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 language | English |
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Pages (from-to) | 194-197 |
Number of pages | 4 |
Journal | Fundamental and Clinical Pharmacology |
Volume | 26 |
Publication status | Published - 2012 |
Keywords
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