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Vol. 287, Issue 3, 926-930, December 1998
Center for Clinical Pharmacology, Departments of Pharmacology and
Medicine, University of Pittsburgh Medical Center, Pittsburgh,
Pennsylvania
In the rat kidney, exogenous adenosine-3'-5'-monophosphate (cAMP) is
converted to adenosine via the metabolism of cAMP to adenosine-5'-monophosphate by phosphodiesterase and
adenosine-5'-monophosphate to adenosine by 5'-nucleotidase. Our purpose
was to investigate whether in the rat kidney adenosine is synthesized
from endogenous cAMP via the same pathway. Rat kidneys were perfused
with Tyrode's solution, and stabilized for 3 hr to minimize basal
renal purine secretion. In control experiments (n = 6),
the renal venous secretion rate of adenosine, inosine, hypoxanthine and
purines (adenosine + inosine + hypoxanthine) did not
change over the two 10-min experimental periods. In contrast, the
beta adrenoceptor agonist (±)-isoproterenol (1 and 10 µM
added to the perfusate) caused a significant (1-factor analysis of
variance with repeated measures; n = 31) increase in
the renal venous secretion of adenosine (P < .0001), inosine (P < .0007), hypoxanthine (P < .0007) and purines
(P < .0001) as measured by high-performance liquid chromatography
with ultraviolet detection. The purines was the most discriminating
index of isoproterenol-induced changes in purine release, and the renal
venous secretion of purines was significantly (2-factor analysis of
variance with repeated measures) attenuated by inhibition of
beta adrenoceptors with propranolol (.1 µM,
n = 6; P < .05), phosphodiesterase with
3-isobutyl-1-methylxanthine (1 mM, n = 5; P < .002) and 5'-nucleotidase with
,
-methyleneadenosine-5'-diphosphate (0.1 mM, n = 5; P < .03). Our data indicate that activation of beta
adrenoceptors increases purine biosynthesis in the rat kidney via a
mechanism that involves phosphodiesterase and 5'-nucleotidase. These
results support the existence of an endogenous cAMP-adenosine pathway
in the rat kidney.
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