Effects of cycloheximide, d-threo-chloramphenicol, erythromycin and actinomycin D on De-novo synthesis of cytoplasmic and mitochondrial proteins in the cotyledons of germinating pea seeds

Planta ◽  
1973 ◽  
Vol 114 (2) ◽  
pp. 169-184 ◽  
Author(s):  
S. S. Malhotra ◽  
T. Solomos ◽  
Mary Spencer
Keyword(s):  
Actinomycin D ◽  
De Novo ◽  
Mitochondrial Proteins ◽  
De Novo Synthesis ◽  
Pea Seeds

scholarly journals Evidence for the De Novo Synthesis of Erythropoietin in Hypoxic Rats

Blood ◽  
1972 ◽  
Vol 40 (5) ◽  
pp. 662-670 ◽  
Author(s):  
J. C. Schooley ◽  
L. J. Mahlmann
Keyword(s):  
Rna Synthesis ◽  
Actinomycin D ◽  
De Novo ◽  
Protein S ◽  
Male Rats ◽  
Hypoxic Exposure ◽  
De Novo Synthesis ◽  
Serum Erythropoietin

Abstract Significant increases in the serum erythropoietin of male rats occur after the end of a brief hypoxic exposure. These increases in the hormone are almost completely abolished when the kidneys are removed after the hypoxic exposure. Injection of puromycin or cycloheximide after the hypoxic exposure significantly decreases the subsequent increases in serum erythropoietin titers, whereas injections of actinomycin D at this time have no significant effect on erythropoietin levels. Injections of actinomycin D before the hypoxic exposure prevent the increase in serum erythropoietin that normally occurs. These findings suggest that a brief period of hypoxia initiates a DNA-dependent RNA synthesis that regulates the de novo ribosomal synthesis of protein(s) involved in the biogenesis of erythropoietin and that the kidney is essential for these reactions to occur.

scholarly journals EFFECTS OF CYTOSINE ARABINOSIDE ON DIFFERENTIAL GENE EXPRESSION IN EMBRYONIC NEURAL RETINA

1974 ◽  
Vol 61 (3) ◽  
pp. 688-700 ◽  
Author(s):  
R. E. Jones ◽  
A. A. Moscona
Keyword(s):  
Cytosine Arabinoside ◽  
Rna Synthesis ◽  
Actinomycin D ◽  
De Novo ◽  
Neural Retina ◽  
Regulatory Genes ◽  
De Novo Synthesis ◽  
Macromolecular Synthesis ◽  
Differential Gene ◽  
Inhibition Of Dna Synthesis

The analogue of cytidine, cytosine arabinoside (Ara-C), elicited a significant increase in the level of glutamine synthetase (GS) in embryonic chick neural retina in the absence of the steroid inducer of the enzyme. The increase was due to de novo synthesis of GS and was mediated by RNA which accumulated in the presence of the effective concentration of Ara-C. Accumulation of GS did not result from the inhibition of DNA synthesis for which Ara-C is best known. This new effect of Ara-C involves differential suppression of macromolecular synthesis in this system: the concentration of Ara-C which caused maximum GS accumulation suppressed overall protein and RNA syntheses 65–75% without inhibiting the transcription and translation of templates essential for GS synthesis. Withdrawal of Ara-C resulted in restoration of RNA synthesis and cessation of GS accumulation, even though preformed templates for the enzyme were present; however, if all RNA synthesis was arrested with actinomycin D at the time of Ara-C withdrawal, GS continued to accumulate. The results are consistent with the hypothesis that Ara-C differentially affects the activity of structural and regulatory genes involved in the regulation of GS levels in the retina: Ara-C allows transcription of the enzyme-specific templates, but reversibly inhibits the expression of regulatory genes which limit the accumulation of GS.

Studies on the nature of the seromucoid and haptoglobin responses to experimental inflammation

1968 ◽  
Vol 46 (5) ◽  
pp. 477-481 ◽  
Author(s):  
M. Maung ◽  
D. G. Baker ◽  
R. K. Murray
Keyword(s):  
Protein Synthesis ◽  
Actinomycin D ◽  
De Novo ◽  
De Novo Synthesis ◽  
Experimental Inflammation ◽  
Haptoglobin Level

The effects of the administration of actinomycin D, ethionine, and puromycin on the elevations of the total seromucoid fraction and of one of its components (haptoglobin) occurring during experimental inflammation have been studied. All three inhibitors of protein synthesis abolished the elevation of haptoglobin level. Ethionine and puromycin also completely suppressed the elevation of total seromucoid level, whereas actinomycin D only partially suppressed it. The seromucoid and haptoglobin levels in control animals injected with only the inhibitors of protein synthesis were not in general significantly different from those of the animals injected with turpentine and these agents. The results are consistent with the concept that the elevation of various plasma glycoproteins occurring during inflammation is principally due to de novo synthesis of these proteins rather than release of preformed proteins from tissue pools.

Salicylic acid treatment of pea seeds induces its de novo synthesis

2011 ◽  
Vol 168 (3) ◽  
pp. 213-219 ◽  
Author(s):  
Gabriella Szalai ◽  
Szabina Horgosi ◽  
Vilmos Soós ◽  
Imre Majláth ◽  
Ervin Balázs ◽  
...  
Keyword(s):  
Salicylic Acid ◽  
Acid Treatment ◽  
De Novo ◽  
De Novo Synthesis ◽  
Salicylic Acid Treatment ◽  
Pea Seeds

scholarly journals OBSERVATIONS ON THE ACID PHOSPHATASES OF EUGLENA GRACILIS

1965 ◽  
Vol 24 (2) ◽  
pp. 223-234 ◽  
Author(s):  
Jacob J. Blum
Keyword(s):  
Cell Division ◽  
Acid Phosphatase ◽  
Phosphatase Activity ◽  
Acid Phosphatase Activity ◽  
Actinomycin D ◽  
De Novo ◽  
Fluoride Concentration ◽  
Acid Phosphatases ◽  
De Novo Synthesis ◽  
Increased Activity

When a bleached strain of Euglena is maintained in a medium containing very low con centrations of phosphate, the acid phosphatase activity increases. The increase in acid phosphatase activity is prevented by Actinomycin D and by p-fluorophenylalanine (PFA), indicating that the increased activity is due to de novo synthesis of acid phosphatase. When phosphate is replenished, the acid phosphatase activity decreases to the level characteristic of uninduced cells before there is any appreciable cell division. When cell division resumes in the presence of PFA, the level of acid phosphatase activity remains approximately constant. This indicates that there are two different phosphatases: a constitutive enzyme, whose synthesis is insensitive to the presence of PFA, and an induced enzyme, whose synthesis is sensitive to PFA. These enzymes are not equally sensitive to changes in pH and in fluoride concentration, thus permitting them to be assayed individually in whole toluene-treated cells. Induced cells also acquire the ability to remove phosphate from the medium very rapidly.

Lipopolysaccharide stimulates de novo synthesis of PGH synthase in human alveolar macrophages

1992 ◽  
Vol 262 (1) ◽  
pp. L78-L85
Author(s):  
R. J. Pueringer ◽  
G. W. Hunninghake
Keyword(s):  
Arachidonic Acid ◽  
Alveolar Macrophage ◽  
Alveolar Macrophages ◽  
Actinomycin D ◽  
De Novo ◽  
Pge2 Production ◽  
De Novo Synthesis ◽  
New Synthesis ◽  
Human Alveolar Macrophages ◽  
Pg E2

Lipopolysaccharide (LPS)-stimulated human alveolar macrophages (HAMs) produce large amounts of prostaglandin (PG) E2 for up to 72 h. The mechanism of this enhanced and prolonged metabolism of arachidonic acid to PGE2 is unknown. To determine whether LPS-stimulated HAM PGE2 production is due in part to an increase in the new synthesis of the first committed enzyme, PGH synthase, we measured PGE2 formation, PGH synthase activity, and newly synthesized PGH synthase at 2, 6, and 24 h after LPS-stimulation. PGE2, measured by radioimmunoassay, was not increased at 2 h but was increased at 6 and 24 h after stimulating HAMs with LPS. Unstimulated HAMs did not produce PGE2. Likewise, the activity of PGH synthase extracted from HAMs was not increased at 2 h but was increased at 6 and 24 h after LPS stimulation. Cycloheximide and actinomycin D markedly inhibited PGE2 production in LPS-stimulated HAMs. Newly synthesized PGH synthase measured by immunoprecipitating 35S-labeled PGH synthase was not detected at 2 h but was detected at 6 and 24 h after stimulation. The parallel increases in PGE2 production, PGH synthase activity, and newly synthesized PGH synthase coupled with the dependence of PGE2 on the ability of the alveolar macrophage to synthesize protein suggest that LPS-stimulated HAM PGE2 production is in part regulated by the de novo synthesis of PGH synthase.

Ragweed-induced expression of GATA-3, IL-4, and IL-5 by eosinophils in the lungs of allergic C57BL/6J mice

2002 ◽  
Vol 282 (2) ◽  
pp. L302-L309 ◽  
Author(s):  
J. Paul Justice ◽  
M. T. Borchers ◽  
J. J. Lee ◽  
W. H. Rowan ◽  
Y. Shibata ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Bronchoalveolar Lavage Fluid ◽  
Actinomycin D ◽  
De Novo ◽  
Allergen Challenge ◽  
Lavage Fluid ◽  
Nuclear Factor Κb ◽  
De Novo Synthesis ◽  
A 23187 ◽  
The Relationship

Allergen-induced recruitment of T lymphocytes and eosinophils to the airways is associated with increased expression of the transcription factor GATA-3. In this study, the relationship between airway inflammation and GATA-3 expression in the lungs was investigated using ragweed-sensitized C57BL/6J mice. Intratracheal ragweed challenge increased both the number of GATA-3-expressing cells in the perivascular and peribronchial regions and the amount of expression per cell. Interleukin (IL)-4 and IL-5 levels in bronchoalveolar lavage fluid were upregulated in parallel with GATA-3 expression. GATA-3 mRNA and protein colocalized to eosinophils. Eosinophils isolated from the lungs and stimulated with phorbol 12-myristate 13-acetate and/or A-23187 released IL-5. The release was inhibited by actinomycin D, which indicates that de novo synthesis of the cytokine was involved. Western blot analysis of proteins from isolated eosinophils demonstrated expression of the p50 subunit of nuclear factor-κB, a transcription factor that is implicated in control of GATA-3 expression. These data provide evidence that allergen challenge increases GATA-3 and proinflammatory cytokine expression by pulmonary eosinophils, which could provide positive feedback for the inflammatory response.

Recovery of normal protein synthesis in heat-shocked chicken myotubes by liposome-mediated transfer of mRNAs

1985 ◽  
Vol 63 (3) ◽  
pp. 231-235 ◽  
Author(s):  
Jnanankur Bag
Keyword(s):  
Protein Synthesis ◽  
Heat Shock ◽  
Rna Synthesis ◽  
Actinomycin D ◽  
De Novo ◽  
Critical Role ◽  
Recovery Process ◽  
De Novo Synthesis ◽  
Normal Pattern ◽  
Large Unilamellar Vesicles

Exposure of chicken myotube culture to 45 °C induced the synthesis of three heat-shock polypeptides of 25 000, 65 000, and 81 000 daltons. Recovery to the normal pattern of protein synthesis was judged by the decrease in the synthesis of heat-shock polypeptides. This recovery to normal protein synthesis required de novo synthesis of mRNAs for normal cellular proteins. Inhibition of RNA synthesis by actinomycin D during recovery at 37 °C blocked the recovery process and resulted in the continued synthesis of heat-shock polypeptides. Large unilamellar vesicles were used to examine the effect of delivery of mRNAs isolated from both normal and heat-shocked myotubes on the recovery of these cells from heat-shock treatment. The results presented here show that liposome-mediated delivery of normal mRNAs to heat-shocked cells relieved the block of recovery by actinomycin. On the other hand, when mRNAs from heat-shocked cells were used during recovery, the synthesis of heat-shock polypeptides was stimulated. These observations suggest that the relative abundance of mRNAs in the cytoplasm plays a critical role in regulating protein synthesis in chicken myotube cultures.

Regulatory mechanisms of hepatic phosphorylase in fetal and neonatal livers of rats.

1977 ◽  
Vol 232 (4) ◽  
pp. E370
Author(s):  
R Biondi ◽  
M P Viola-Magni
Keyword(s):  
Actinomycin D ◽  
De Novo ◽  
Fetal Liver ◽  
Glycogen Metabolism ◽  
Regulatory Mechanisms ◽  
De Novo Synthesis ◽  
Neonatal Liver ◽  
Enzymatic Changes ◽  
Rat Livers

Active phosphorylase was determined in rat livers during the end of the fetal period and the first days of life. This enzyme increases between the 16th day of gestation and birth. After birth, another increase in observed that takes place with 6 h. In the neonatal liver, the rapid increase in active phosphorylase, is inhibited by high levels of blood glucose, but is unaffected by actinomycin D. In fetal liver glucagon administration is followed after 5 h by an increase in total phosphorylase with only a small increase in active phosphorylase; this effect is blocked by actinomycin D. The fetal changes are interpreted as de novo synthesis, whereas the neonatal increase is due to an activation of inactive phosphorylase. Both enzymatic changes appear to be regulated by glycogen. The role of phosphorylase in the regulation of glycogen metabolism in neonatal liver is discussed.

Thyroid Hormone-Induced Changes in Cytoplasmic and Mitochondrial Proteins of a Teleost

1998 ◽  
Vol 53 (1-2) ◽  
pp. 120-124 ◽  
Author(s):  
G. Tripathi
Keyword(s):  
Skeletal Muscle ◽  
Actinomycin D ◽  
De Novo ◽  
Mitochondrial Protein ◽  
Mitochondrial Proteins ◽  
Cytoplasmic Protein ◽  
Freshwater Teleost ◽  
Mitochondrial Fractions ◽  
Induced Changes ◽  
Induced Proteins

AbstractThe effect of triiodothyronine (T3) on the cytoplasmic and mitochondrial protein contents were studied in the liver and skeletal muscle of a freshwater teleost. The fish exposed to thiouracil for 28 days showed 1.5-2 times reduction in the total protein contents of cytoplasmic and mitochondrial fractions. A single injection of T3 to thiouracil exposed fish caused the earliest induction in the liver and skeletal muscle mitochondrial protein and the skeletal muscle cytoplasmic protein at 12 hr of lapses. However, the initial induction in the cytoplasmic protein of the liver was observed at 3 hr after T3 treatment. The maximum inductions (1.5-3.2 fold) in the cytoplasmic and mitochondrial proteins of the liver and skeletal muscle were obtained at 1 8 -2 4 hr following hormonal administration. Thereafter, the cytoplasmic and mitochondrial protein contents of both the tissues declined to their control levels within 3 6 - 4 8 hr of T3 injection which reflected the half-life and turnover period of the induced proteins. These T3 dependent inductions in the cytoplasmic and mitochondrial proteins of the liver (1 .4 -3 .2 fold) and skeletal muscle (1.8 -2.7 fold) were inhibited by actinomycin D and cycloheximide indicating T3-induced de novo synthesis of the proteins. The induction in the cytoplasmic protein (3 fold) was almost double to that of the mitochondrial protein (1.6 fold) suggesting more synthesis of protein molecules in the cytoplasm for cellular and subcellular activities.

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