The reversal of inhibition of protein synthesis by double-stranded RNA in lysed rabbit reticulocytes with fructose 6-phosphate

1979 ◽  
Vol 86 (3) ◽  
pp. 648-653 ◽  
Author(s):  
Joseph M. Wu ◽  
Chi P. Cheung ◽  
Alan R. Bruzel ◽  
Robert J. Suhadolnik
Keyword(s):  
Protein Synthesis ◽  
Double Stranded Rna ◽  
Inhibition Of Protein Synthesis ◽  
Rabbit Reticulocytes

Phosphorylation and the control of protein synthesis

1983 ◽  
Vol 302 (1108) ◽  
pp. 127-134 ◽  
Keyword(s):  
Protein Synthesis ◽  
Protein Kinases ◽  
Molecular Mechanism ◽  
The Other ◽  
Initiation Factor ◽  
Reversible Phosphorylation ◽  
Double Stranded Rna ◽  
Inhibition Of Protein Synthesis ◽  
The One ◽  
Rabbit Reticulocytes

This paper reviews the evidence that protein synthesis in rabbit reticulocytes is regulated by the reversible phosphorylation of the initiation factor eIF-2 by protein kinases under the control of the cytoplasmic haemin concentration on the one hand, and double-stranded RNA on the other. A molecular mechanism is proposed to account for the observation that inhibition of protein synthesis occurs when considerably less than half the eIF-2 present has been phosphorylated. The question of whether phosphorylation regulates protein synthesis in other types of cell is discussed.

scholarly journals Inhibition of protein synthesis by a toxic lectin from Viscum album L. (mistletoe)

1980 ◽  
Vol 190 (3) ◽  
pp. 843-845 ◽  
Author(s):  
F Stirpe ◽  
R F Legg ◽  
L J Onyon ◽  
P Ziska ◽  
H Franz
Keyword(s):  
Protein Synthesis ◽  
Viscum Album ◽  
Lag Time ◽  
Cells In Culture ◽  
Inhibition Of Protein Synthesis ◽  
Gross Lesions ◽  
Rabbit Reticulocytes

1. The haemagglutinating and toxic lectin from Viscum album L. (mistletoe) inhibits protein synthesis in a lysate of rabbit reticulocytes, with an ID50 (concentration giving 50% inhibition) of 2.6 microgram/ml. This effect is enhanced (ID50 0.21 microgram/ml) if the lectin is reduced with 2-mercaptoethanol. 2. The lectin inhibits protein synthesis also in BL8L cells in culture. Inhibition occurs after a lag time of 3 h. The ID50 is 7 ng/ml, and increases after reduction of the lectin. 3. This and the gross lesions observed in rats poisoned with V. album lectin indicate this is a toxin very similar to ricin.

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