Adenosine, cyclic AMP metabolism, and glycogenolysis in rat liver cells.

Rat liver cells rapidly metabolized adenosine added to the medium by incorporating the adenosine into nucleotides or oxidizing it to uric acid. In the presence of allopurinol (4hydroxypyrazolo(3,4-d)pyrimidine) the formation of uric acid was blocked and hypoxanthine accumulated as the end product of adenosine catabolism. Adenosine added to the medium at concentrations up to 20 PM was almost completely removed by liver cells during the first 5 min of incubation. In the presence of 200 PM adenosine about half of the adenosine was present after a 20-min incubation of rat liver cells in the presence of allopurinol and erythro-9(2-hydroxy-3-nonyl) adenine which is an inhibitor of adenosine deaminase. There was no increase in adenosine release by rat liver cells incubated with 270 nM glucagon. Adenosine release could be accelerated by valinomycin which markedly elevated labeled AMP and phosphorylase a. Valinomycin was only effective as an activator of phosphorylase a in the presence of calcium in the medium. In contrast cyanide and dinitrophenol worked equally well as activators of phosphorylase a in regular or calcium-free buffer. Adenosine (200 PM) inhibited the stimulation of glycogenolysis by glucagon or epinephrine in isolated rat liver cells. Basal glycogenolysis and the increases due to valinomycin were unaffected by 200 FM adenosine. In contrast, 100 PM 2’,5’-dideoxyadenosine was ineffective as an inhibitor of glycogenolysis while 10 PM dideoxyadenosine was much more potent than 200 PM adenosine as an inhibitor of cyclic AMP accumulation by intact rat liver cells. Similarly, 5 to 10 PM 2’,5’-dideoxyadenosine reduced the activation of adenylate cyclase by glucagon to about the extent as 50 to 100 PM adenosine. Neither 200 PM adenosine nor 50 FM 2’,5’dideoxyadenosine affected glycogen phosphorylase a activity. These data suggest that the inhibition of hormone-activated glycogenolysis seen in the presence of 200 P.M adenosine is not secondary to inhibition of cyclic AMP accumulation in rat liver cells. Furthermore, the results with 2’,5’dideoxyadenosine suggest that modulation of phosphorylase

• Publication year

  1977

• Venue

  Journal of Biological Chemistry

• Publication date

  1977-11-25

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1016/s0021-9258(17)40937-9PMID 199600
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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