Morphogenetic disturbances from timed inhibitions of protein synthesis in Fundulus

Development ◽  
1973 ◽  
Vol 29 (2) ◽  
pp. 363-382
Author(s):  
Richard B. Crawford ◽  
Charles E. Wilde ◽  
Murk H. Heinemann ◽  
F. J. Hendler
Keyword(s):  
Protein Synthesis ◽  
Serial Order ◽  
Time Dependent ◽  
Amino Acid Incorporation ◽  
Active Expression ◽  
Dependent Protein ◽  
Early Zygote ◽  
The Times ◽  
Cleavage Failure ◽  
Ribosomal Complex

The reversible inhibition of protein synthesis at the 75–95% level in the early zygote of Fundulus results in a specific series of developmental failures dependent upon the times of inhibitor pulse initiation. The severity of the morphogenetic failure is inversely related to the time of initiation and directly to the length of the pulse. The defects reflect the time dependent serial order of events in morphogenesis. The defects range from failure of cleavage through disorders of blastulation, failure of axiation, anencephaly to microcephaly and are entirely predictable. With the exception of cleavage failure the pattern is identical with that found using pulses of actinomycin D in a similar manner. The agent used was pactamycin, an antibiotic which reversibly inhibits amino acid incorporation into protein by disturbing the assembly of the functional ribosomal complex. The significance of time dependent protein synthesis as an active expression in morphogenesis of similarly time dependent information flow via RNA synthesis is discussed.

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

scholarly journals Protein Synthesis in Human Leukocytes and Lymphocytes: 1. Effect of Steroids and Sterols

Blood ◽  
1969 ◽  
Vol 34 (3) ◽  
pp. 348-356 ◽  
Author(s):  
SEYMOUR WERTHAMER ◽  
CARL HICKS ◽  
LEONARD AMARAL
Keyword(s):  
Protein Synthesis ◽  
Steroid Hormones ◽  
Plasma Protein ◽  
Human Lymphocytes ◽  
Amino Acid Incorporation ◽  
Binding Factor ◽  
In Vitro Effects ◽  
Physiologic Role

Abstract The in vitro effects of sterols, cholesterol and 3-methyl cholanthrene and steroids, cortisol, prednisolone and testosterone on protein synthesis in separate popultions of human lymphocytes and leukocytes has been investigated. It has been shown that all agents used result in the inhibition of protein synthesis under these conditions. It has also been shown that the inhibitory mechanism of the steroid hormones requires the presence of plasma, presumably as a protein binding factor in order to achieve its effect. The sterol, cholesterol and 3-methyl cholanthrene, in the absence of plasma, still inhibit amino acid incorporation. However, in the case of cholesterol, the magnitude of inhibition is lower than that observed in the presence of plasma, perhaps indicating a partial plasma dependence. The results presented therefore support the hypothesis that the inhibition of lymphocyte protein synthesis by steroid hormones occurs only when the steroid is bound to a plasma protein. The physiologic role of the plasma protein-cortisol complex and its relation to the condition of lymphopenia in man is discussed.

Effect of Cycloheximide on In Vitro and In Vivo Protein Synthesis by Certain Tissues of Rats and Pigeons with Special Reference to Muscle

1973 ◽  
Vol 51 (12) ◽  
pp. 933-941 ◽  
Author(s):  
Njanoor Narayanan ◽  
Jacob Eapen
Keyword(s):  
Amino Acids ◽  
Body Weight ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Incorporation ◽  
Contrast Administration ◽  
Acid Incorporation ◽  
Tissue Homogenates

The effect of cycloheximide in vitro and in vivo on the incorporation of labelled amino acids into protein by muscles, liver, kidneys, and brain of rats and pigeons was studied. In vitro incorporation of amino acids into protein by muscle microsomes, myofibrils, and myofibrillar ribosomes was not affected by cycloheximide. In contrast, administration of the antibiotic into intact animals at a concentration of 1 mg/kg body weight resulted in considerable inhibition of amino acid incorporation into protein by muscles, liver, kidneys, and brain. This inhibition was observed in all the subcellular fractions of these tissues during a period of 10–40 min after the administration of the precursor. Tissue homogenates derived from in vivo cycloheximide-treated animals did not show significant alteration in in vitro amino acid incorporation with the exception of brain, which showed a small but significant enhancement.

scholarly journals Decomposition of time-dependent fluorescence signals reveals codon-specific kinetics of protein synthesis

2018 ◽  
Vol 46 (22) ◽  
pp. e130-e130 ◽  
Author(s):  
Nadin Haase ◽  
Wolf Holtkamp ◽  
Reinhard Lipowsky ◽  
Marina Rodnina ◽  
Sophia Rudorf
Keyword(s):  
Protein Synthesis ◽  
Time Dependent ◽  
Kinetics Of ◽  
Kinetics Of Protein Synthesis

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.

scholarly journals Action of growth hormone in vitro on the net uptake and incorporation into protein of amino acids in muscle from intact rabbits given protein-deficient diets

1976 ◽  
Vol 35 (1) ◽  
pp. 1-10 ◽  
Author(s):  
M. R. Turner ◽  
P. J. Reeds ◽  
K. A. Munday
Keyword(s):  
Amino Acids ◽  
Growth Hormone ◽  
Protein Synthesis ◽  
Amino Acid ◽  
De Novo ◽  
Amino Acid Uptake ◽  
Acid Uptake ◽  
Amino Acid Incorporation ◽  
Acid Incorporation

1. Net amino acid uptake, and incorporation into protein have been measured in vitro in the presence and absence of porcine growth hormone (GH) in muscle from intact rabbits fed for 5 d on low-protein (LP), protein-free (PF) or control diets.2. In muscle from control and LP animals GH had no effect on the net amino acid uptake but stimulated amino acid incorporation into protein, although this response was less in LP animals than in control animals.3. In muscle from PF animals, GH stimulated both amino acid incorporation into protein and the net amino acid uptake, a type of response which also occurs in hypophysectomized animals. The magnitude of the effect of GH on the incorporation of amino acids into protein was reduced in muscle from PF animals.4. The effect of GH on the net amino acid uptake in PF animals was completely blocked by cycloheximide; the uptake effect of GH in these animals was dependent therefore on de novo protein synthesis.5. It is proposed that in the adult the role of growth hormone in protein metabolism is to sustain cellular protein synthesis when there is a decrease in the level of substrate amino acids, similar to that which occurs during a short-term fast or when the dietary protein intake is inadequate.

Synthesis of 70K stress protein by human leukocytes: effect of exercise in the heat

1991 ◽  
Vol 70 (1) ◽  
pp. 466-471 ◽  
Author(s):  
A. J. Ryan ◽  
C. V. Gisolfi ◽  
P. L. Moseley
Keyword(s):  
Protein Synthesis ◽  
Relative Humidity ◽  
Treadmill Exercise ◽  
Stress Protein ◽  
Exercise Bout ◽  
Time Dependent ◽  
Dependent Manner ◽  
Human Leukocytes ◽  
Before And After

To determine whether reinduction of 70,000-Da (70K) stress protein synthesis could be used as an assay for thermal history and/or cellular levels of 70K stress protein in hyperthermic humans, leukocytes were obtained before and after 2 h of exercise and then incubated at 37 or 41 degrees C. Five healthy males completed 2 h of treadmill exercise consisting of running at 4–6 km/h for 30–45 min followed by 75–90 min of walking up a 2–10% grade. This exercise bout was performed by two subjects in hot (46 degrees C, 15% relative humidity) and by five subjects in cooler (30 degrees C, 40% relative humidity) environmental conditions. Exercise resulting in rectal temperature (Tre) less than 40 degrees C did not alter the amount of 70K stress protein synthesized by leukocytes incubated at 41 degrees C. In contrast, exercise resulting in Tre greater than 40 degrees C reduced the amount of 70K stress protein synthesized by leukocytes incubated at 41 degrees C. A protein immunoblot, probed with an antibody specific for the inducible 72K stress protein, showed that the reduction of 35S-labeled 70K stress protein in these postexercise leukocyte samples occurred without marked elevations of this protein. In vitro incubation of human leukocytes at 40 degrees C for 15–120 min reduced, in a time-dependent manner, the amount of 70K stress protein synthesized during a subsequent 41 degrees C heat stress. This reduction of 70K stress protein synthesis in 41 degrees C-treated leukocytes was abolished when cycloheximide was present during the 40 degrees C preincubation.(ABSTRACT TRUNCATED AT 250 WORDS)

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