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Papers In Press, published online ahead of print November 13, 2001
Neurochemistry, Howard Florey Institute, Parkville, Vic 3010
Corresponding Author: sychai{at}hfi.unimelb.edu.au
Central infusion of angiotensin IV, or its more stable analogues, facilitates memory retention and retrieval in normal animals and reverses amnesia induced by scopolamine or by bilateral perforant pathway lesions. These peptides bind with high affinity and specificity to a novel binding site designated the angiotensin AT4 receptor. Until now, the AT4 receptor has eluded molecular characterisation. Here we identify the AT4 receptor, by protein purification and peptide sequencing, to be insulin-regulated aminopeptidase (IRAP). HEK293T cells transfected with IRAP exhibit typical AT4 receptor binding characteristics; the AT4 receptor ligands, Ang IV and LVV-hemorphin 7, compete for the binding of [125I]Nle1-Ang IV with IC50 values of 32 and 140 nM respectively. The distribution of IRAP and its mRNA in the brain, determined by immunohistochemistry and hybridisation histochemistry, parallels that of the AT4 receptor determined by radioligand binding. We also show that "AT4 receptor" ligands dose-dependently inhibit the catalytic activity of IRAP. We have therefore demonstrated that the AT4 receptor is IRAP and propose that "AT4 receptor" ligands may exert their effects by inhibiting the catalytic activity of IRAP thereby extending the half-life of its neuropeptide substrates.
J. Biol. Chem, 10.1074/jbc.C100512200
Submitted on September 7, 2001
Revised on November 1, 2001
Accepted on November 13, 2001
Evidence that the angiotensin IV (AT4) receptor is the enzyme insulin regulated aminopeptidase
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