Selective labeling of IRAP by the tritiated AT4 receptor ligand [3H]Angiotensin IV and its stable analog [3H]AL-11
| Autor: | Aneta Lukaszuk, Jean-Paul De Backer, Sridhara Chakravarthy, Géza Tóth, Dirk Tourwé, Erzsébet Szemenyei, Heidi Demaegdt, Yvette Michotte, Evi De Buyser, Georges Vauquelin, Mitradas M. Panicker |
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| Přispěvatelé: | Molecular and Biochemical Pharmacology, Experimental Pharmacology, Chemistry, Department of Bio-engineering Sciences, Organic Chemistry |
| Rok vydání: | 2009 |
| Předmět: |
Cell
CHO Cells Ligands Tritium Binding Competitive Biochemistry Divalent Mice 03 medical and health sciences Cricetulus 0302 clinical medicine Endocrinology IRAP Cricetinae medicine Animals Humans Cystinyl Aminopeptidase Receptor Molecular Biology 030304 developmental biology chemistry.chemical_classification 0303 health sciences Receptors Angiotensin Ang IV Staining and Labeling biology Angiotensin II Chinese hamster ovary cell HEK 293 cells Ligand (biochemistry) Kinetics Membrane medicine.anatomical_structure chemistry biology.protein Biological Assay AL-11 030217 neurology & neurosurgery GLUT4 |
| Zdroj: | Molecular and Cellular Endocrinology. 311:77-86 |
| ISSN: | 0303-7207 |
| DOI: | 10.1016/j.mce.2009.07.020 |
| Popis: | ‘AT4 receptors’ through which Angiotensin IV (Ang IV) improves memory acquisition, were recently identified as insulin regulated aminopeptidase (IRAP). Radioligand binding studies have hitherto been performed with iodinated Ang IV in the presence of divalent cation chelators EDTA and 1,10-phenanthrolin. Hence, they referred to the apo-form of IRAP. Presently, binding of [3H]Ang IV and [3H]AL-11, a stable Ang IV analog, was compared on Chinese hamster ovary (CHO-K1) and mouse hippocampal (P40H1) cell membranes. With chelators, their high affinity sites showed the same pharmacological profile as for [125I]Ang IV binding. Without chelators, only high affinity binding was perceived for [3H]AL-11. The same pharmacological profile was recorded in both membrane preparations; it was different from the one in the presence of chelators and corresponded to catalytically active IRAP (despite the concurrent presence of aminopeptidase N (APN) in P40H1 cell membranes). This confirms that the active and apo-forms of IRAP have a distinct pharmacological profile. |
| Databáze: | OpenAIRE |
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