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

Autor: Demaegdt, Heidi, De Backer, Jean-Paul, Lukaszuk, Aneta, Tóth, Géza, Szemenyei, E, Tourwe, Dirk, Vauquelin, Georges
Přispěvatelé: Molecular and Biochemical Pharmacology, Chemistry, Department of Bio-engineering Sciences, Organic Chemistry
Jazyk: angličtina
Rok vydání: 2012
Předmět:
Popis: 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.
Databáze: OpenAIRE