scholarly journals REFORMATION OF NUCLEOLI AFTER ETHIONE-INDUCED FRAGMENTATION IN THE ABSENCE OF SIGNIFICANT PROTEIN SYNTHESIS

1969 ◽  
Vol 41 (1) ◽  
pp. 280-286 ◽  
Author(s):  
Hisashi Shinozuka ◽  
Emmanuel Farber
Keyword(s):  
Protein Synthesis ◽  
Xenopus Laevis ◽  
Rat Liver ◽  
Actinomycin D ◽  
Compact Mass ◽  
Early Stages ◽  
Nucleolar Organization ◽  
Inhibition Of Protein Synthesis ◽  
Fibrillar Component

The rat liver nucleolus, after fragmentation induced by ethionine treatment, has been found to undergo complete reformation by adenine in the presence of a dose of cycloheximide sufficient to cause inhibition of protein synthesis by 90–95%. In contrast, actinomycin D given along with adenine was followed by the appearance of a small compact mass containing only the fibrillar component with no evident granules. This structure resembled pseudonucleoli seen in the anucleolate mutant of Xenopus laevis or in certain early stages of amphibian oocytes. Actinomycin D administered 2 hr after adenine induced a segregation of the fibrillar and granular components of nucleoli similar to that induced in the normal nucleolus. The implications of these findings in relation to nucleolar organization are briefly discussed.

scholarly journals Inhibition of protein synthesis in frog (Xenopus laevis) egg extracts by an antibody against phosphatidylinositol 4,5-bisphosphate

1996 ◽  
Vol 317 (3) ◽  
pp. 643-646
Author(s):  
Thomas J. KEATING ◽  
Kiyoko FUKAMI ◽  
Kenneth R. ROBINSON
Keyword(s):  
Protein Synthesis ◽  
Xenopus Laevis ◽  
Similar Reduction ◽  
Inhibition Of Protein Synthesis ◽  
Egg Extracts ◽  
Hydrolysis Of

The antibody kt10, which is directed against the phospholipid PtdIns(4,5)P2, inhibits protein synthesis when added to cytosolic extracts prepared from frog eggs. Addition of stable analogues of diacylglycerol and Ins(1,4,5)P3 failed to rescue the inhibition of translation, suggesting that the effect of the antibody was not to block hydrolysis of PtdIns(4,5)P2. Neomycin, which also binds PtdIns(4,5)P2, produced a similar reduction in protein-synthesis levels in the extract system, supporting the idea that it is the interaction of the antibody with PtdIns(4,5)P2 that is producing the effect.

Activated ribosomal RNA synthesis in regenerated rat liver upon inhibition of protein synthesis

1991 ◽  
Vol 15 (1) ◽  
pp. 45-52 ◽  
Author(s):  
Emil H. Nikolov ◽  
Bistra B. Nankova ◽  
Mariana D. Dabeva
Keyword(s):  
Protein Synthesis ◽  
Rat Liver ◽  
Ribosomal Rna ◽  
Rna Synthesis ◽  
Inhibition Of Protein Synthesis

scholarly journals Enhancement of the anti-anabolic response to adenosine 3′:5′-cyclic monophosphate during development. The inhibition of hepatic protein synthesis

1977 ◽  
Vol 168 (2) ◽  
pp. 271-275 ◽  
Author(s):  
A Klaipongpan ◽  
D P Bloxham ◽  
M Akhtar
Keyword(s):  
Protein Synthesis ◽  
Cyclic Amp ◽  
Rat Liver ◽  
Anabolic Response ◽  
Cyclic Monophosphate ◽  
Age Dependent ◽  
Inhibition Of Protein Synthesis ◽  
Dependent Inhibition ◽  
Hepatic Protein Synthesis

Cyclic AMP causes an age-dependent inhibition of protein synthesis in rat liver. The onset of inhibition is about 10—12 days after birth. The developmental response to cyclic AMP is associated with a change in the microsomal component of the protein-synthesizing system.

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