scholarly journals Histone acetylation and hormone action. Early effects of oestradiol-17β on histone acetylation in rat uterus

1972 ◽  
Vol 130 (3) ◽  
pp. 663-669 ◽  
Author(s):  
P. R. Libby

The effect of oestradiol treatment on the acetylation of histones of the immature rat uterus has been studied. A 10μg dose of oestradiol causes a 70% increase at 5min and a 140% increase at 10min after administration in the labelling of the histone fraction F2+F3. No effect of oestradiol is seen on the labelling of histones F1 or acidic non-histone chromatin proteins. The oestradiol stimulation is seen in animals pretreated with either cycloheximide or actinomycin D. The stimulation of labelling caused by oestradiol is completely abolished by pretreatment of the animals with the anti-oestrogen, nafoxidine. The stimulation is given by lower doses of oestradiol, by stilboestrol and oestriol, but is not given by testosterone. These results suggest that stimulation of histone acetylation in the uterus is the earliest known effect of the hormone on its target tissue.

1971 ◽  
Vol 125 (2) ◽  
pp. 605-614 ◽  
Author(s):  
J. T. Knowler ◽  
R. M. S. Smellie

Stimulation of incorporation of labelled precursors into the RNA of immature rat uterus is an early result of oestradiol-17β action. However, the extent of the increased incorporation varies with the mode of administration of the labelled precursors and with the weight of the rat. At the age and weight range normally used response is maximal at ten times control incorporation, 4h after the administration of 0.3μg or more of oestradiol-17β. Under these conditions the stimulation of incorporation into the acid-soluble fraction is only 2–2.5-fold. When the purified RNA is separated on polyacrylamide gels the major increase in incorporation of radioactive precursor is found in rRNA and 4S RNA; the formation of the former has been followed from the 45S precursor. Preceding these events by at least 30min, however, is an increase in the incorporation of precursor into RNA species of very high molecular weight, which remained in the first few slices of the gel. The possible significance of these findings is discussed. The increased synthesis of rRNA in response to oestradiol-17β is more strongly inhibited by actinomycin D than the synthesis of other RNA species. Cycloheximide, depending on time of administration and dosage, inhibits either RNA synthesis or the maturation of rRNA.


1968 ◽  
Vol 42 (2) ◽  
pp. 261-NP ◽  
Author(s):  
F. A. DUGAN ◽  
B. RADHAKRISHNAMURTHY ◽  
R. A. RUDMAN ◽  
G. S. BERENSON

SUMMARY Glycoproteins from immature and immature, oestrogen-stimulated and adult rat uteri were isolated and analysed by chemical and gel electrophoretic methods. Esterase, acid phosphatase, alkaline phosphatase and peroxidase activities were found. Changes in electrophoretic mobilities of certain enzyme bands in polyacrylamide gel were also observed after hydrolysis of the preparations with neuraminidase. These latter observations and chemical analyses provide additional evidence of the carbohydrate nature of the enzymes. The influence of 17β-oestradiol on immature rat uteri caused a significant increase in total protein and sialic acid per uterus compared with controls. Oestrogen treatment also resulted in an increase in the total activity of esterase and acid and alkaline phosphatases per uterus, but there was no increase in specific activities. Observations of electrophoretic patterns of glycoprotein preparations from untreated and oestrogen-stimulated, immature uteri did not show the evolution to a more adult pattern by oestrogen stimulation. These studies show that stimulation with oestrogen increases the synthesis of glycoprotein in the immature rat uterus. Factors which are involved in the more intricate control of glycoprotein biosynthesis need to be elucidated.


1973 ◽  
Vol 134 (4) ◽  
pp. 907-912 ◽  
Author(s):  
Paul R. Libby

Histone acetylation in the kidney of the adrenalectomized rat was increased 5 min after a physiological dose of aldosterone. The increase was exclusively in the histone F2a1. The increase in histone acetylation was given by 9α-fluorocortisol, deoxycorticosterone and cortisol, but not by progesterone. The increase in histone acetylation was abolished by prior treatment of the animals with the anti-mineralocorticoid agent, SC14266 [potassium 3-(3-oxo-17β-hydroxy-4,6-androstadien-17-yl) propionate]; the basal degree of histone acetylation was unaffected. Pretreatment of the animals with actinomycin D or cyclo-heximide did not affect the stimulation, showing the stimulation was not due to increased synthesis of enzyme.


Biochimie ◽  
1976 ◽  
Vol 58 (4) ◽  
pp. 443-454 ◽  
Author(s):  
Jean-Louis Borgan ◽  
Jean-Claude Bonnafous ◽  
Magdeleine Mousseron-Canet ◽  
Jean-Calaude Mani ◽  
Catherine Cazaubon

1974 ◽  
Vol 77 (1) ◽  
pp. 64-70 ◽  
Author(s):  
Gustav Wägar

ABSTRACT Whether the short-term regulation of thyroidal protein synthesis by TSH occurs at the transcriptional or the translational level was tested by measuring the effect of actinomycin D (act D) on the TSH-induced stimulation of L-14C-leucine incorporation into the thyroidal proteins of rats. TSH was injected 6 h before the rats were killed. The thyroid glands were then removed and incubated in vitro in the presence of L-14C-leucine for 2 h. The pronounced stimulation of leucine incorporation in the TSH-treated animals was depressed as compared with controls but still significant even when the animals had been pre-treated with 100 μg act D 24 and 7 h before sacrifice. On the other hand, act D strongly decreased incorporation of 3H-uridine into RNA. Short-term regulation of thyroidal protein synthesis by TSH appears to be partly but not wholly dependent on neosynthesis of RNA. Hence regulation may partly occur at the translation level of protein synthesis.


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