Cellular targets for angiotensin II fragments: pharmacological and molecular evidence
Although angiotensin II has long been considered to represent the end product of the renin-angiotensin system (RAS), there is accumulating evidence that it encompasses additional effector peptides with diverse functions. In this respect, angiotensin IV (Ang IV) formed by deletion of the two N termin...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
SAGE Publications
2002-12-01
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| Series: | Journal of the Renin-Angiotensin-Aldosterone System |
| Online Access: | https://doi.org/10.3317/jraas.2002.041 |
| _version_ | 1797285754771079168 |
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| author | Georges Vauquelin Yvette Michotte Ilse Smolders Sophie Sarre Guy Ebinger Alain Dupont Patrick Vanderheyden |
| author_facet | Georges Vauquelin Yvette Michotte Ilse Smolders Sophie Sarre Guy Ebinger Alain Dupont Patrick Vanderheyden |
| author_sort | Georges Vauquelin |
| collection | DOAJ |
| description | Although angiotensin II has long been considered to represent the end product of the renin-angiotensin system (RAS), there is accumulating evidence that it encompasses additional effector peptides with diverse functions. In this respect, angiotensin IV (Ang IV) formed by deletion of the two N terminal amino acids, has sparked great interest because of its wide range of physiological effects. Among those, its facilitatory role in memory acquisition and retrieval is of special therapeutic relevance. High affinity binding sites for this peptide have been denoted as `AT 4 receptors' and, very recently, they have been proposed to correspond to the membrane-associated OTase/ IRAP aminopeptidase. This offers new opportunities for examining physiological roles of Ang IV in the fields of cognition, cardiovascular and renal metabolism and pathophysiological conditions like diabetes and hypertension. Still new recognition sites may be unveiled for this and other angiotensin fragments. Recognition sites for Ang-(1-7) (deletion of the C terminal amino acid) are still elusive and some of the actions of angiotensin III (deletion of the N terminal amino acid) in the CNS are hard to explain on the basis of their interaction with AT 1 -receptors only. A more thorough cross-talk between in vitro investigations on native and transfected cell lines and in vivo investigations on healthy, diseased and transgenic animals may prove to be essential to further unravel the molecular basis of the physiological actions of these small endogenous angiotensin fragments. |
| first_indexed | 2024-03-07T18:07:49Z |
| format | Article |
| id | doaj.art-bdd9c12561a54acca8d96f40181ae225 |
| institution | Directory Open Access Journal |
| issn | 1470-3203 |
| language | English |
| last_indexed | 2024-03-07T18:07:49Z |
| publishDate | 2002-12-01 |
| publisher | SAGE Publications |
| record_format | Article |
| series | Journal of the Renin-Angiotensin-Aldosterone System |
| spelling | doaj.art-bdd9c12561a54acca8d96f40181ae2252024-03-02T08:32:53ZengSAGE PublicationsJournal of the Renin-Angiotensin-Aldosterone System1470-32032002-12-01310.3317/jraas.2002.041Cellular targets for angiotensin II fragments: pharmacological and molecular evidenceGeorges VauquelinYvette MichotteIlse SmoldersSophie SarreGuy EbingerAlain DupontPatrick VanderheydenAlthough angiotensin II has long been considered to represent the end product of the renin-angiotensin system (RAS), there is accumulating evidence that it encompasses additional effector peptides with diverse functions. In this respect, angiotensin IV (Ang IV) formed by deletion of the two N terminal amino acids, has sparked great interest because of its wide range of physiological effects. Among those, its facilitatory role in memory acquisition and retrieval is of special therapeutic relevance. High affinity binding sites for this peptide have been denoted as `AT 4 receptors' and, very recently, they have been proposed to correspond to the membrane-associated OTase/ IRAP aminopeptidase. This offers new opportunities for examining physiological roles of Ang IV in the fields of cognition, cardiovascular and renal metabolism and pathophysiological conditions like diabetes and hypertension. Still new recognition sites may be unveiled for this and other angiotensin fragments. Recognition sites for Ang-(1-7) (deletion of the C terminal amino acid) are still elusive and some of the actions of angiotensin III (deletion of the N terminal amino acid) in the CNS are hard to explain on the basis of their interaction with AT 1 -receptors only. A more thorough cross-talk between in vitro investigations on native and transfected cell lines and in vivo investigations on healthy, diseased and transgenic animals may prove to be essential to further unravel the molecular basis of the physiological actions of these small endogenous angiotensin fragments.https://doi.org/10.3317/jraas.2002.041 |
| spellingShingle | Georges Vauquelin Yvette Michotte Ilse Smolders Sophie Sarre Guy Ebinger Alain Dupont Patrick Vanderheyden Cellular targets for angiotensin II fragments: pharmacological and molecular evidence Journal of the Renin-Angiotensin-Aldosterone System |
| title | Cellular targets for angiotensin II fragments: pharmacological and molecular evidence |
| title_full | Cellular targets for angiotensin II fragments: pharmacological and molecular evidence |
| title_fullStr | Cellular targets for angiotensin II fragments: pharmacological and molecular evidence |
| title_full_unstemmed | Cellular targets for angiotensin II fragments: pharmacological and molecular evidence |
| title_short | Cellular targets for angiotensin II fragments: pharmacological and molecular evidence |
| title_sort | cellular targets for angiotensin ii fragments pharmacological and molecular evidence |
| url | https://doi.org/10.3317/jraas.2002.041 |
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