Zinc (Zn2+) binds to and stimulates the activity of group I but not group II phospholipase A2.

Phospholipase A2 plays an important part in the generation of inflammatory lipid mediators and so it is of major interest to understand functional distinctions between structurally similar forms of phospholipase A2. In the present study, the influence of zinc (Zn2+) on the activity of group I and group II phospholipase A2 was examined in vitro. It appeared that Zn2+ (0.04-1 x 10(-3)M) increased group I phospholipase A2 activity from porcine pancreas and rat lung whereas the activity of group II phospholipase A2 from Crotalus atrox and Vipera russelli was unaffected. The presence of Cd2+ of Hg2+ (0.8-5 x 10(-3)M) also increased group I pancreatic phospholipase A2 activity while no augmentation was found with Cr2+, Fe2+ or Mg2+. The selective stimulation of group I phospholipase A2 by Zn2+ corresponded to a binding of these phospholipases A2 to a zinc-affinity column, while group II phospholipase A2 was not bound. Furthermore, the PLA2 activity in bronchoalveolar lavage fluid from rat was stimulated by Zn2+. These results indicate that Zn2+ binds to and increases the activity of group I, but not group II phospholipase A2. This difference in Zn(2+)-binding may be used to discriminate between group I and group II phospholipase A2 and to separate the enzymes from each other in complex biological materials. The possibility that activation of group I phospholipase A2 in the lung is important in zinc-induced metal fume fever is implied.