Polylysine stimulated protein phosphorylation in rabbit ciliary processes: casein kinase activities.

Protein phosphorylation in response to polylysine was investigated in vitro in rabbit ciliary process homogenates by SDS-PAGE autoradiography. The degree of phosphorylation was greater in the soluble/cytoplasmic fraction than in the particulate fraction and was antagonized by heparin. Time and dose-dependent studies indicated several different kinetic patterns of phosphorylation/dephosphorylation among the approximately 15 significantly 32P-labeled bands found in each fraction. These results are consistent with phosphorylation of endogenous substrates by casein kinase II, and dephosphorylations by type I and type II phosphoprotein phosphatase enzymes. The presence of EGF receptors in ciliary processes was indicated by high affinity (kD < 0.5 nM) binding sites and by intraocular pressure and blood-aqueous barrier responses to injection of low doses of EGF (100 ng per eye). EGF did not stimulate protein phosphorylation in ciliary process homogenates in vitro. The results show that casein kinase II is a significant kinase activity in ciliary processes and may have a modulatory role on signal transduction proteins involved in cellular response to hormones.