scholarly journals Histone acetylation and hormone action. Early effects of aldosterone on histone acetylation in rat kidney

1973 ◽  
Vol 134 (4) ◽  
pp. 907-912 ◽  
Author(s):  
Paul R. Libby
Keyword(s):  
Histone Acetylation ◽  
Actinomycin D ◽  
Rat Kidney ◽  
Prior Treatment ◽  
Hormone Action ◽  
Early Effects ◽  
Physiological Dose

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.

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
Keyword(s):  
Histone Acetylation ◽  
Actinomycin D ◽  
Target Tissue ◽  
Not Given ◽  
Rat Uterus ◽  
Histone Fraction ◽  
Immature Rat ◽  
Chromatin Proteins ◽  
Early Effects ◽  
Stimulation Of

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.

Transport of RNA from nucleus to cytoplasm following mitogenic stimulation of human lymphocytes

1978 ◽  
Vol 56 (6) ◽  
pp. 659-666 ◽  
Author(s):  
Mary Mitchell ◽  
Enzo Bard ◽  
Rod L'Anglais ◽  
J. G. Kaplan
Keyword(s):  
Actinomycin D ◽  
Human Lymphocytes ◽  
Cell Types ◽  
Resting Cells ◽  
Con A ◽  
Mitogenic Stimulation ◽  
Gene Transcripts ◽  
Early Effects ◽  
Nucleolar Rna ◽  
Kinetics Of

An improved method affording clean separation of nuclei from cytoplasm was utilized to study the kinetics of appearance of [3H]uridine-labelled polyadenylated (poly(A)+) and nonpolyadenylated (poly(A)−) RNA in the cytoplasm of human lymphocytes stimulated with the mitogen concanavalin A (Con A). While our previous and present studies utilizing lymphocyte preparations purified on Ficoll-Hypaque gradients had shown that the earliest observable increase in labelled total cell RNA occurred after 12 h of exposure to Con A, we were here able to detect highly significant increases in levels of uridine-labelled poly(A)− RNA in the cytoplasm of lymphocytes which had been exposed to mitogen for 6 h; these cells had been pulsed with [3H]uridine for 2 h prior to harvest. This suggested that the early effects of mitogen may be to increase processing and transport of RNA rather than to increase the production of gene transcripts. At least 13 h of exposure to Con A was required before labelled poly(A)+ RNA appeared in the cytoplasmic extracts of stimulated cells and it did not appear in those of resting cells. The lag between addition of isotope and appearance of labelled RNA in cytoplasm was inversely related to the duration of incubation of the cells with mitogen. However, once the label appeared in the cytoplasm, its rate of appearance and its final level were similar at both 12 and 36 h of incubation with Con A. These kinetic data also suggest that mitogen acts mainly to accelerate the processing and transport of RNA at least during the first 12 h of mitogenic stimulation. A concentration (0.05 μg/ml) of actinomycin D which is known to inhibit specifically the transcription of nucleolar RNA in a variety of cell types was found to affect the transcription of poly(A)+ RNA in human lymphocytes; in some experiments, specific inhibition of nucleolar RNA synthesis was observed at 0.005 μg actinomycin D per millilitre.

scholarly journals Cell-shape-dependent modulation of p52(PAI-1) gene expression involves a secondary response pathway

1995 ◽  
Vol 306 (2) ◽  
pp. 497-504 ◽  
Author(s):  
P J Higgins ◽  
L Staiano-Coico ◽  
M P Ryan
Keyword(s):  
Protein Synthesis ◽  
Transcriptional Activation ◽  
Actinomycin D ◽  
De Novo ◽  
Rat Kidney ◽  
Secondary Response ◽  
Protein Levels ◽  
Run Off ◽  
Dependent Pathway ◽  
Pai 1

Expression of the rat p52(PAI-1) gene is positively regulated by agents that influence cellular microfilament organization and/or cell-to-substrate adhesion [e.g. cytochalasin D (CD) and sodium n-butyrate (NaB)] [Higgins, Chaudhari and Ryan (1991) Biochem. J. 273, 651-658; Higgins, Ryan and Providence (1994) J. Cell. Physiol. 159, 187-195]. As shape-responsive genes may be subject to inducer-specific controls, the biochemical mechanisms underlying the shape-dependent pathway of p52(PAI-1) gene regulation were examined in v-ras-transformed rat kidney (KNRK) cells. NaB and/or CD effectively stimulated p52(PAI-1) run-off transcription and augmented de novo p52(PAI-1) mRNA and protein synthesis in KNRK cells; induction at both the mRNA and protein levels was inhibited by actinomycin D. Pretreatment with cycloheximide (CX) markedly attenuated NaB- and/or CD-stimulated p52(PAI-1) expression. CX alone, however, induced low levels of p52(PAI-1) mRNA; increased p52(PAI-1) protein synthesis was evident after release of KNRK cells from CX blockade. Such CX-mediated induction was also sensitive to actinomycin D. Full stimulation of p52(PAI-1) expression in KNRK cells in response to the shape modulators NaB and/or CD involves transcriptional activation of the p52(PAI-1) gene, requires de novo RNA synthesis and occurs through a secondary-response (i.e. protein-synthesis-dependent) pathway.

BABIES, HORMONES AND KIDNEYS—A NEW LOOK AT DEVELOPMENT

PEDIATRICS ◽  
1972 ◽  
Vol 50 (1) ◽  
pp. 3-4
Author(s):  
Wallace W. McCrory
Keyword(s):  
Cyclic Amp ◽  
Rat Kidney ◽  
Adenyl Cyclase ◽  
Endocrine Gland ◽  
Hormone Action ◽  
Abundant Evidence ◽  
Cell Target ◽  
Urinary Cyclic Amp ◽  
Adenyl Cyclase System

The role of cyclic AMP (adenosine 3’,5’-monophosphate) in hormone action is now quite firmly established. Abundant evidence now demonstrates that after release from an endocrine gland a hormone (first messenger) is transported to its effector cell (target) where it interacts with the adenyl cyclase system to release cyclic AMP (second messenger) which acts intracellularly to carry out the work of the hormone. In 1967, Chase and Aurbach demonstrated that urinary cyclic AMP, now known to be derived from both plasma and kidney, increased when parathormone (PTH) was administered to the rat and man. These workers also demonstrated a PTH-sensitive adenyl cyclase in the proximal tubules of the rat kidney and in fetal bone.

scholarly journals Antagonistic effect of actinomycin D and cycloheximide on estradiol-induced activation of rat kidney enzymes

1992 ◽  
Vol 58 ◽  
pp. 134
Author(s):  
Shiro Suzuki ◽  
Junko Yoshida ◽  
Keigo Sugiki ◽  
Masao Imai ◽  
Osamu Niwa
Keyword(s):  
Actinomycin D ◽  
Rat Kidney ◽  
Antagonistic Effect

Inhibition of hexose transport in adipocytes by dexamethasone: role of protein synthesis

1985 ◽  
Vol 248 (2) ◽  
pp. E215-E223
Author(s):  
C. Carter-Su ◽  
K. Okamoto
Keyword(s):  
Protein Synthesis ◽  
Effective Dose ◽  
Glucose Oxidation ◽  
Actinomycin D ◽  
Hexose Transport ◽  
Hormone Action ◽  
Transport Assay ◽  
Isolated Rat ◽  
Synthetic Glucocorticoid

The ability of the synthetic glucocorticoid, dexamethasone, to alter 3-O-methylglucose transport was investigated using isolated rat adipocytes. A maximally effective dose of dexamethasone (10(-7) M) inhibited transport up to 80% within 60–90 min. Inhibition of transport was evident as early as 15–30 min after addition of steroid, and was prevented by both actinomycin D and cycloheximide. When added within 45 or 60 min after dexamethasone, actinomycin D interfered with the cells' ability to respond to the steroid but had no effect when added between 60 and 90 min or longer after the steroid. Cycloheximide interfered with steroid-induced inhibition of transport when added at any time before the 15- to 30-min period immediately preceding the transport assay. This interference with hormone action appeared to be independent of the length of time cells were exposed to dexamethasone before addition of cycloheximide. Thus cells that were maximally inhibited by dexamethasone by 90 min became only partially inhibited when cycloheximide was added at 90 or 120 min, and cells were incubated for an additional 60 or 30 min, respectively. These findings are consistent with the following: dexamethasone inhibits glucose oxidation as a result of inhibiting hexose transport; inhibition of transport by dexamethasone requires the synthesis of RNA during the first 45–60 min after steroid addition and requires protein synthesis during the entire incubation period with dexamethasone; and transport is inhibited within minutes after protein synthesis is initiated.

Receptors and effectors in hormone action on the kidney

1981 ◽  
Vol 241 (4) ◽  
pp. F333-F339 ◽  
Author(s):  
I. S. Edelman
Keyword(s):  
Rat Kidney ◽  
Receptor Occupancy ◽  
Hormone Action ◽  
Na Transport ◽  
Receptor Complexes ◽  
Glycerophosphate Dehydrogenase ◽  
Transepithelial Na Transport ◽  
Aldosterone Receptor ◽  
Nuclear Abundance ◽  
Molecular Bases

An analysis is presented of the similarities and differences in receptor-effector relationships in the actions of aldosterone and triiodothyronine on the kidney. Both agents augment tubular reabsorption of sodium at different sites in the nephron. Aldosterone acts primarily distally and triiodothyronine, primarily proximally. In both cases, the respective hormone-receptor complexes associate with target cell chromatin and modulate the abundance of specific coding by mRNAs for regulatory proteins. The quantitative relationships between nuclear-receptor occupancy and responses were analyzed by fractional plots in a bounded domain. When applied to the toad bladder, this analysis revealed a parabolic dependence of the increase in transepithelial Na+ transport on the abundance of nuclear of the increase in transepithelial Na+ transport on the abundance of nuclear aldosterone-receptor complexes. In contrast, four independent response parameters (QO2, QO2(t), Na-K-ATPase, alpha-glycerophosphate dehydrogenase) exhibited a hyperbolic dependence on nuclear abundance of T3 in the rat kidney. The observed cosaturation of nuclear occupancy and responses in both systems, for both hormones, implies that the respective high-affinity binding sites are authentic receptors. Further information is needed on the molecular bases of the nonlinear response-occupancy relationships in hormone action on the kidney.

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