Possible role for a calcium-activated, phospholipid-dependent protein kinase in mode of action of DSCG

Ronit Sagi-Eisenberg suggests that the anti-allergic drug disodium cromoglycate (DSCG) exerts its inhibitory activity on mast cell degranulation by interacting with a Ca²⁺- and phospholipid-dependent protein kinase C involved in the stimulus-secretion coupling of these cells. Her hypothesis is based on similarities between the conditions required to activate this kinase and those needed to evoke secretion. In addition, binding of DSCG of mast cells leads to protein phosphorylation; protein kinase C has been shown to play a dual role in the activation and termination of the secretory process in RBL-2H3 cells. Hence, the Ca²⁺ phospholipid-dependent protein kinase C appears to be an attractive candidate for the protective action of DSCG.