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Blood, 1 July 2001, Vol. 98, No. 1, pp. 100-107
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Novel structurally altered
P2X1 receptor is preferentially activated by
adenosine diphosphate in platelets and megakaryocytic cells
Nicholas J. Greco,
Giovanni Tonon,
Weidong Chen,
Xunyi Luo,
Rakhi Dalal, and
G. A. Jamieson
From the Platelet Biology and the Product Development
Departments, American Red Cross, Rockville, MD.
Experimental and clinical data suggest the presence of multiple
types of adenosine diphosphate (ADP) receptors, one coupled to
ligand-gated cation channels (P2X) and others coupled to
G-protein-coupled (P2Y) receptors. This report
identifies cDNA for a structurally altered
P2X1-like receptor in megakaryocytic cell lines (Dami and
CMK 11-5) and platelets that, when transfected into nonresponsive 1321 cells, confers a specific sensitivity to ADP with the pharmacologic rank order of ADP > > ATP > > >  , -methylene-ATP as
measured by Ca++ influx. This receptor
(P2X1del) contains a deletion of 17 amino acids
(PALLREAENFTLFIKNS) that includes an NFT consensus sequence for
N-linked glycosylation. Glycosylated forms of the P2X1del and P2X1wt receptors were indistinguishable
electrophoretically by Western blot or by immunoprecipitation using
available antihuman and antirat antibodies. These results indicate that
the expression of the P2X1del receptor results in an influx
of Ca++ induced by ADP. Expression of P2X1del
receptor homomeric subunits is sufficient to express a receptor
preferentially activated by ADP and suggests that this altered form,
alone or in combination with P2X1wt receptors, is a
component of an ADP-activated ion channel.
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