Alteration in the magnitude of induction of tyrosine transaminase by glucocorticoids

1969 ◽  
Vol 131 (1) ◽  
pp. 57-66 ◽  
Author(s):  
David Kupfer ◽  
Ruth Partridge ◽  
Trudy Munsell Jones
1972 ◽  
Vol 71 (2_Suppla) ◽  
pp. S369-S380 ◽  
Author(s):  
Francis T. Kenney ◽  
Kai-Lin Lee ◽  
Charles D. Stiles

ABSTRACT Analyses of the response of hydrocortisone-induced tyrosine transaminase in cultured H-35 cells to inhibitors of translation (cycloheximide, puromycin) suggest: (1) that bound ribosomes stabilize messenger RNA in vivo; (2) that messenger is degraded at a rate determined by the rate of translation. Since specific messenger RNAs of mammalian cells are degraded at quite different rates, there may be extensive heterogeneity either in the rate at which ribosomes traverse different messengers or in the number of ribosomes which translate specific messenger RNAs.


Life Sciences ◽  
1973 ◽  
Vol 12 (2) ◽  
pp. 49-56
Author(s):  
George P. Tryfiates ◽  
Edward F. Plow ◽  
Mark H. Hefner

1972 ◽  
Vol 50 (9) ◽  
pp. 1010-1015 ◽  
Author(s):  
Arthur J. Rizzo ◽  
Camille Kelly ◽  
Thomas E. Webb

Cordycepin (3′-deoxyadenosine), at a dose of 10 mg/kg, inhibits the accumulation of ribosomes in rat liver cytoplasm within 2.5 h of administration. This effect is not due to an inhibition of RNA synthesis per se but rather to the premature termination of the transcription of the 45 S ribosomal precursor in the presence of the analogue. The nucleoside analogue also inhibits the corticosteroid-mediated induction of tyrosine transaminase and general protein synthesis. The latter results are consistent with the current theory that cordycepin inhibits the formation of polyadenylic acid which is involved in the nuclear processing and/or nucleocytoplasmic transport of messenger RNA.


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