In vitro brain tyrosine hydroxylase activation in catfish Heteropneustes fossilis (Bloch): seasonal changes in involvement of cAMP-dependent protein kinase A and Ca2+ -dependent protein kinase C.

In the present in vitro study, the involvement of cAMP dependent-protein kinase A (PKA) and calcium-dependent protein kinase C (PKC) in the regulation of forebrain (telencephalon and hypothalamus) tyrosine hydroxylase (TH) activity was demonstrated during the reproductive seasons of the female catfish H. fossilis. In the concentration studies conducted in prespawning phase, cAMP (0.05 nM, 0.5 nM, 1 mM and 2.0 mM) or the phosphodiesterase inhibitor isobutylmethylxanthine (IBMX-0.5-2.0 mM) stimulated enzyme activity. Likewise, the incubation of the enzyme preparations with the cAMP dependent-protein kinase A inhibitor H-89 (1 and 10 microM) and PKC inhibitor calphostin C (cal C; 1 and 10 microM) inhibited enzyme activity in a concentration-dependent manner. In seasonal studies, the incubation of the enzyme preparations with cAMP (1 mM), IBMX (1 mM), H-89 (10 microM) and cal-C (10 microM) produced season-dependent effects on enzyme activity. The stimulatory effect of cAMP and IBMX and the inhibitory effect of H-89 and cal C were greater in the resting and spawning phases. The results suggest the involvement of both signal transduction pathways in TH activation vis-à-vis catecholaminergic activity with a more dominant role by the cAMP-PKA pathway.