AT4 receptors: Specificity and distribution

Harding, Joseph W.; Wright, John W.; Swanson, Geoffrey N.; Hanesworth, Jodie M.; Krebs, Luke T.

doi:10.1038/ki.1994.432

Cited by 79 publications

(34 citation statements)

References 12 publications

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“…21,22 Ang IV is extensively studied for its memory-facilitating properties in mice and rats, however its mechanism of action remains unresolved. 23 Ang IV is also reported to protect against ischemic stroke, 24,25 hyperglycemia 26 and atherosclerosis.…”

Section: Introductionmentioning

confidence: 99%

Presence and regulation of insulin-regulated aminopeptidase in mouse macrophages

Nikolaou

Stijlemans

Laoui

et al. 2014

J Renin Angiotensin Aldosterone Syst

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Introduction: The insulin-regulated aminopeptidase (IRAP) is expressed in several cell types, where it is mainly located in specialized secretory endosomes that are quickly recruited to the cell surface upon cell type-specific activation. Here we describe for the first time the expression and subcellular distribution of IRAP in macrophages. Methods: IRAP mRNA expression, protein expression and presence at the cell surface was investigated by real-time polymerase chain reaction (PCR), Western blot and [³H]IVDE77 binding, respectively. Results: IRAP mRNA expression was increased by interferon-γ (IFN-γ) and lipopolysaccharide (LPS), but not by antiinflammatory cytokines (interleukin (IL)-4, IL-10, transforming growth factor β (TGF-β)). IFN-γ increased [³H]IVDE77 binding steadily over time, while LPS quickly and transiently recruited IRAP to the cell surface. Combined stimulations with IFN-γ and LPS showed the same pattern as LPS alone. Latex particles also induced a transient recruitment of IRAP to the cell surface, but no difference was observed in phagocytic uptake between wild-type and IRAP -/-macrophages, suggesting that the enzymatic activity of IRAP is not required for the ingestion of particles. Conclusion: IRAP is more highly expressed in pro-inflammatory M1-activated macrophages and its presence at the cell surface is modulated upon exposure to IFN-γ, LPS or exogenous particles.

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Section: Introductionmentioning

confidence: 99%

Presence and regulation of insulin-regulated aminopeptidase in mouse macrophages

Nikolaou

Stijlemans

Laoui

et al. 2014

J Renin Angiotensin Aldosterone Syst

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“…There is evidence that ANG IV elicits its effects via a specific AT 4 receptor. This receptor has been described in many tissues, including human collecting duct cells (4,7,15). Due to AT 1 -receptor stimulation, the actions of ANG IV may mimic some of the effects produced by ANG II.…”

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confidence: 99%

Effects of truncated angiotensins in humans after double blockade of the renin system

Plovsing

Wamberg²,

Sandgaard³

et al. 2003

American Journal of Physiology-Regulatory, Integrative and Comp

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We studied the effects of 3-h infusions of ANG III, ANG-(1-7), and ANG IV in doses equimolar to physiological amounts of ANG II (3 pmol ⅐ kg Ϫ1 ⅐ min Ϫ1 ), in six men on low-sodium diet (30 mmol/ day). The subjects were acutely pretreated with canrenoate and captopril to inhibit aldosterone actions and ANG II synthesis, respectively. ANG II infusion increased plasma angiotensin immunoreactivity to 53 Ϯ 6 pg/ml (ϩ490%), plasma aldosterone to 342 Ϯ 38 pg/ml (ϩ109%), and blood pressure by 27%. Glomerular filtration rate decreased by 16%. Concomitantly, clearance of endogenous lithium fell by 66%, and fractional proximal reabsorption of sodium increased from 77 to 92%; absolute proximal reabsorption rate of sodium remained constant. ANG II decreased sodium excretion by 70%, potassium excretion by 50%, and urine flow by 80%, whereas urine osmolality increased. ANG III also increased plasma aldosterone markedly (ϩ45%), however, without measurable changes in angiotensin immunoreactivity, glomerular filtration rate, or renal excretion rates. During vehicle infusion, plasma renin activity decreased markedly (ϳ700 to ϳ200 mIU/l); only ANG II enhanced this decrease. ANG-(1-7) and ANG IV did not change any of the measured variables persistently. It is concluded that 1) ANG III and ANG IV are cleared much faster from plasma than ANG II, 2) ANG II causes hypofiltration, urinary concentration, and sodium and potassium retention at constant plasma concentrations of vasopressin and atrial natriuretic peptide, and 3) a very small increase in the concentration of ANG III, undetectable by usual techniques, may increase aldosterone secretion substantially. healthy humans; angiotensin peptides; aldosterone secretion; sodium excretion THE RENIN-ANGIOTENSIN-ALDOSTERONE system (RAAS) is the single most important regulator of the sodium homeostasis. This specific role of the RAAS makes it a major determinant of extracellular fluid volume and arterial blood pressure. It has long been recognized that ANG II is the pivotal component of this system.

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“…13 Both are seven-transmembrane glycoproteins (G-protein-coupled receptors) with 30% sequence similarity, 13,14 and both are expressed in the kidney. [15][16][17][18] AT 1 receptors are abundantly expressed in cells of the renal glomeruli, tubules, vasculature and interstitial space. 18 In rodents, two subtypes of the AT 1 receptor have been identified, AT 1a and AT 1b receptors, 19 which share 95% sequence homology and exhibit similar ligand binding affinities and signal-transduction properties, but differ in their tissue expression.…”

Section: Angiotensin II At 1 and At 2 Receptorsmentioning

confidence: 99%

“…55,109 Yet, Ang IV displays certain biological effects already at nanomolar concentrations, which are not blocked by AT 1 and AT 2 receptor antagonists (Figure 2). This, together with the discovery of highaffinity binding sites for [ 125 I]Ang IV in the central nervous, vascular and renal systems, 16,116,117 has led to the concept of a novel Ang receptor subtype: the 'AT 4 receptor' , 14 which was convincingly shown to be 'insulin-regulated aminopeptidase (IRAP)' , a membraneanchored zinc-dependent metallopeptidase. 118 Autoradiographic and radioligand binding experiments have localized AT 4 binding sites on microvilli and cell bodies of rat proximal convoluted and straight tubules, 17 cultured rat mesangial cells, 111 cultured opossum proximal tubule cells, 119 apical and basolateral membranes of rabbit cortical tubules, 119 cultured rabbit 120 and human collecting duct cells 121 and cultured human proximal tubule epithelial cells.…”

Section: Angiotensin II At 1 and At 2 Receptorsmentioning

confidence: 99%