Effects of calmodulin inhibitors on cyprid larvae of the barnacle, Balanus amphitrite.

During our study on signal transduction systems involved in larval settlement and metamorphosis of the barnacle Balanus amphitrite, we could detect calmodulin, a major intracellular calcium-binding protein, in both cyprids and adult barnacles using immunoblot technique. In order to examine roles of calmodulin in larval settlement and metamorphosis, we examined the effects of calmodulin inhibitors involved in phosphodiesterase (PDE), myosin light chain kinase (MLCK), calmodulin kinase II (CaM-II) on cyprids. Calcium-calmodulin-dependent PDE inhibitors inhibited larval attachment and metamorphosis in a dose-dependent manner. In contrast, cyclic AMP (cAMP)-dependent PDE inhibitors promoted larval attachment and metamorphosis, while cyclic GMP (cGMP)-dependent PDE inhibitors did not show such effect. Thus, PDE activity may depend on cAMP rather than calmodulin or cGMP in promotion of larval attachment and metamorphosis. Moreover, calmodium inhibitors involved in MLCK or CaM-II inhibited larval behaviors for attachment and metamorphosis. These results suggest that calmodulin, which is present in both adult barnacles and cyprids, may be involved in enzyme reactions such as MLCK or CaM-II rather than PDE in B. amphitrite cyprids.