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

Autor:	Georges Vauquelin, Géza Tóth, Jean-Paul De Backer, Erzsébet Szemenyei, Heidi Demaegdt, Aneta Lukaszuk, Dirk Tourwé
Rok vydání:	2011
Předmět:	Pharmacology chemistry.chemical_classification chemistry.chemical_element Zinc Aminopeptidase Angiotensin II Angiotensin IV Low affinity Enzyme chemistry Biochemistry Insulin regulated aminopeptidase Pharmacology (medical) Receptor
Zdroj:	Fundamental & Clinical Pharmacology. 26:194-197
ISSN:	0767-3981
DOI:	10.1111/j.1472-8206.2011.00948.x
Popis:	Radioligand binding studies revealed that Ang IV binds to insulin-regulated aminopeptidase (IRAP)/'AT(4) receptors' with high affinity. Yet, as these experiments were routinely carried out 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 [(3) H]AL-11, we here show that the native enzyme is only a low-affinity target for Ang IV.
Databáze:	OpenAIRE
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