Abstract
Regucalcin, a calcium-binding protein isolated from rat liver cytosol, inhibited Ca2(+)- and phospholipid-dependent protein kinase (protein kinase C) activity in hepatic cytosol. With the increasing concentrations of Ca2+ or phosphatidylserine in the medium, regucalcin caused a remarkable inhibition of protein kinase C activity. Moreover, regucalcin significantly inhibited dioctanoylglycerol-activated protein kinase C. Regucalcin itself did not have protein kinase activity in either the presence or the absence of Ca2+ and phospholipids. These findings clearly indicate that regucalcin has an inhibitory effect on protein kinase C in hepatic cytosol. This inhibitory effect of regucalcin may be due to the regucalcin-induced Ca2+ binding and/or the direct binding of regucalcin to protein kinase C.
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