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J Biol Chem, Vol. 274, Issue 2, 755-761, January 8, 1999
From the Institute of Physiology, Medical Faculty,
Pauwelsstrasse 30, D-52057 Aachen, Germany
ATP is known to act as an extracellular signal in
many organs. In the heart, extracellular ATP modulates ionic processes
and contractile function. This study describes a novel, metabolic effect of exogenous ATP in isolated rat cardiomyocytes. In these quiescent (i.e. noncontracting) cells, micromolar
concentrations of ATP depressed the rate of basal,
catecholamine-stimulated, or insulin-stimulated glucose transport by up
to 60% (IC50 for inhibition of
insulin-dependent glucose transport, 4 µM).
ATP decreased the amount of glucose transporters (GLUT1 and GLUT4) in
the plasma membrane, with a concomitant increase in intracellular microsomal membranes. A similar glucose transport inhibition was produced by P2 purinergic agonists with the following rank
of potencies: ATP 
ATP
S 2-methylthio-ATP
(P2Y-selective) > ADP > 
,
meATP
(P2X-selective), whereas the P1 purinoceptor
agonist adenosine was ineffective. The effect of ATP was suppressed by the poorly subtype-selective P2 antagonist
pyridoxal-phosphate-6-azophenyl-2',4'-disulfonic acid but,
surprisingly, not by the nonselective antagonist suramin nor by the
P2Y-specific Reactive Blue 2. Glucose transport inhibition by ATP was not affected by a drastic reduction of the extracellular concentrations of calcium (down to 10
9 M) or
sodium (down to 0 mM), and it was not mimicked by a
potassium-induced depolarization, indicating that purinoceptors of the
P2X family (which are nonselective cation channels whose
activation leads to a depolarizing sodium and calcium influx) are not
involved. Inhibition was specific for the transmembrane transport of
glucose because ATP did not inhibit (i) the rate of glycolysis under
conditions where the transport step is no longer rate-limiting nor (ii)
the rate of [1-14C]pyruvate decarboxylation. In
conclusion, extracellular ATP markedly inhibits glucose transport in
rat cardiomyocytes by promoting a redistribution of glucose
transporters from the cell surface to an intracellular compartment.
This effect of ATP is mediated by P2 purinoceptors,
possibly by a yet unknown subtype of the P2Y purinoceptor family.
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