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Biomedical subjects

F Chytil

Publications and source records attributed to F Chytil.

At least 127 records · Page 7Linked to original sources
PubMed1973

In vitro binding of retinol to rat-tissue components.

The high-speed supernatant fraction of rat liver, lung, kidney, testis, and intestinal mucosa contains a component capable of binding [(3)H]retinol in vitro when binding is analyzed by sucrose density gradient centrifugation or gel filtration. This binding component can be distinguished from one identified in rat serum. Whereas the tissue component sediments in the 2S region of sucrose gradients, the serum component sediments in the 4.6S region. Molecular weight estimations by gel filtration indicate molecular weights of 16,000 and 67,000 for the tissue and serum binding components, respectively. Unlabeled retinol, but not retinoic acid, competes for the binding of [(3)H]retinol in tissue cytosols. Competition for the binding of [(3)H]retinol by unlabeled retinal has also been observed in tissue cytosols, but may result from the in vitro reduction of retinal to retinol. Unlabeled retinol, retinal, and retinoic acid fail to compete for the binding of [(3)H]retinol in serum under the conditions used. The tissue binding component (testis) is sensitive to digestion with Pronase, but not with RNase or DNase, indicating a protein nature for this component.

Aldehydes↗
PubMed1972

Early effects of oestradiol-17 on the chromatin and activity of the deoxyribonucleic acid-dependent ribonucleic acid polymerases (I and II) of the rat uterus.

Oestradiol-17beta (1.0mug) was injected intravenously into ovariectomized rats. The earliest detectable hormonal response in isolated uterine nuclei was an increase (10-15min) in RNA polymerase II activity (DNA-like RNA synthesis), which reached a peak at 30min and then decreased to control values (by 1-2h) before displaying a second increase over control activity from 2 to 12h. The next response to oestradiol-17beta was an increase (30-60min) in polymerase I activity (rRNA synthesis) and template capacity of the chromatin. The concentrations of acidic chromatin proteins did not begin to increase until 1h after injection of oestradiol-17beta and histone concentrations showed no significant changes during the 8h period after administration. The early (15min) increase in RNA synthesis in ;high-salt conditions' can be completely eliminated by alpha-amanitin, an inhibitor of the RNA polymerase II. The exact nature of this early increase in endogenous polymerase II activity remains to be determined, e.g. whether it is caused by the increased availability of transcribable DNA of the chromatin or via direct hormonal activation of the enzyme per se.

Animals↗
PubMedDate not supplied

Localization of cellular retinol-binding protein and cellular retinoic acid-binding protein in the rat testis and epididymis.

The distribution of cellular retinol-binding protein (CRBP) and cellular retinoic acid-binding protein (CRABP) in rat testis and epididymis was examined by the peroxidase-antiperoxidase immunolocalization technique. In the testis, cellular retinol-binding protein was localized exclusively in the Sertoli cells. Staining varied with the stages of the seminiferous epithelium cycle and was maximal prior to the maturation divisions. Cellular retinoic acid-binding protein was localized exclusively in the germinal cells in the adluminal compartment. The results suggest that retinoic acid may be the retinoid form used by the germinal cells, and that Sertoli cells may use the cellular retinol-binding protein to transfer retinol from the basal to the adluminal compartment. In the epididymis, cellular retinol-binding protein was localized in the cytoplasm and stereocilia of the principal cells in the proximal caput epididymidis, while cellular retinoic acid-binding protein was localized in the spermatozoa and the stereocilia of the principal cells throughout the epididymis and in the epithelial cells of the distal vas deferens. Sperm staining intensity decreased from the initial segment to the cauda. The presence of high levels of cellular retinol-binding protein in the epithelial cells and high levels of cellular retinoic acid-binding protein in the spermatozoa of the caput epididymidis, known to be involved in the synthesis and secretion of factors necessary for sperm maturation, suggests that vitamin A may have a role in this process.

Animals↗