Phosphoinositide hydrolysis by phospholipase C modulated by multivalent cations La(3+), Al(3+), neomycin, polyamines, and melittin.

Second messenger production from phosphoinositide hydrolysis is regulated by different pathways, such as G-proteins or tyrosine phosphorylation of phosphoinositide phospholipase C (PI-PLC). Another means of altering the activity of PI-PLC is through cation interaction with the phosphoinositide substrate. A variety of organic and inorganic multi-valent cations were examined for their effects on the activity of purified PI-PLC delta. Surprisingly, the cations produced both stimulation and inhibition of PI-PLC catalyzed phosphoinositide hydrolysis, depending on the substrate and the ion to phosphoinositide stoichiometry. These data support the hypothesis that ionic complexes with phosphoinositides may alter their hydrolysis by PI-PLC.