The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 

Comparative antagonist pharmacology at the native mouse bradykinin B(2) receptor: radioligand binding and smooth muscle contractility studies.

Background and purpose:The aim was to characterize the recently discovered non-peptide antagonist MEN16132 at the mouse B(2) receptor, relative to other antagonists.Experimental approach:[(3)H]-BK binding experiments used mouse lung and ileum tissue membranes and antagonist potency was measured in the isolated ileum contractility assay.Key results:Two BK binding sites resulted from saturation and homologous competition experiments. A role for the B(1) receptor was excluded because of the poor affinity of B(1) receptor ligands (pIC(50) <5). MEN16132, and the other reference antagonists, inhibited only one portion of BK specific binding, and the rank order of potency was (pIC(50)): Icatibant (lung 10.7; ileum 10.2)=MEN11270 (lung 10.4; ileum 9.9)=MEN16132 (lung 10.5; ileum 9.9). > LF16-0687 (lung 8.9; ileum 8.8) > FR173657 (lung 8.6; ileum 8.2). BK homologous curves performed with lung membranes after treatment with the antagonist MEN16132 or Icatibant (10 nM) displayed only the low affinity site. The functional antagonism by MEN16132 (pA(2) 9.4) and Icatibant (pA(2) 9.1), towards BK (control EC(50) 6.1 nM) induced ileum contractions, was concentration-dependent and surmountable, but the Schild plot slope was less than unity.Conclusions and Implications:In mouse tissue, radiolabelled BK recognizes two binding sites and B(2) receptor antagonists can compete only for the higher affinity one. The pharmacological profile of the novel non-peptide antagonist MEN16132 indicates that it exhibits subnanomolar affinity and potency for the mouse B(2) receptor and is suitable for further characterization in in vivo pathophysiological models.British Journal of Pharmacology (2007) 150, 313-320. doi:10.1038/sj.bjp.0706995; published online 18 December 2006.[1]

References

  1. Comparative antagonist pharmacology at the native mouse bradykinin B(2) receptor: radioligand binding and smooth muscle contractility studies. Meini, S., Cucchi, P., Bellucci, F., Catalani, C., Giuliani, S., Santicioli, P., Maggi, C.A. Br. J. Pharmacol. (2007) [Pubmed]
 
WikiGenes - Universities