The regulation of amino acid incorporation into thyroid protein: Evidence that thyroxine and iodide inhibit protein synthesis at a ribosomal site

1966 ◽  
Vol 123 (1) ◽  
pp. 188-196 ◽  
Author(s):  
Stuart M. Heywood
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Amino Acid Incorporation ◽  
Inhibit Protein Synthesis ◽  
Acid Incorporation

scholarly journals INHIBITION OF PROTEIN SYNTHESIS IN NONINFECTED L CELLS BY PARTIALLY PURIFIED INTERFERON PREPARATIONS

1968 ◽  
Vol 36 (3) ◽  
pp. 617-624 ◽  
Author(s):  
Terry C. Johnson ◽  
Michael P. Lerner ◽  
Gerald J. Lancz
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Inhibitory Effect ◽  
Amino Acid Incorporation ◽  
Inhibit Protein Synthesis ◽  
Cell Monolayers ◽  
L Cells ◽  
Acid Incorporation ◽  
L Cell ◽  
Identical Manner

Partially purified interferon preparations, obtained from L-cell monolayers infected with Newcastle disease virus (NDV), were shown to inhibit protein synthesis in noninfected L cells. The incorporation of several amino acids-14C was equally sensitive to the pretreatment of the cells with the interferon preparation. Treatment of L-cell monolayers for 24 hr with 800 units of interferon resulted in a 50% decrease in amino acid incorporation. The degree of inhibition was found to be a function of the interferon concentration and the time of exposure of the cells to the partially purified preparations. No inhibitory effect was detected in medium obtained from noninfected cells and purified in an identical manner. The inhibitory effect was shown to be cell specific in that the partially purified interferon from L cells did not reduce amino acid incorporation in heterospecific cell lines. Heating the interferon preparations at 60°C destroyed their antiviral activity and their ability to inhibit valine-14C incorporation in L cells.

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 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.

Polysomal organization in growing and resting cultures and its relation to protein synthesis in Tetrahymena

1983 ◽  
Vol 59 (1) ◽  
pp. 121-131
Author(s):  
P. Isberner ◽  
G. Cleffmann
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Growth Conditions ◽  
The Other ◽  
Protein Accumulation ◽  
Resting Cells ◽  
Amino Acid Incorporation ◽  
Total Rna ◽  
Acid Incorporation ◽  
Other Hand

Cytosol from Tetrahymena cells growing at different rates was isolated and separated by centrifugation into polysomal and non-polysomal fractions. The RNAs of either fraction were separated chromatographically into poly(A)+ RNA and poly(A)-RNA. It was found that in resting cultures the total RNA per cell is only about half of that of rapidly growing cultures. All fractions of RNA were reduced proportionally. Thus, the percentage of polysomally bound total RNA (70% of cytosol RNA) and polysomally bound poly(A)+ RNA (72% of cytosol poly(A)+ RNA) is the same in growing and resting cultures. Differences, however, were found in the polysomal structure. Polysomes from resting cultures contained significantly fewer ribosomes. The amounts of RNA bound to polysomes were related to the rate of protein synthesis under different growth conditions. The decrease in cellular RNA corresponded well with the reduction in amino acid incorporation in resting cells. The rate of protein accumulation in resting cells, on the other hand, was considerably less, suggesting that polypeptides in resting cultures are less stable.

scholarly journals Biotin-mediated protein biosynthesis

1974 ◽  
Vol 140 (3) ◽  
pp. 549-556 ◽  
Author(s):  
R. L. Boeckx ◽  
K. Dakshinamurti
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Rat Liver ◽  
Intestinal Mucosa ◽  
Protein Biosynthesis ◽  
Amino Acid Incorporation ◽  
Acid Incorporation ◽  
Stimulation Of

The effect of administration of biotin to biotin-deficient rats on protein biosynthesis was studied. Biotin treatment resulted in stimulation by more than twofold of amino acid incorporation into protein, both in vivo and in vitro in rat liver, pancreas, intestinal mucosa and skin. Analysis of the products of amino acid incorporation into liver proteins in vivo and in vitro indicated that the synthesis of some proteins was stimulated more than twofold, but others were not stimulated at all. This indicates a specificity in the stimulation of protein synthesis mediated by biotin.

Effect of Curvularia lunata phytotoxin on membrane permeability of corn roots

1976 ◽  
Vol 54 (24) ◽  
pp. 2918-2923 ◽  
Author(s):  
A. Vianello ◽  
F. Macrì ◽  
C. Passera
Keyword(s):  
Protein Synthesis ◽  
Plasma Membrane ◽  
Amino Acid ◽  
Active Transport ◽  
Curvularia Lunata ◽  
Amino Acid Incorporation ◽  
Corn Roots ◽  
Acid Incorporation ◽  
Specific Membrane ◽  
General Plasma

Corn roots exposed to the Curvularia lunata phytotoxin show a decreased ability to absorb and to retain rubidium, sulphate, and leucine compared with control roots. The phytotoxin also decreased the amount of the amino acid incorporation into protein, whereas respiration was only slightly affected. The effect on active transport was more pronounced and rapid than loss of ions and inhibition of protein synthesis. The data suggest that the phytotoxin causes a general plasma membrane derangement similar to that caused by other phytotoxins, which results in a depression of the active transport, reflected in an inhibition of precursors of proteins and in a loss of ions. The toxin is to be regarded as a specific membrane poison.

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