Abstract
[ 125I]-Ang IV binding to rabbit collecting duct cell membranes was inhibited by hemorphins (H), a class of endogenous peptides obtained by hydrolysis of the β chain of hemoglobin. The most potent competitors were those with a valine in their N-terminal part such as LVV-H7 and VV-H7 (IC 50 = 1.3 n M) followed by VV-H8 and K 6VV-H7 (5.1 n M). The same H, like Ang IV, interacted with aminopeptidase N (APN) as shown by their inhibitory effect (28–36%) on APN activity. HPLC analysis showed that only H with a N-terminal valine or leucine were hydrolyzed. Since H are detected in the body fluids, they are likely to act as endogenous competitors of Ang IV.
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