory effect on the translocation. These results suggest that intracellular Zn^2+ plays a role in the stimulant-induced translocation of PKC in guinea pig synaptoneurosomes.