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Retinoic acid receptor (RAR)- agonists have been of interest as chemotherapeutic agents for the treatment of cancers including leukemia 2, 3 but they are of limited utility in treating tumors as a result of their cardiotoxic and teratogenic effects 4. An improved RAR- agonist is therefore of clinical interest. Retinoic acid receptor (RAR)- agonists include AGN-193836 (1) 5 with selectivity for RAR-(1-2,3) (5) 6. AGN-193836 (1) is a more potent and more selective RAR- antagonist (IC50 3th, IC50 24th ) versus RXR- than AGN-1285 (3) (IC50 3th = IC50 24th ).
RAR (3 2) is an important consequence of acute rejection after heart transplantation (HTX). RAR was associated with a higher level of AngII, AGTR1 and AGTR1 polymorphism. Higher AngII and AGTR1 levels were associated with rejection and higher AGTR1 levels were associated with lower tacrolimus trough levels. Our data suggest that inhibition of the AngII pathway can be used to prevent RAR. A randomized, double-blind, placebo-controlled, crossover clinical trial with losartan is currently underway to investigate the potential clinical impact of AngII receptor blockade on the prevention of RAR.
Retinoic acid receptor (RAR)- (RAR- and RAR- 1-2,3 ) is expressed in all specimens, whereas RAR-1 and RAR-2 were expressed in 100% of normal breast tissue but in only 11 of 14 tumorous lesions. RAR-1 was found in all cases of normal breast tissue localized distant from the tumor, but in 13 of 14 cases it was completely absent in the tumor and the morphologically normal appearing tissue adjacent to the tumor.
Exclusive expression of and activity by retinoid receptors suggests that these receptors act as ligand-gated transcription factors. Since ligand specificity is conferred by the ligand binding domains of these receptors, their exquisite ligand specificity is likely due to shape specificity of their receptors. The crystal structure of retinoic acid-bound RAR-alpha suggests that shape selectivity may be realized through positioning of the ligand into a series of holes of RARs, allowing the different substituents to orient themselves and interact with the residue volumes. By extending our previous study of shape selectivity of RARs, we studied the ligand binding pockets of all three RAR subtypes by systematically substituting various aromatic rings (e.g., indene, naphthalene, and biphenyl) for the isoprenoid ring and analyzed the effects of these changes on the ligand binding modes in each pocket. Interestingly, the halogen atoms on the aromatic ring, which are usually expected to be somewhat bulky, do not impact RAR ligand binding. Therefore, the shape selectivity of RAR is likely established by the presence of a set of accessible pockets for positioning of the substituents of different size, rather than the presence of a single all-encompassing hole. The most interesting feature of the first RAR-binding retinoids was their ability to displace in vitro labelled receptor-activating steroid 5 (RAS) from its specific binding sites on lymphoid cells. However, the concentrations used were several orders of magnitude higher than those for which they were effective in vitro or in vivo on cultured cells. We thus designed and synthesized ligands that could be expected to occupy the RAS binding site of RAR but at much lower concentrations . Apart from these, we also introduced specific functional groups into RAR ligands to improve their activity, affinity, stability, and metabolic profiles. The syntheses of the amide hopeandprismatic , the ether 5ec8ef588b
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