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Vol. 273, Issue 1, 475-483, January 2, 1998

The Identification and Characterization of Oligodendrocyte Thromboxane A2 Receptors

Samuel C. BlackmanDagger , Glyn Dawson§, Kostas Antonakis, and Guy C. Le BretonDagger

From the Dagger  Department of Pharmacology, University of Illinois at Chicago, Chicago, Illinois 60612, the § Department of Biochemistry, University of Chicago School of Medicine, Chicago, Illinois 60637, and the  Institut de Recherches Scientifiques Sur Le Cancer, 94801 Villejuif, France

The presence of functional thromboxane A2 receptors in neonatal rat oligodendrocytes and human oligodendroglioma cells was investigated using immunocytochemistry, ligand affinity chromatography, radioligand binding analysis, immunoblot analysis, and calcium mobilization studies. Immunocytochemical studies revealed the presence of receptor protein on both oligodendrocytes and human oligodendroglioma cells. Ligand affinity chromatography allowed for the purification of a protein with an electrophoretic mobility (55 kDa) indistinguishable from human platelet thromboxane A2 receptors. This affinity purified protein was immunoreactive against a polyclonal anti-thromboxane A2 receptor antibody. Intact human oligodendroglioma cells specifically bound [3H]SQ29,548 with a KD of 4 nM and were found to have approximately 3500 binding sites per cell. Human oligodendroglioma cells also demonstrated calcium mobilization in response to receptor activation with U46619. These results demonstrate the presence of a functional thromboxane A2 receptor in oligodendrocytes and are consistent with previous observations indicating a high density of thromboxane A2 receptors in myelinated brain and spinal cord fiber tracts.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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