scholarly journals THE EFFECT OF PROTEIN SYNTHESIS INHIBITION ON THE ENTRY OF MESSENGER RNA INTO THE CYTOPLASM OF SEA URCHIN EMBRYOS

1971 ◽  
Vol 49 (3) ◽  
pp. 692-701 ◽  
Author(s):  
Brigid Hogan ◽  
Paul R. Gross
Keyword(s):  
Protein Synthesis ◽  
Sea Urchin ◽  
Messenger Rna ◽  
Potent Inhibitor ◽  
Protein Synthesis Inhibition ◽  
Embryonic Cells ◽  
Synthesis Inhibition ◽  
Uridine Incorporation ◽  
Sea Urchin Embryos ◽  
Inhibitor Of Protein Synthesis

Emetine is a potent inhibitor of protein synthesis in sea urchin embryos. At a concentration of the drug that rapidly inhibits protein synthesis in blastulae by 95%, uridine incorporation into RNA continues for more than 1 hr and presumptive histone messenger RNA is synthesized and transported into the cytoplasm where it is apparently associated with polyribosomes. Possible explanations of this result and its implications for the "informasome" theory of messenger transport in embryonic cells are discussed.

scholarly journals SYNTHESIS AND STORAGE OF MICROTUBULE PROTEINS BY SEA URCHIN EMBRYOS

1971 ◽  
Vol 50 (2) ◽  
pp. 516-528 ◽  
Author(s):  
Rudolf A. Raff ◽  
Gerald Greenhouse ◽  
Kenneth W. Gross ◽  
Paul R. Gross
Keyword(s):  
Amino Acids ◽  
Sea Urchin ◽  
Messenger Rna ◽  
Binding Activity ◽  
Total Soluble Protein ◽  
Cell Stage ◽  
Lytechinus Pictus ◽  
Sea Urchin Embryos ◽  
Tritiated Amino Acids ◽  
Vinblastine Sulfate

Studies employing colchicine binding, precipitation with vinblastine sulfate, and acrylamide gel electrophoresis confirm earlier proposals that Arbacia punctulata and Lytechinus pictus eggs and embryos contain a store of microtubule proteins. Treatment of 150,000 g supernatants from sea urchin homogenates with vinblastine sulfate precipitates about 5% of the total soluble protein, and 75% of the colchicine-binding activity. Electrophoretic examination of the precipitate reveals two very prominent bands. These have migration rates identical to those of the A and B microtubule proteins of cilia. These proteins can be made radioactive at the 16 cell stage and at hatching by pulse labeling with tritiated amino acids. By labeling for 1 hr with leucine-3H in early cleavage, then culturing embryos in the presence of unlabeled leucine, removal of newly synthesized microtubule proteins from the soluble pool can be demonstrated. Incorporation of labeled amino acids into microtubule proteins is not affected by culturing embryos continuously in 20 µg/ml of actinomycin D. Microtubule proteins appear, therefore, to be synthesized on "maternal" messenger RNA. This provides the first protein encoded by stored or "masked" mRNA in sea urchin embryos to be identified.

Protein synthesis inhibition alters Drosophila mating behavior

1977 ◽  
Vol 6 (3) ◽  
pp. 355-357 ◽  
Author(s):  
Anita Pruzan ◽  
Philip B. Applewhite ◽  
Michael J. Bucci
Keyword(s):  
Protein Synthesis ◽  
Mating Behavior ◽  
Protein Synthesis Inhibition ◽  
Synthesis Inhibition

Focal protein synthesis inhibition in a model of neonatal hypoxic-ischemic brain injury

1987 ◽  
Vol 95 (2) ◽  
pp. 277-289 ◽  
Author(s):  
Barney E. Dwyer ◽  
Robert N. Nishimura ◽  
Clydette L. Powell ◽  
Susan L. Mailheau
Keyword(s):  
Protein Synthesis ◽  
Brain Injury ◽  
Ischemic Brain Injury ◽  
Protein Synthesis Inhibition ◽  
Ischemic Brain ◽  
Synthesis Inhibition ◽  
Hypoxic Ischemic Brain Injury

scholarly journals Effects on protein synthesis of injecting synthetic polyribonucleotides into living cells

1974 ◽  
Vol 144 (1) ◽  
pp. 11-19 ◽  
Author(s):  
Hugh Woodland ◽  
Sarah E. Ayers
Keyword(s):  
Protein Synthesis ◽  
Xenopus Laevis ◽  
Potent Inhibitor ◽  
Living Cells ◽  
Initiation Factor ◽  
Rna Molecules ◽  
Endogenous Protein ◽  
Limited Supply ◽  
Inhibitor Of Protein Synthesis ◽  
Haemoglobin Synthesis

Micro-injection into the oocytes and eggs of Xenopus laevis was used to ascertain the effects of synthetic polyribonucleotides on protein synthesis in living cells. Poly(U) and poly(A) were not translated detectably, nor did they change the rate of endogenous protein synthesis. The same was true of poly(G,U), poly(A,G,U), poly(A,C,G,U), G-U-G-(U)n, A-(U)n and AUG. In contrast, A-U-G-(U)n was a potent inhibitor of protein synthesis in the cell. This might be because it is initiated normally but lacks a termination codon, or because it inhibits the translation of other molecules in some way not dependent on its normal initiation. Poly(G,U), poly(A,G,U) and poly(A,C,G,U) inhibited haemoglobin synthesis when they were injected into the oocyte with haemoglobin mRNA. The synthetic polyribonucleotides did not inhibit the translation of the natural mRNA when the two sorts of molecules were injected at different times. It is suggested that the synthetic RNA molecules compete with the natural mRNA for a pre-initiation factor in limited supply.

Protein Synthesis Inhibition and Oxidative Stress Induced by Cylindrospermopsin Elicit Apoptosis in Primary Rat Hepatocytes

2013 ◽  
Vol 26 (2) ◽  
pp. 203-212 ◽  
Author(s):  
Henar López-Alonso ◽  
Juan Andrés Rubiolo ◽  
Félix Vega ◽  
Mercedes R. Vieytes ◽  
Luis M. Botana
Keyword(s):  
Oxidative Stress ◽  
Protein Synthesis ◽  
Rat Hepatocytes ◽  
Protein Synthesis Inhibition ◽  
Synthesis Inhibition ◽  
Primary Rat Hepatocytes ◽  
And Oxidative Stress

scholarly journals Protein synthesis in rabbit reticulocytes: mechanism of protein synthesis inhibition by heme-regulated inhibitor.

1979 ◽  
Vol 76 (10) ◽  
pp. 5076-5079 ◽  
Author(s):  
A. Das ◽  
R. O. Ralston ◽  
M. Grace ◽  
R. Roy ◽  
P. Ghosh-Dastidar ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Protein Synthesis Inhibition ◽  
Synthesis Inhibition ◽  
Rabbit Reticulocytes
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