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The goal of this study was to determine the validity of using N 6 -etheno-bridged adenine nucleotides to evaluate ecto-nucleotidase activity. We observed that the metabolism of N 6 -etheno-ATP versus ATP was quantitatively similar when incubated with recombinant CD39, ENTPD2, ENTPD3, or ENPP-1, and the quantitative metabolism of N 6 -etheno-AMP versus AMP was similar when incubated with recombinant CD73. This suggests that ecto-nucleotidases process N 6 -etheno-bridged adenine nucleotides similarly to endogenous adenine nucleotides. Four cell types rapidly (t 1/2 , 0.21 to 0.66 h) metabolized N 6 -etheno-ATP. Applied N 6 -etheno-ATP was recovered in the medium as N 6 -etheno-ADP, N 6 -etheno-AMP, N 6 -etheno-adenosine, and surprisingly N 6 -etheno-adenine; intracellular N 6 -etheno compounds were undetectable. This suggests minimal cellular uptake, intracellular metabolism, or deamination of these compounds. N 6 -etheno-ATP, N 6 -etheno-ADP, N 6 -etheno-AMP, N 6 -etheno-adenosine, and N 6 -etheno-adenine had little affinity for recombinant A 1 , A 2A , or A 2B receptors, for a subset of P2X receptors ( 3 H-α,β-methylene-ATP binding to rat bladder membranes), or for a subset of P2Y receptors ( 35 S-ATP-αS binding to rat brain membranes), suggesting minimal pharmacological activity. N 6 -etheno-adenosine was partially converted to N 6 -etheno-adenine in four different cell types; this was blocked by purine nucleoside phosphorylase (PNPase) inhibition. Intravenous N 6 -etheno-ATP was quickly metabolized, with N 6 -etheno-adenine being the main product in naïve rats, but not in rats pretreated with a PNPase inhibitor. PNPase inhibition reduced the urinary excretion of endogenous adenine and attenuated the conversion of exogenous adenosine to adenine in the renal cortex. The N 6 -etheno-bridge method is a valid technique to assess extracellular metabolism of adenine nucleotides by ecto-nucleotidases. Also, rats express an enzyme with PNPase-like activity that metabolizes N 6 -etheno-adenosine to N 6 -etheno-adenine.

purinergic signalling

Characterization of the N6-etheno-bridge method to assess extracellular metabolism of adenine nucleotides: detection of a possible role for purine nucleoside phosphorylase in adenosine metabolism