thapsigargin and glutamyl-leucyl-threonyl-phenylalanyl-threonyl-prolyl-asparaginyl-tryptophanamide

Protein kinase C and calmodulin play key roles in cockroach fat body during activation of phosphorylase and trehalose efflux by HTH-II. The data support the view that an increase in cytosolic Ca2+ is prerequisite for enhanced activity of protein kinase C and calmodulin. Chelation of Ca2+ (i) with BAPTA blocks HTH-II-induced trehalose efflux from the fat body whereas thapsigargin, which raises [Ca2+]i to the same level as HTH-II, produces only a small, yet significant increase in trehalose efflux. Sphingosine, an inhibitor of protein kinase C, inhibits HTH-II-induced trehalose efflux in a concentration-dependent manner. Trehalose efflux is not activated by the protein kinase C activators OAG or PMA alone but in the presence of thapsigargin both agents increase trehalose efflux to a level comparable to that obtained with HTH-II. Thapsigargin has only a moderate activating effect on phosphorylase but in combination with OAG produces an activation indistinguishable from that provoked by HTH-II. Each of the structurally different calmodulin inhibitors, trifluoperazine, W-7, and calmidazolium, blocks completely the action of HTH-II on trehalose efflux, thus confirming the importance of calmodulin in HTH-II initiated trehalose efflux.

Topics: Animals; Calcium; Calmodulin; Chelating Agents; Diglycerides; Egtazic Acid; Enzyme Activation; Enzyme Inhibitors; Fat Body; Male; Neuropeptides; Periplaneta; Phosphorylases; Protein Kinase C; Sphingosine; Tetradecanoylphorbol Acetate; Thapsigargin; Trehalose; Trifluoperazine