By Tadashi Inagami, Masato Mizukoshi, Deng-Fu Guo (auth.), Juan M. Saavedra, Pieter B. M. W. M. Timmermans (eds.)
From molecular biology to medical functions of selective receptor blockade, the current quantity compiles the most recent advances of this rising box. Of specific value is the eye given to the newly found AT2 receptors, and the body structure and pathophysiology of angiotensin receptor subtypes. The ebook will offer clinicians treating heart problems and high blood pressure with a clearer figuring out of this therapeutically very important and intricate hormone.
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Extra info for Angiotensin Receptors
This results in a synergistic effect of the phorbol ester TPA and dexamethasone, producing a marked increase in the ATI mRNA level. However, such a synergism does not occur between ANG II and dexamethasone, again indicating that the effect of ANG II is not exerted through protein kinase C. The positive effect of aldosterone on the vascular smooth muscle is interesting since this effect is compounded by the stimulation of aldosterone production by ANG II in the adrenal. In vitro studies also showed that cAMP or forskolin inhibits the ATI receptor gene expression,39 which can be a negative result of cAMP-responsive element in the upstream regions of the 5'-noncoding region of the gene.
The response to ANG II was blocked by micromolar concentrations of the peptidic AT2 antagonist CGP 42112A, which usually has nanomolar affinity for AT2 sites (Table III). Binding assays revealed a single site having high affinity for ANG II (3 nM). ANG II binding was inhibited by CGP 42112A (lCso = 724 nM) and losartan (ICso = 59 /lM) and not by PD 123319 (lCso> 100 /lM). Therefore, this receptor does not seem to belong to either ATI or AT2 groups. Recent evidence suggests that avian ANG II receptors may differ pharmacologically from mammalian ones; the cloning of an avian ANG II receptorS2 may help to resolve this issue.
1) by uncharged glutamine induced a marked inhibition of [125I]-ANG II binding, suggesting that the ligand might be tightly associated with the receptor inside the plasma membrane. The second study focused on the domains likely to interact with cytoplasmic G-proteins. 56 In each mutant a group of polar amino acids was replaced by neutral homologues. Mutations affecting either end of the second cytoplasmic loop, deletion of the cytoplasmic tail, and to a lesser degree mutation of the carboxy side of the third cytoplasmic loop, all inhibited the GTPyS-induced shift in agonist binding and inositol phosphate production.