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Adenosine 3 :5-Cyclic Monophosphate (cAMP)-Inducible
Pyrimidine 5-Nucleotidase and Pyrimidine Nucleotide Metabolism
of Chick Embryonic Erythrocytes
Stefanie Dragon,
Rainer Hille,
Robert Götz, and
Rosemarie Baumann
From the Physiologisches Institut, Universität Regensburg,
Regensburg, Germany.
Terminally differentiating erythrocytes degrade most of their RNA
with subsequent release of mononucleotides. Pyrimidine mononucleotides are preferentially cleaved by an erythrocyte-specific pyrimidine 5 -nucleotidase; deficiency of this enzyme causes hemolytic
anemia in humans. Details of the regulation of its activity during
erythroid differentiation are unknown. The present study arose from the observation that the immature red blood cells (RBCs) of mid-term chick
embryos contain high concentrations of uridine 5-triphosphate (UTP) (5 to 6 mmol/L), which decline rapidly from days 13 to 14 onward.
We analyzed two key enzymes of RBC pyrimidine nucleotide metabolism:
pyrimidine nucleoside phosphorylase (PNP) and pyrimidine 5-nucleotidase (P-5-N), to evaluate if changes of enzyme
activity during embryonic development are correlated with changes of
RBC UTP. Secondly, we tested if these enzymes are under hormonal
control. The results show that embryonic RBCs contain only minimal
activity of PNP. In contrast, P-5-N increases from day 13 on,
suggesting that the enzyme is a limiting factor in UTP degradation.
Activation of  -adrenergic and A2A-adenosine receptors
causes transcription-dependent de novo synthesis of P-5-N.
Because -adrenergic and adenosine receptors are also found on adult
erythroid cells, P-5-N might be an enzyme of differentiating
RBCs whose expression is in part controlled by adenosine
3:5-cyclic monophosphate (cAMP).
Blood, Vol. 91 No. 8 (April 15), 1998:
pp. 3052-3058
© 1998 by The American Society of Hematology.
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