Abstract
Incubation of big endothelin-1 (bET-1) with protein derived from the detergent-extracted 100,000 g pellet prepared from human brain tissue resulted in the formation of endothelin-1 (ET-1) at a rate of 90 fmol mg-1 protein min-1. This formation was inhibited in a concentration-dependent manner by either phosphoramidon or EDTA, with half-maximal inhibitory concentrations of 2 and 20 microM, respectively. No conversion of big endothelin-3 (bET-3) to endothelin-3 (ET-3) was detected under the same conditions. These results show the presence in the human brain of a metalloprotease-like enzymatic activity which selectively converts bET-1 and ET-1. Together with earlier reports of mRNA for ET-1 this suggests the presence of the entire synthetic pathway for ET-1 in human brain.
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