Cycloheximide Inhibition of Cytokinin-dependent Protein Synthesis: Correlation with Betacyanin Synthesis

1983 ◽  
Vol 10 (2) ◽  
pp. 145
Author(s):  
D.C Elliott ◽  
A Koltunow
Keyword(s):  
Protein Synthesis ◽  
Biological Response ◽  
Leucine Incorporation ◽  
Basal Rate ◽  
Dependent Protein ◽  
Lag Period

Cytokinin-dependent betacyanin accumulation in Amaranthus trlcolor half-seedlings (cotyledons plus 5-mm hypocotyls) can be detected after a lag period of about 6 h. A significant (P<O.01) promotion by cytokinin of [3H]leucine incorporation into protein was observed at 5-7 h. It is concluded that the cytokinin-induced biological response was subsequent to or at the same time as the effect on protein synthesis and therefore could be dependent on it, a conclusion that is strengthened by the correlation between the effects of cycloheximide on the two processes. Cycloheximide preferentially inhibits cytokinin-dependent protein synthesis as compared to the effect of the inhibitor on the basal rate.

EFFECT OF ACTINOMYCIN D ON TSH-INDUCED STIMULATION OF THYROIDAL PROTEIN SYNTHESIS IN THE RAT

1974 ◽  
Vol 77 (1) ◽  
pp. 64-70 ◽  
Author(s):  
Gustav Wägar
Keyword(s):  
Protein Synthesis ◽  
Actinomycin D ◽  
The Other ◽  
Leucine Incorporation ◽  
Short Term ◽  
Other Hand ◽  
Thyroid Glands ◽  
Translational Level ◽  
Stimulation Of

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.

scholarly journals P2-202: INHIBITION OF ACTIVITY-DEPENDENT PROTEIN SYNTHESIS BY IL-1β IN HIPPOCAMPAL DENDRITES

2019 ◽  
Vol 15 ◽  
pp. P654-P654
Author(s):  
G. Aleph Prieto ◽  
Erica D. Smith ◽  
Liqi Tong ◽  
Michelle Nguyen ◽  
Carl W. Cotman
Keyword(s):  
Protein Synthesis ◽  
Dependent Protein ◽  
Activity Dependent

Use of an in Vitro Protein Synthesizing System to Test the Mode of Action of Chloracetamides

Weed Science ◽  
1980 ◽  
Vol 28 (3) ◽  
pp. 334-340 ◽  
Author(s):  
Luanne M. Deal ◽  
J. T. Reeves ◽  
B. A. Larkins ◽  
F. D. Hess
Keyword(s):  
Protein Synthesis ◽  
Sand Culture ◽  
Leucine Incorporation ◽  
Insoluble Protein ◽  
In Vitro System ◽  
A Cell ◽  
Protein Incorporation ◽  
Vitro Protein

The effects of chloracetamides on protein synthesis were studied both in vivo and in vitro. Four chloracetamide herbicides, alachlor [2-chloro-2′,6′-diethyl-N-(methoxymethyl)acetanilide], metolachlor [2-chloro-N-(2-ethyl-6-methylphenyl)-N-(2-methoxy-1-methylethyl)acetamide], CDAA (N–N-diallyl-2-chloroacetamide), and propachlor (2-chloro-N-isopropylacetanilide) were tested for inhibition of [3H]-leucine incorporation into protein. Incorporation of3H-leucine into trichloroacetic acid (TCA)-insoluble protein was inhibited in oat (Avena sativaL. ‘Victory’) seedlings grown in sand culture and treated 12 h at 1 × 10−4M with these chloracetamides. The herbicides were also tested in a cell-free protein synthesizing system containing polyribosomes purified from oat root cytoplasm. These herbicides had no effect on the rates of polypeptide elongation nor on the synthesis of specific polypeptides when herbicides (1 × 10−4M) were added directly to the system. Polypeptide formation was inhibited 89% when 1 × 10−4M cycloheximide was added during translation. Cytoplasmic polyribosomes were isolated from oat roots treated 12 h with 1 × 10−4M herbicide. Translation rates and products were not altered when these polyribosomes were added to the in vitro system. Protein synthesis is inhibited when tested in an in vivo system; however, the inhibition does not occur during the translation of mRNA into protein.

Initiation in einem Polyribosomen-abhängigen Protein-synthetisierenden zellfreien System aus Saccharomyces / Initiation in a Polyribosome-Dependent Protein-Synthesizing Cell-Free System from Saccharomyces

1976 ◽  
Vol 31 (3-4) ◽  
pp. 169-173 ◽  
Author(s):  
Bernd Schulz-Harder ◽  
Ernst-Randolf Lochmann
Keyword(s):  
Protein Synthesis ◽  
Free System ◽  
Cell Free System ◽  
Aurintricarboxylic Acid ◽  
Dependent Protein ◽  
A Cell

Abstract A method to prepare polyribosomes from yeasts by using the french-press is described. The highest yield of polyribosomes was derived from late log-phase cells. These polyribosomes, incubated in a cell-free system, were able to reinitiate protein synthesis, which was shown by inhibiting aminoacid incorporation by aurintricarboxylic acid, edeine and sodiumfluoride. We developed the translational system in order to look for the optimal ion-conditions of a DNA-dependent protein-synthesizing system. We found out that at the optimal MgCL2-concentration (6 mᴍ) protein synthesis was strongly inhibited by Mangan ions which are required for transcription in yeast. If protein-synthesis was carried out with 2 mᴍ and 3 mᴍ MgCl2 maximal aminoacid incorporation was observed at 2 mᴍ and 1.5 mᴍ MnCl2.

Abstract 15161: Adiponectin Exerts a Protective Role Against Vascular Remodeling During Hypertension

Circulation ◽  
2015 ◽  
Vol 132 (suppl_3) ◽  
Author(s):  
Crystal M Ghantous ◽  
Sarah Hanache ◽  
Firas Kobaissy ◽  
Asad Zeidan
Keyword(s):  
Protein Synthesis ◽  
Vascular Remodeling ◽  
Mechanical Stretch ◽  
Protective Role ◽  
Leucine Incorporation ◽  
Rat Portal Vein ◽  
Length Relationship ◽  
Longitudinal Orientation ◽  
Ros Formation

Introduction: Hypertension is associated with leptin production and ROS formation in vascular smooth muscle cells (VSMC) and contributes to vascular remodeling. Adiponectin (ADQ) has a cardioprotective role on the heart, but the protective role of ADQ on VSMC during hypertension has not been fully elucidated yet. Hypothesis: Mechanical stretch/hypertension is associated with a low ADQ/leptin ratio in VSMC, leading to VSMC remodeling. Methods: To mimic hypertension, the rat portal vein was cultured either mechanically stretched with 1.2 gram weights (due to the force-length relationship normalized to the human force of stretch during hypertension and the longitudinal orientation of its VSMC) or left unstretched. ADQ, leptin, eNOS, p-ERK1/2 and p-AKT expression in VSMC was evaluated by Western blot. The protective effect of adiponectin (5-10 μg/ml; 15 min-24 hr) was investigated on ROS formation by DHE staining and on hypertrophy by protein synthesis via [ 3 H]leucine incorporation. Results: Mechanical stretch for 24 hr reduced the expression of ADQ in VSMC (0.49 ± 0.08 fold, n=6, p<0.05) and increased leptin (2.51 ± 0.39 fold, n=6, p<0.05) compared to controls. Stretch (24 hr) decreased ADQ mRNA expression by 0.31 ± 0.11 fold (n=7, p<0.05) and ADQ receptor R2 by 0.51 ± 0.21 fold (n=7, p<0.05) but had no effect on ADQ receptor R1 (n=8). This effect of stretch was associated with increased protein synthesis by 1.39 ± 0.06 fold (n=6, p<0.05), while exogenous ADQ significantly inhibited stretch-induced hypertrophy (n=6, p<0.05). Stretch (15 min) increased p-ERK1/2 and p-AKT by 2.10 ± 0.25 and 4.03 ± 0.61 fold respectively (n=5, p<0.05), but ADQ reduced p-ERK1/2 and p-AKT by 0.82 ± 0.26 and 0.55 ± 0.25 fold respectively (n=3, p<0.05) in stretched vessels. eNOS expression decreased by 0.70 ± 0.06 fold (n=5, p<0.05) after stretch for 24 hr, while ADQ increased eNOS in stretched veins by 2.02 ± 0.41 fold (n=3, p<0.05). Stretch for 1 hr increased ROS by 5.69 ± 0.13 fold (n=3, p<0.05), whereas ADQ significantly inhibited ROS in stretched vessels (1.71 ± 0.22 fold, n=3). Conclusion: Mechanical stretch reduces the ADQ/leptin ratio in VSMC. ADQ plays a protective role against vascular remodeling during hypertension by affecting eNOS, ERK, AKT, ROS and hypertrophy.

Abstract 22: Crosstalk Between Phosphotidylinositol-4,5 Bisphosphonate-3 Kinase Pathway and Mitogen-Activated Protein Kinase Pathway Regulates Platelet Activation and Protein Synthesis via Phosphoinositide-Dependent Kinase-1

2017 ◽  
Vol 37 (suppl_1) ◽  
Author(s):  
Bhanu Kanth Manne ◽  
Patrick Münzer ◽  
Rachit Badolia ◽  
Andrew S. Weyrich ◽  
Satya P Kunapuli ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Protein Kinase ◽  
Platelet Activation ◽  
Mapk Pathway ◽  
Mitogen Activated Protein Kinase ◽  
Genetic Ablation ◽  
Upstream Kinase ◽  
Dependent Protein ◽  
Kinase Pathway ◽  
Pharmacologic Inhibition

Phosphoinositide-dependent protein kinase 1 (PDK1) is known to regulate PAR4 induced platelet activation and thrombus formation through GSK3β. However, whether PDK1 signaling also involves the ADP receptor and, if so, downstream functional consequences are unknown. We employed both pharmacologic (e.g. the selective PDK1 inhibitor, BX795) and genetic (platelet specific deletion of PDK1) approaches to dissect the role of PDK1 in ADP-induced platelet activation and protein synthesis. Inhibition of PDK1 with BX795 reduced 2MeSADP-induced platelet aggregation by abolishing thromboxane generation. Similar results were observed in PDK1 -/- mice (Fig A). Inhibition of PDK1 protected mice from collagen and epinephrine-induced pulmonary embolism (Fig B). PDK1 was also necessary for the phosphorylation of MEK1/2, Erk1/2 and cPLA2, indicating that PDK1 regulates an upstream kinase in MAPK pathway. We next identified that this upstream kinase is Raf1 (necessary for the phosphorylation of MEK1/2), as pharmacologic inhibition and genetic ablation of PDK1 was sufficient to prevent Raf1 phosphorylation (Fig C). Pharmacologic inhibition and genetic ablation of PDK1 blocked MAPK- and mTORC1-dependent protein synthesis in platelets through a mechanism requiring the phosphorylation of eIF4E and S6K. Concordantly, PDK1 is necessary for signal-dependent synthesis of the protein bcl3, which is under mTORC1-dependent control (Fig C). Taken together, our findings show for the first time that PDK1, a master kinase in the PI3K pathway, directly governs thromboxane generation, thrombosis, and protein synthesis in platelets through regulating MAPK and mTORC1 pathways.

Protein and Nucleic Acid Syntheses in Dark-dormant Common Purslane(Portulaca oleracea)Seed

Weed Science ◽  
1978 ◽  
Vol 26 (6) ◽  
pp. 669-672 ◽  
Author(s):  
Bonnie J. Reger ◽  
Ida E. Yates
Keyword(s):  
Protein Synthesis ◽  
Nucleic Acid ◽  
Rna Synthesis ◽  
Acid Synthesis ◽  
Portulaca Oleracea ◽  
Dark Incubation ◽  
Radicle Protrusion ◽  
Lag Period ◽  
Common Purslane ◽  
H Protein

Dark-incubated common purslane(Portulaca oleraceaL.) seed synthesize very little protein and essentially no nucleic acids. Dark-incubated seed incorporate only 14 × 10−3nmoles14C-leucine/mg protein/12-h dark. In contrast, seed exposed to 12-h light following 24-h dark incubation incorporate 365 × 10−3-nmoles14C-leucine/mg protein/12-h light. Once dormancy is broken by exposure of seed to light, initiation of radicle protrusion occurs at 12 h. Protein synthesis gradually increases with time in the light and precedes nucleic acid synthesis which is associated with radicle protrusion. During the 12-h lag period preceding radicle protrusion protein synthesis increases significantly by 3 to 9 h in light, RNA synthesis by 9 h in light, and DNA synthesis by 12 h in light. After 12 h in light,32P can be detected in all nucleic acid fractions, DNA and RNAs.

Increase in Cap- and IRES-Dependent Protein Synthesis by Overproduction of Translation Initiation Factor eIF4G

2000 ◽  
Vol 277 (1) ◽  
pp. 117-123 ◽  
Author(s):  
Satoko Hayashi ◽  
Kazuhiro Nishimura ◽  
Tomomi Fukuchi-Shimogori ◽  
Keiko Kashiwagi ◽  
Kazuei Igarashi
Keyword(s):  
Protein Synthesis ◽  
Translation Initiation ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Dependent Protein
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