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J Biol Chem, Vol. 273, Issue 36, 23093-23097, September 4, 1998
From the Department of Pharmacology-0636, University of California,
San Diego, La Jolla, California 92093-0636
Extracellular nucleotides regulate function in
many cell types via activation of multiple
P2-purinergic receptor subtypes. However, it has been
difficult to define which individual subtypes mediate responses to the
physiological agonist ATP. We report a novel means to determine this by
exploiting the differential activation of an autocrine/paracrine
signaling pathway. We used Madin-Darby canine kidney epithelial cells
(MDCK-D1) and assessed the regulation of cAMP formation by nucleotides.
We found that ATP, 2-methylthio-ATP (MT-ATP) and UTP increase cAMP
production. The cyclooxygenase inhibitor indomethacin completely
inhibited UTP-stimulated, did not inhibit MT-ATP-stimulated, and only
partially blocked ATP-stimulated cAMP formation. In parallel studies,
ATP and UTP but not MT-ATP stimulated prostaglandin production. By pretreating cells with indomethacin to eliminate the
P2Y2/prostaglandin component of cAMP formation, we could
assess the indomethacin-insensitive P2 receptor component.
Under these conditions, ATP displayed a ten-fold lower potency for
stimulation of cAMP formation compared with untreated cells. These data
indicate that ATP preferentially activates P2Y2 relative to
other P2 receptors in MDCK-D1 cells (P2Y1 and
P2Y11, as shown by reverse transcriptase polymerase chain
reaction) and that P2Y2 receptor activation is the
principal means by which ATP increases cAMP formation in these cells.
Blockade of autocrine/paracrine signaling can aid in dissecting the
contribution of multiple receptor subtypes activated by an agonist.
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