The angiotensin IV/AT4 receptor

Chai, S. Y., Fernando, R., Peck, G., Ye, S. -Y., Mendelsohn, F. A. O., Jenkins, T. A. and Albiston, A. L. 2004, The angiotensin IV/AT4 receptor, Cellular and molecular life sciences, vol. 61, no. 21, pp. 2728-2737, doi: 10.1007/s00018-004-4246-1.

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Title The angiotensin IV/AT4 receptor
Author(s) Chai, S. Y.
Fernando, R.
Peck, G.
Ye, S. -Y.ORCID iD for Ye, S. -Y.
Mendelsohn, F. A. O.
Jenkins, T. A.
Albiston, A. L.
Journal name Cellular and molecular life sciences
Volume number 61
Issue number 21
Start page 2728
End page 2737
Total pages 10
Publisher Birkhaeuser Verlag AG
Place of publication Basel, Switzerland
Publication date 2004-11
ISSN 1420-682X
Keyword(s) insulin-regulated aminopeptidase
Summary The angiotensin AT4 receptor was originally defined as the specific, high-affinity binding site for the hexapeptide angiotensin IV (Ang IV). Subsequently, the peptide LVV-hemorphin 7 was also demonstrated to be a bioactive ligand of the AT4 receptor. Central administration of Ang IV, its analogues or LVV-hemorphin 7 markedly enhance learning and memory in normal rodents and reverse memory deficits observed in animal models of amnesia. The AT4 receptor has a broad distribution and is found in a range of tissues, including the adrenal gland, kidney, lung and heart. In the kidney Ang IV increases renal cortical blood flow and decreases Na+ transport in isolated renal proximal tubules. The AT4 receptor has recently been identified as the transmembrane enzyme, insulin-regulated membrane aminopeptidase (IRAP). IRAP is a type II integral membrane spanning protein belonging to the M1 family of aminopeptidases and is predominantly found in GLUT4 vesicles in insulin-responsive cells. Three hypotheses for the memory-potentiating effects of the AT4 receptor/IRAP ligands, Ang IV and LVV-hemorphin 7, are proposed: (i) acting as potent inhibitors of IRAP, they may prolong the action of endogenous promnestic peptides; (ii) they may modulate glucose uptake by modulating trafficking of GLUT4; (iii) IRAP may act as a receptor, transducing the signal initiated by ligand binding to its C-terminal domain to the intracellular domain that interacts with several cytoplasmic proteins.
Language eng
DOI 10.1007/s00018-004-4246-1
Field of Research 119999 Medical and Health Sciences not elsewhere classified
Socio Economic Objective 970111 Expanding Knowledge in the Medical and Health Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
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Document type: Journal Article
Collections: Faculty of Health
School of Medicine
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