Pharmacological profile of valsartan: a potent, orally active, nonpeptide antagonist of the angiotensin II AT1-receptor subtype.

1. The pharmacological profile of valsartan, (S)-N-valeryl-N-([2'-(1H-tetrazol-5-yl)biphenyl-4-yl]-methyl)-vali ne, a potent, highly selective, and orally active antagonist at the angiotensin II (AII) AT1-receptor, was studied in vitro and in vivo. 2.

Angiotensin II binding sites on micro-organisms contaminating cell cultures.

An angiotensin II (Ang II) binding site, distinct from AT1 and AT2, has been found in cell cultures of rat aortic smooth muscle and rat glomerular mesangium. It is characterized by a high affinity for Ang II (Kd 0.75 +/- 0.

Biochemical characterization of two angiotensin II receptor subtypes in the rat.

Two angiotensin II receptor subtypes, A and B, have been described by means of specific and selective ligands (Biochem Biophys Res Commun 1989; 163:284-91). The present report describes the binding characteristics and the distribution of these subtypes in various rat tissues. Adrenal and uterus expressed both subtypes but in different proportions.

Three new epoxy-spirolactone derivatives: characterization in vivo and in vitro.

The use of spironolactone, the most commonly used antimineralocorticoid compound, is limited by the occurrence of sexual endocrine effects. New antagonists are therefore required which lack these unwanted effects. Three 9 alpha,11 alpha-epoxy-derivatives of known aldosterone antagonists (spironolactone, prorenone and mexrenone) have been characterised in vitro and in vivo.

Monoclonal antibodies against eucaryotic ribosomes. Use to characterize a ribosomal protein not previously identified and antigenically related to the acidic phosphoproteins P1/P2.

Mice were immunized against chick ribosomes with the use of various protocols and immunogen preparations. Hybridomas were prepared, clones screened, and specific antibodies identified by reversible protein staining followed by immunoperoxidase staining on nitrocellulose blots. Clones were obtained which secreted specific antibodies against ribosomal proteins S6, L7, L18a, P1/P2, and also against ribosomal RNA.

Evolutionary microdivergence of chick and rat liver ribosomal proteins.

We have set out to establish a nomenclature for ribosomal proteins which transcends, as far as is possible, the species from which the ribosomes were isolated. Initally, we identified individual proteins of rat liver by two-dimensional polyacrylamide gel electrophoresis and comparison with the classification system established by others (Sherton, C.C.