Melittin, a 26 amino acid polypeptide, activated membrane-associated guanylate cyclase in a manner suggesting that membrane phospholipids play an important role in regulating the enzyme activity. Melittin was unique in that it activated only the particulate activity in a dose-dependent manner in the concentration range 15 to 200 μg/ml, and, unlike other known activators, solubilization of enzyme did not occur. The effects of melittin on guanylate cyclase showed a lag of two minutes and were not blocked by inhibitors of prostaglandin synthetase or phospholipase suggesting that the effect was not mediated by prostaglandin endoperoxides or phospholipase products but may be due to the ability of melittin to alter membrane lipid properties.
|Original language||English (US)|
|Number of pages||7|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Jul 12 1979|