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The P2X1 Receptor, an Adenosine Triphosphate-Gated
Cation Channel, Is Expressed in Human Platelets but not in Human
Blood Leukocytes
Erin E. Clifford,
Karen Parker,
Benjamin D. Humphreys,
Sylvia B. Kertesy, and
George R. Dubyak
From the Department of Physiology and Biophysics, School of Medicine,
Case Western Reserve University, Cleveland, OH.
Extracellular adenosine triphosphate (ATP) and adenosine diphosphate
(ADP) activate multiple types of P2-nucleotide receptors expressed in
platelets or leukocytes. Electrophysiological and biochemical studies
have indicated expression of the P2X1 receptor, an
ATP-gated cation channel, in human and rat platelets, rat basophilic leukemia (RBL) cells, and phorbol myristate acetate
(PMA)-differentiated HL-60 myeloid cells. Although these findings
suggest that P2X1 receptors are present in both blood
leukocytes and blood platelets, the relative levels of P2X1
receptor expression and function in human blood leukocytes and
platelets have not been directly characterized. On the basis of both
immunoblot analysis and functional assays of P2X1
receptor-mediated ionic fluxes, we report that there is significant
expression of P2X1 receptors in human platelets, but not in
neutrophils, monocytes, or blood lymphocytes. Thus, unlike platelets
and myeloid progenitor cell lines, fully differentiated human blood
leukocytes do not express functionally significant numbers of
P2X1 receptors, suggesting the downregulation of
P2X1 receptor gene expression during the differentiation of
phagocytic leukocytes. By contrast, P2X1 receptor
expression is strongly maintained during megakaryocytic differentiation
and platelet release. Immunoblot analysis indicated that the platelet
P2X1 receptor migrates as an approximately 60-kD protein
during SDS-electrophoresis under reducing or nonreducing conditions.
Treatment of platelet membranes with endoglycosidase-F causes the
P2X1 receptor band to migrate as a 46-kD protein, verifying
the highly glycosylated nature of the mature receptor protein.
Additional studies of nucleotide-induced changes in Ca2+
influx/mobilization demonstrated that the platelet P2X1
receptors are pharmacologically distinct from the well-characterized
ADP receptors of these cells. This finding suggests a unique role for
these ATP-gated ion channels during hemostasis or thrombosis.
Blood, Vol. 91 No. 9 (May 1), 1998:
pp. 3172-3181
© 1998 by The American Society of Hematology.
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