<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Heidi Demaegdt</style></author><author><style face="normal" font="default" size="100%">Jean-Paul De Backer</style></author><author><style face="normal" font="default" size="100%">Aneta Lukaszuk</style></author><author><style face="normal" font="default" size="100%">Géza Tóth</style></author><author><style face="normal" font="default" size="100%">Erzsébet Szemenyei</style></author><author><style face="normal" font="default" size="100%">Dirk Tourwé</style></author><author><style face="normal" font="default" size="100%">Georges Vauquelin</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Angiotensin IV displays only low affinity for native insulin-regulated aminopeptidase (IRAP).</style></title><secondary-title><style face="normal" font="default" size="100%">Fundam Clin Pharmacol</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Angiotensin II</style></keyword><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">CD13 Antigens</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Chelating Agents</style></keyword><keyword><style  face="normal" font="default" size="100%">Cho Cells</style></keyword><keyword><style  face="normal" font="default" size="100%">Cricetinae</style></keyword><keyword><style  face="normal" font="default" size="100%">Cricetulus</style></keyword><keyword><style  face="normal" font="default" size="100%">Cystinyl Aminopeptidase</style></keyword><keyword><style  face="normal" font="default" size="100%">mice</style></keyword><keyword><style  face="normal" font="default" size="100%">Organophosphorus Compounds</style></keyword><keyword><style  face="normal" font="default" size="100%">Radioligand Assay</style></keyword><keyword><style  face="normal" font="default" size="100%">Tyrosine</style></keyword><keyword><style  face="normal" font="default" size="100%">Zinc</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2012</style></year><pub-dates><date><style  face="normal" font="default" size="100%">2012 Apr</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">26</style></volume><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Radioligand binding studies revealed that Ang IV binds to insulin-regulated aminopeptidase (IRAP)/&amp;#39;AT(4) receptors&amp;#39; 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 &amp;#39;7B&amp;#39; 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.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue></record></records></xml>