The angiotensin AT2 receptor stimulates protein tyrosine phosphatase activity and mediates inhibition of particulate guanylate cyclase

Bottari, Serge P.; King, Isabelle N.; Reichlin, Serge; Dahlstroem, Ilse; Lydon, Nicholas B.; Gasparo, Marc de

doi:10.1016/0006-291x(92)91629-5

Cited by 243 publications

(100 citation statements)

References 23 publications

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“…The role of the AT2 receptors, which have high affinities for the peptide CGP 42112A and non-peptide PD 123 177 antagonists [6,7], is not well known. Recently, it has been suggested that A-II decreases the cellular concentration of cGMP in neurons through AT2 receptors [S], and Bottari et al [9] have suggested that AT2 receptors could activate a membrane-associated phosphotyrosine phosphatase. A third type of A-II receptors (AT3) has been postulated [lo], but they are not yet well characterized.…”

Section: Introductionmentioning

confidence: 99%

Characterization and regulation of the angiotensin II type‐1 receptor (binding and mRNA) in human adrenal fasciculata‐reticularis cells

et al. 1993

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The classical concept of human adrenal physiology indicates that only glomerulosa cells are the target of A-II. Herein, we demonstrated that cultured human adrenal fasciculata-reticularis cells were also responsive to this hormone. Indeed, these cells contained high affinity (Kd = 0.9-l. 1 nM) and low capacity (8,000-13,000 sites/cell) A-II receptors, and more than 95% of them were of the type-l. These AT1 receptors are functional since A-II was able to increase cortisol production after 48 h of treatment. These effects were inhibited by losartan, an AT1 antagonist, but not by CGP 42112A, an AT2 antagonist. The expression of the type-l A-II recptor mRNA was detected in the whole adrenal in both adult and fetus, and in cultured human adrenal fasciculata-reticularis cells. In these cells A-II negatively regulated AT1 receptor mRNA, and this effect was also mediated through the AT1 receptor subtype.Angiotensin-II type 1 receptor; Human adrenal

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Section: Introductionmentioning

confidence: 99%

Characterization and regulation of the angiotensin II type‐1 receptor (binding and mRNA) in human adrenal fasciculata‐reticularis cells

et al. 1993

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“…For example, AT2 receptors have been shown to mediate prostaglandin synthesis in human astrocytes [19], to modulate T-type calcium channels in NGlO8-15 cells [20], and to stimulate cGMP production in the N1 E-115 cell line [21], but to inhibit it in neonatal rat brain neuronal cultures [22]. A recent report [23] suggests that in PC12 W cells the AT2 receptor inhibits an atrial-natriuretic-peptide-stimulated guanylyl cyclase through the activation of a protein tyrosine phosphatase.…”

mentioning

confidence: 99%

Characterization of a membrane glycoprotein having pharmacological and biochemical properties of an AT2 angiotensin II receptor from human myometrium

Lazard

Villageois

Briend-Sutren

et al. 1994

European Journal of Biochemistry

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The angiotensin 11 receptors of human myometrial tissue were characterized using ligand binding, cross-linking with radioactive label, detergent solubilization and partial purification by lectinaffinity chromatography. Human myometrial membrane preparations contained variable amounts (5-650 fmol/mg protein) of high affinity (Kd = 44-65 pM) binding sites for '251-CGP42112, a ligand specific for the AT2 subtype of angiotensin I1 receptors. Competition studies with AT1-specific and AT2-specific compounds indicated that angiotensin I1 receptors on these membranes were exclusively of the AT2 subtype. The binding sites for '251-CGP42112 were efficiently solubilized by the detergent Chaps, albeit with a marked decrease in affinity (Kd = 1.2 nM). The proteins in the myometrial membrane preparation were cross-linked to '251-[Sarl, Ile8langiotensin I1 (Sarile) with disuccinimidyl suberate. When low concentrations of cross-linker were used, a single radiolabelled band of about 66-70 kDa was revealed on SDSPAGE. At higher concentrations additional bands of about 105 -120 kDa and 200 kDa were labelled. The 66 -70-kDa and 105 -120-kDa bands were separated by electroelution of SDSPAGE gel slices and submitted to trypsin cleavage. The tryptic-peptide maps were identical for both products, suggesting that the additional bands are homodimers and trimers of the labelled polypeptide. The Chaps-solubilized receptor was retained on wheat-germ-agglutinin -Sepharose and specifically eluted by the competing sugar triacetylchitotriose, leading to a fivefold purification factor. Treatment of the 1251-Sarile-labelled protein with N-glycanase caused a shift in its apparent molecular mass on SDSPAGE from 66-70kDa to 33 kDa.The peptide hormone angiotensin I1 exerts its numerous physiological actions through binding to membrane receptors. At least two subtypes of receptors for angiotensin I1 exist, which can be distinguished on the basis of their different affinity for synthetic ligands. The non-peptide antagonist DuP753 (losartan) is specific for the AT1 receptor subtype, while the synthetic peptide CGP42112 is specific for the AT2 receptor subtype. The expression of these two subtypes is tissue-specific and species-specific ; some tissues express only one subtype while others express both [ 1, 21. Most known physiological actions of angiotensin I1 such as regulation of blood pressure, extracellular fluid volume, catecholamine and aldosterone secretion, etc., can be ascribed to its binding to the AT1 receptor [3, 41. Binding of angiotensin I1 to this subtype results in modulation of the CAMP and/or Ca2+ second-messenger pathways through activation of guanine-nucleotide-binding regulatory proteins (G proteins). Recently, the cDNA encoding AT1 receptors from several spe- Little is known about the AT2 receptor subtype, but apparently it also comprises several members with different molecular properties. Bovine cerebellum [ 111, human myometrium [ll -131, rat ovarian granulosa cells [14], the R3T3 [15]and PC12 W 1161 cell lines express AT2 recept...

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“…These studies revealed that Ang II through the AT 2 receptor regulates ionic currents, decreases cyclic guanosine monophosphate (GMP) levels, and stimulates the production of arachidonic acid. 68 Bottari and coworkers demonstrated that Ang II decreases cyclic GMP levels in the pheochromocytoma cell line PC12W 69 and Sumners et al 70 has shown that a similar effect by Ang II on neonatal neuronal cultures was inhibited by PD123177 and CGP42112A, but not by losartan.…”

Section: At 2 Receptor and Signal Transductionmentioning

confidence: 99%

Receptors and their classification: focus on angiotensin II and the AT2 receptor

1998

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The angiotensin AT2 receptor stimulates protein tyrosine phosphatase activity and mediates inhibition of particulate guanylate cyclase

Cited by 243 publications

References 23 publications

Characterization and regulation of the angiotensin II type‐1 receptor (binding and mRNA) in human adrenal fasciculata‐reticularis cells

Characterization and regulation of the angiotensin II type‐1 receptor (binding and mRNA) in human adrenal fasciculata‐reticularis cells

Characterization of a membrane glycoprotein having pharmacological and biochemical properties of an AT2 angiotensin II receptor from human myometrium

Receptors and their classification: focus on angiotensin II and the AT2 receptor

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