Evidence that the angiotensin IV (AT(4)) receptor is the enzyme insulin-regulated aminopeptidase
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 designate...
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| Published in: | The Journal of biological chemistry Vol. 276; no. 52; p. 48623 |
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| Main Authors: | , , , , , , , , , , |
| Format: | Journal Article |
| Language: | English |
| Published: |
United States
28.12.2001
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| Subjects: | |
| ISSN: | 0021-9258 |
| Online Access: | Get more information |
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| Abstract | 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 AT(4) receptor. Until now, the AT(4) receptor has eluded molecular characterization. Here we identify the AT(4) receptor, by protein purification and peptide sequencing, to be insulin-regulated aminopeptidase (IRAP). HEK 293T cells transfected with IRAP exhibit typical AT(4) receptor binding characteristics; the AT(4) receptor ligands, angiotensin IV and LVV-hemorphin 7, compete for the binding of [(125)I]Nle(1)-angiotensin IV with IC(50) values of 32 and 140 nm, respectively. The distribution of IRAP and its mRNA in the brain, determined by immunohistochemistry and hybridization histochemistry, parallels that of the AT(4) receptor determined by radioligand binding. We also show that AT(4) receptor ligands dose-dependently inhibit the catalytic activity of IRAP. We have therefore demonstrated that the AT(4) receptor is IRAP and propose that AT(4) receptor ligands may exert their effects by inhibiting the catalytic activity of IRAP thereby extending the half-life of its neuropeptide substrates. |
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| AbstractList | 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 AT(4) receptor. Until now, the AT(4) receptor has eluded molecular characterization. Here we identify the AT(4) receptor, by protein purification and peptide sequencing, to be insulin-regulated aminopeptidase (IRAP). HEK 293T cells transfected with IRAP exhibit typical AT(4) receptor binding characteristics; the AT(4) receptor ligands, angiotensin IV and LVV-hemorphin 7, compete for the binding of [(125)I]Nle(1)-angiotensin IV with IC(50) values of 32 and 140 nm, respectively. The distribution of IRAP and its mRNA in the brain, determined by immunohistochemistry and hybridization histochemistry, parallels that of the AT(4) receptor determined by radioligand binding. We also show that AT(4) receptor ligands dose-dependently inhibit the catalytic activity of IRAP. We have therefore demonstrated that the AT(4) receptor is IRAP and propose that AT(4) receptor ligands may exert their effects by inhibiting the catalytic activity of IRAP thereby extending the half-life of its neuropeptide substrates. 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 AT(4) receptor. Until now, the AT(4) receptor has eluded molecular characterization. Here we identify the AT(4) receptor, by protein purification and peptide sequencing, to be insulin-regulated aminopeptidase (IRAP). HEK 293T cells transfected with IRAP exhibit typical AT(4) receptor binding characteristics; the AT(4) receptor ligands, angiotensin IV and LVV-hemorphin 7, compete for the binding of [(125)I]Nle(1)-angiotensin IV with IC(50) values of 32 and 140 nm, respectively. The distribution of IRAP and its mRNA in the brain, determined by immunohistochemistry and hybridization histochemistry, parallels that of the AT(4) receptor determined by radioligand binding. We also show that AT(4) receptor ligands dose-dependently inhibit the catalytic activity of IRAP. We have therefore demonstrated that the AT(4) receptor is IRAP and propose that AT(4) receptor ligands may exert their effects by inhibiting the catalytic activity of IRAP thereby extending the half-life of its neuropeptide substrates.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 AT(4) receptor. Until now, the AT(4) receptor has eluded molecular characterization. Here we identify the AT(4) receptor, by protein purification and peptide sequencing, to be insulin-regulated aminopeptidase (IRAP). HEK 293T cells transfected with IRAP exhibit typical AT(4) receptor binding characteristics; the AT(4) receptor ligands, angiotensin IV and LVV-hemorphin 7, compete for the binding of [(125)I]Nle(1)-angiotensin IV with IC(50) values of 32 and 140 nm, respectively. The distribution of IRAP and its mRNA in the brain, determined by immunohistochemistry and hybridization histochemistry, parallels that of the AT(4) receptor determined by radioligand binding. We also show that AT(4) receptor ligands dose-dependently inhibit the catalytic activity of IRAP. We have therefore demonstrated that the AT(4) receptor is IRAP and propose that AT(4) receptor ligands may exert their effects by inhibiting the catalytic activity of IRAP thereby extending the half-life of its neuropeptide substrates. |
| Author | Matsacos, D Chai, S Y Lee, J McDowall, S G Simpson, R J Sim, P Connolly, L M Mustafa, T Albiston, A L Mendelsohn, F A Clune, E |
| Author_xml | – sequence: 1 givenname: A L surname: Albiston fullname: Albiston, A L organization: Howard Florey Institute of Experimental Physiology and Medicine, University of Melbourne, Victoria 3010, Australia – sequence: 2 givenname: S G surname: McDowall fullname: McDowall, S G – sequence: 3 givenname: D surname: Matsacos fullname: Matsacos, D – sequence: 4 givenname: P surname: Sim fullname: Sim, P – sequence: 5 givenname: E surname: Clune fullname: Clune, E – sequence: 6 givenname: T surname: Mustafa fullname: Mustafa, T – sequence: 7 givenname: J surname: Lee fullname: Lee, J – sequence: 8 givenname: F A surname: Mendelsohn fullname: Mendelsohn, F A – sequence: 9 givenname: R J surname: Simpson fullname: Simpson, R J – sequence: 10 givenname: L M surname: Connolly fullname: Connolly, L M – sequence: 11 givenname: S Y surname: Chai fullname: Chai, S Y |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/11707427$$D View this record in MEDLINE/PubMed |
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| PublicationTitle | The Journal of biological chemistry |
| PublicationTitleAlternate | J Biol Chem |
| PublicationYear | 2001 |
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| Snippet | Central infusion of angiotensin IV or its more stable analogues facilitates memory retention and retrieval in normal animals and reverses amnesia induced by... |
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| SubjectTerms | Aminopeptidases - antagonists & inhibitors Aminopeptidases - genetics Aminopeptidases - isolation & purification Aminopeptidases - metabolism Angiotensin II - analogs & derivatives Angiotensin II - chemistry Angiotensin II - metabolism Angiotensin Receptor Antagonists Animals Autoradiography Brain - cytology Brain - enzymology Brain - metabolism Cell Line Cystinyl Aminopeptidase Hemoglobins - metabolism Humans Immunohistochemistry In Situ Hybridization Iodine Radioisotopes - chemistry Iodine Radioisotopes - metabolism Mice Mice, Inbred C57BL Peptide Fragments - metabolism Radioligand Assay Receptors, Angiotensin - genetics Receptors, Angiotensin - isolation & purification Receptors, Angiotensin - metabolism Recombinant Fusion Proteins - metabolism Transfection |
| Title | Evidence that the angiotensin IV (AT(4)) receptor is the enzyme insulin-regulated aminopeptidase |
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