scholarly journals Anti-anabolic effects of adenosine 3′:5′-cyclic monophosphate. Inhibition of protein synthesis

1974 ◽  
Vol 138 (3) ◽  
pp. 335-340 ◽  
Author(s):  
Anthony Sellers ◽  
David P. Bloxham ◽  
Kenneth A. Munday ◽  
Muhammad Akhtar
Keyword(s):  
Protein Synthesis ◽  
Cyclic Amp ◽  
Rat Liver ◽  
Physiological Role ◽  
Free System ◽  
Cell Free System ◽  
Cyclic Monophosphate ◽  
Anabolic Action ◽  
Inhibition Of Protein Synthesis ◽  
A Cell

1. Evidence is presented that cyclic AMP inhibits the incorporation of l-[4,5-3H]leucine into protein in a cell-free system from rat liver. This inhibition occurs after aminoacyl-tRNA formation. 2. Microsomal fractions, isolated after the incubation of postmitochondrial supernatant with cyclic AMP and ATP, show a diminished ability to synthesize protein. Both cyclic AMP and ATP are required for this effect. 3. A possible physiological role for the anti-anabolic action of cyclic AMP is discussed in terms of the control of gluconeogenesis.

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.

scholarly journals Inhibition of protein synthesis in Krebs 2 ascites cells and cell-free systems by phenylalanine and its effect on leucine and lysine in the amino acid pool

1968 ◽  
Vol 109 (4) ◽  
pp. 507-515 ◽  
Author(s):  
Joan P. Roscoe ◽  
M. D. Eaton ◽  
Gladys Chin Choy
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Specific Radioactivity ◽  
Transfer Rna ◽  
Free System ◽  
Cell Free System ◽  
Whole Cells ◽  
System L ◽  
Inhibition Of Protein Synthesis ◽  
A Cell

1. The inhibition of incorporation of 14C-labelled amino acids into protein of whole cells by phenylalanine has been reproduced in a cell-free system. In both cases only the l-isomer was inhibitory. 2. The effect of phenylalanine on incorporation of [14C]leucine and [14C]lysine into protein was different in both whole cells and cell-free systems. 3. In whole cells inhibition of incorporation of leucine at 2·5μg./ml. was very rapid, but when the concentration was increased to 100μg./ml. the inhibition was not apparent for about 1hr. The kinetics of inhibition of lysine was the same at both these concentrations and was similar to that found with leucine at 100μg./ml. 4. Neither a lower specific radioactivity of the two amino acids in the pool nor a decrease in their pool size could be consistently related with inhibition of protein synthesis. 5. In the cell-free system l-phenylalanine inhibited the incorporation of leucine but not of lysine. 6. Charging of transfer RNA by leucine was markedly decreased in the presence of phenylalanine, whereas charging of transfer RNA by lysine was not.

scholarly journals Trafficking of lipids from the endoplasmic reticulum to the Golgi apparatus in a cell-free system from rat liver

1991 ◽  
Vol 266 (7) ◽  
pp. 4322-4328 ◽  
Author(s):  
P Moreau ◽  
M Rodriguez ◽  
C Cassagne ◽  
D M Morré ◽  
D J Morré
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Apparatus ◽  
Rat Liver ◽  
Free System ◽  
Cell Free System ◽  
A Cell
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