Mechanism of action of oxazolidinones: effects of linezolid and eperezolid on translation reactions.

The oxazolidinones are a new class of synthetic antibiotics with good activity against gram-positive pathogenic bacteria. Experiments with a susceptible Escherichia coli strain, UC6782, demonstrated that in vivo protein synthesis was inhibited by both eperezolid (formerly U-100592) and linezolid (formerly U-100766). Both linezolid and eperezolid were potent inhibitors of cell-free transcription-translation in E.

Estrogen sulfotransferase of the rat liver: complementary DNA cloning and age- and sex-specific regulation of messenger RNA.

Mammalian estrogen sulfotransferase (EST; EC 2.8.2.

Androgen receptor messenger ribonucleic acid (mRNA) in the rat liver: changes in mRNA levels during maturation, aging, and calorie restriction.

By means of RNAase protection assay with an antisense cRNA probe, we have shown that the liver of the young adult male rat contains androgen receptor (AR) mRNA to a level of 4% compared to the prostate. Steady state levels of AR mRNA in the liver show both sex and age specificity. Compared to that of the male, the female liver contains a markedly reduced amount of AR mRNA.

Loss of androgenic induction of alpha 2u-globulin gene family in the liver of NIH black rats.

Unlike all known strains of rat, the androgen-inducible alpha 2u-globulin gene family is totally silent in the liver of NIH black (NB) rats. No endocrinological or reproductive abnormalities are apparent, and the mRNA for the androgen-repressible hepatic protein SMP-2 is normally regulated in these animals. Furthermore, immunoblot analysis shows a normal level of the male-specific cytoplasmic androgen-binding protein.

Purification and immunochemical characterization of the cytoplasmic androgen-binding protein of rat liver.

The cytoplasmic androgen-binding (CAB) protein of the male rat liver has been implicated to play a role in the androgen-dependent regulation of alpha 2u-globulin synthesis. The liver of the adult male rat contains about 50 fmol of specific high-affinity androgen-binding activity per milligram of total cytosolic protein. Photoaffinity labeling with [3H]R-1881 followed by SDS-polyacrylamide gel electrophoresis and autoradiography shows that the CAB is a 31-kilodalton protein.