Activation of microsomal guanylate cyclase by a cytotoxic polypeptide: Melittin

Pushkaraj J. Lad, W. Thomas Shier

Research output: Contribution to journalArticlepeer-review

13 Scopus citations

Abstract

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 languageEnglish (US)
Pages (from-to)315-321
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume89
Issue number1
DOIs
StatePublished - Jul 12 1979

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