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Hemorphins inhibit angiotensin IV binding and interact with aminopeptidase N

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Garreau, Isabelle | Chansel, Dominique | Vandermeersch, Sophie | Fruitier, Ingrid | Piot, Jean Marie | Ardaillou, Raymond

Edité par CCSD ; Elsevier -

International audience. [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 beta chain of hemoglobin. The most potent competitors were those with a valine in their N-terminal part such as LVV-H7 and VV-H7 (IC50 = 1.3 nM) followed by VV-H8 and K6VV-H7 (5.1 nM). 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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