Activities of cAMP-dependent protein kinase and enzymes of 2',5'-oligoadenylate metabolism in NIH 3T3 cells deepening into the resting state.
The activity of cAMP-dependent protein kinase was found to increase continuously in the NIH 3T3 cells, deepening into the resting state. The increase correlated with intracellular level of heat-stable protein inhibitor of the protein kinase rather than with the cAMP content. The elevation of 2',5'-oligo(A) synthetase activity and the decrease in 2'-phosphodiesterase activity were also observed in the cells sinking into the resting state. The variations in enzyme activities were similar to those caused by the increase in the intracellular cAMP content described elsewhere. These results agree with the idea that the cAMP-dependent protein kinase is involved in the regulation of the enzymes of 2',5'-oligo(A) metabolism.
Itkes
A V
AV
Kartasheva
O N
ON
Tunitskaya
V L
VL
Turpaev
K T
KT
Kafiani
C A
CA
Severin
E S
ES
D015088:2',5'-Oligoadenylate Synthetase / Q000378:metabolism*; D000227:Adenine Nucleotides / Q000378:metabolism*; D000818:Animals; D002460:Cell Line; D000242:Cyclic AMP / Q000378:metabolism; D005095:Exoribonucleases / Q000378:metabolism*; D007399:Interphase; D051379:Mice; D009841:Oligonucleotides / Q000378:metabolism*; D009843:Oligoribonucleotides / Q000378:metabolism*; D047428:Protein Kinase Inhibitors; D011494:Protein Kinases / Q000378:metabolism*
D000227:Adenine Nucleotides; D009841:Oligonucleotides; D009843:Oligoribonucleotides; D047428:Protein Kinase Inhibitors; C023505:2',5'-oligoadenylate; D000242:Cyclic AMP; D011494:Protein Kinases; D015088:2',5'-Oligoadenylate Synthetase; D005095:Exoribonucleases; C029364:2'-phosphodiesterase