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P2X1 receptor activation in HL60 cells
G Buell, AD Michel, C Lewis, G Collo, PP Humphrey and A Surprenant
Glaxo Institute for Molecular Biology, Geneva, Switzerland.
Recent cloning of the human P2X1 receptor revealed high levels of its
messenger RNA in differentiated promyelocytes (HL60 cells). We found
expression of P2X1 receptor protein in HL60 cells by radioligand binding,
by immunohistochemistry, using a receptor specific antibody, and by
electrophysiology. The currents elicited by adenosine triphosphate (ATP)
had the expected properties of P2X1 receptors (rapid desensitization,
mimicked by alpha,beta-methylene-ATP). However, these currents were only
observed in cells that were pretreated with apyrase, which destroys
extracellular ATP, or with suramin, a P2X receptor antagonist. This implies
that HL60 cells release ATP, which chronically desensitizes the receptor.
ATP release was detected by direct measurement, using the
luciferin-luciferase assay. It is concluded that functional P2X1 receptors
are present in the membrane of differentiated HL60 cells.
Volume 87,
Issue 7,
pp. 2659-2664,
04/01/1996
Copyright © 1996 by The American Society of Hematology
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