Angiotensin IV displays only low affinity for native insulin-regulated aminopeptidase (IRAP)

Heidi Demaegdt, Jean-Paul De Backer, Aneta Lukaszuk, Géza Tóth, E Szemenyei, Dirk Tourwe, Georges Vauquelin

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Radioligand binding studies revealed that Ang IV binds to IRAP/'AT4 receptors' with high affinity. Yet, as these experiments were routinely done in the presence of chelators, only the catalytic zinc-depleted apo-form of IRAP was labelled. While the chelators remove the catalytic zinc from IRAP and protect Ang IV from proteolytic degradation, the Aminopeptidase N selective inhibitor '7B' only exerts the latter effect. By using 7B along with the new stable Ang IV-analog [3H]AL-11, we here show that the native enzyme is only a low affinity target for Ang IV.
Original languageEnglish
Pages (from-to)194-197
Number of pages4
JournalFundamental and Clinical Pharmacology
Volume26
Publication statusPublished - 2012

Keywords

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