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Journal of Neuroscience, Vol 7, 3306-3316, Copyright © 1987 by Society for Neuroscience
Dependence of an adenosine-activated potassium current on a GTP-binding protein in mammalian central neurons
LO Trussell and MB Jackson
Department of Biology, University of California, Los Angeles 90024.
Neurons in hippocampal and striatal cell cultures respond to adenosine with
an inhibitory potassium current. This response disappears during whole-cell
patch-clamp recording in which the cell is filled with minimal saline. We
have found that this loss of sensitivity to adenosine can be prevented by
including 100 microM GTP in the patch electrode filling solution. GDP is
less effective than GTP in supporting the adenosine response, while GMP has
little, if any, effect. Treatments known to inhibit GTP-binding proteins
(G-proteins) block the adenosine-activated potassium current: The adenosine
response is inhibited by including poorly metabolized analogs of guanine
nucleotides along with GTP in the recording electrode. Diphosphate and
triphosphate analogs appear to achieve this effect through different
mechanisms. The adenosine response is also blocked by incubating cultures
in islet-activating protein (pertussis toxin), an inhibitor of a class of
G-protein. Thus, our data implicate a G-protein in the activation of a
potassium current by adenosine. Intracellular ATP can increase the
effectiveness of GMP, GDP, or low concentrations of GTP, suggesting that
even during internal dialysis, neurons can maintain GTP levels through
phosphotransferase reactions. Intracellular ATP also appears to suppress an
outward current that is different from the adenosine-activated current.
Raising intracellular cAMP levels either with bath-applied forskolin or by
including a cAMP analog in the recording electrode did not alter the
adenosine response. These results indicate that a G-protein is involved in
the coupling between the adenosine receptor and a potassium channel, and
that this coupling is not mediated by cAMP.
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