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Cellular targets for angiotensin II fragments: pharmacological and molecular evidence

Department of Molecular and Biochemical Pharmacology, Institute for Molecular Biology and Biotechnology, Vrije Universiteit Brussel (VUB), Paardenstraat 65, 1640 Sint-Genesius Rode, Belgium, gvauquel{at}vub.ac.be

Yvette Michotte

Department of Pharmaceutical Chemistry, Drug Analysis and Drug Information, Vrije Universiteit Brussel (VUB), Laarbeeklaan 103, 1090 Brussels, Belgium

Ilse Smolders

Department of Pharmaceutical Chemistry, Drug Analysis and Drug Information, Vrije Universiteit Brussel (VUB), Laarbeeklaan 103, 1090 Brussels, Belgium

Sophie Sarre

Department of Pharmaceutical Chemistry, Drug Analysis and Drug Information, Vrije Universiteit Brussel (VUB), Laarbeeklaan 103, 1090 Brussels, Belgium

Guy Ebinger

Department of Neurology, University Hospital-Vrije Universiteit Brussel (AZ-VUB), Laarbeeklaan 101, 1090 Brussels, Belgium

Alain Dupont

Department of Pharmacology, Vrije Universiteit Brussel (VUB), Laarbeeklaan 103, 1090 Brussels, Belgium

Patrick Vanderheyden

Department of Molecular and Biochemical Pharmacology, Institute for Molecular Biology and Biotechnology, Vrije Universiteit Brussel (VUB), Paardenstraat 65, 1640 Sint-Genesius Rode, Belgium

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 `AT₄receptors' 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 AT₁-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.

Key Words: angiotensin fragments • AT1- • AT2- • AT4-and AT-(1-7) receptors • insulin-regulated aminopeptidase • Oxytocinase • CNS • kidney

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Journal of Renin-Angiotensin-Aldosterone System, Vol. 3, No. 4, 195-204 (2002)
DOI: 10.3317/jraas.2002.041


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