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The Journal of Neurophysiology Vol. 81 No. 5 May 1999, pp. 2088-2094
Copyright ©1999 by the American Physiological Society
Laboratory of Molecular and Cellular Neurobiology, National Institute on Alcohol Abuse and Alcoholism, National Institutes of Health, Bethesda, Maryland 20892-8115
Xiong, Keming,
Robert W. Peoples,
Jennifer
P. Montgomery,
Yisheng Chiang,
Randall R. Stewart,
Forrest F. Weight, and
Chaoying Li.
Differential Modulation by Copper and Zinc of P2X2
and P2X4 Receptor Function. J. Neurophysiol. 81: 2088-2094, 1999.
Differential Modulation by Copper and Zinc of P2X2 and
P2X4 Receptor Function. The modulation by
Cu2+ and Zn2+ of P2X2 and
P2X4 receptors expressed in Xenopus oocytes was
studied with the two-electrode, voltage-clamp technique. In oocytes
expressing P2X2 receptors, both Cu2+ and
Zn2+, in the concentration range 1-130 µM, reversibly
potentiated current activated by submaximal concentrations of ATP. The
Cu2+ and Zn2+ concentrations that produced 50%
of maximal potentiation (EC50) of current activated by 50 µM ATP were 16.3 ± 0.9 (SE) µM and 19.6 ± 1.5 µM, respectively. Cu2+ and Zn2+
potentiation of ATP-activated current was independent of membrane potential between 
80 and +20 mV and did not involve a shift in the
reversal potential of the current. Like Zn2+,
Cu2+ increased the apparent affinity of the receptor for
ATP, as evidenced by a parallel shift of the ATP concentration-response
curve to the left. However, Cu2+ did not enhance
ATP-activated current in the presence of a maximally effective
concentration of Zn2+, suggesting a common site or
mechanism of action of Cu2+ and Zn2+ on
P2X2 receptors. For the P2X4 receptor,
Zn2+, from 0.5 to 20 µM enhanced current activated by 5 µM ATP with an EC50 value of 2.4 ± 0.2 µM.
Zn2+ shifted the ATP concentration-response curve to the
left in a parallel manner, and potentiation by Zn2+ was
voltage independent. By contrast, Cu2+ in a similar
concentration range did not affect ATP-activated current in oocytes
expressing P2X4 receptors, and Cu2+ did not
alter the potentiation of ATP-activated current produced by
Zn2+. The results suggest that Cu2+ and
Zn2+ differentially modulate the function of
P2X2 and P2X4 receptors, perhaps because of
differences in a shared site of action on both subunits or the absence
of a site for Cu2+ action on the P2X4 receptor.
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