Key result
Prostaglandin E2 receptor binding on human peripheral blood monocytes was saturable and specific, with a Kd of 1.1 X 10(-9) mol/l and 240 binding sites per cell.
The characterization of the PGE2 receptor on human monocytes establishes a foundation for studying its role in diseases involving PGE2-monocyte interactions, such as immunological disorders and bone resorption.
May inform monocyte-PGE2 studies in immunology; leaves open clinical relevance in disease.
The prostaglandin E2 (PGE2) receptor on human peripheral blood monocytes is characterized. The receptor binding at physiological temperature and pH was saturable, specific, and reversible. Scatchard analysis of binding data revealed a linear plot giving a Kd = 1.1 X 10(-9) mol/l and Bmax = 4.1 fmol/10(7) cells, equal to 240 binding sites per cell. PGE2 increased intracellular cyclic adenosine 5'-monophosphate by a maximal factor of 3. PGF2 alpha and arachidonic acid had no stimulatory effects on adenyl cyclase, in accordance with their low binding to the cells. The characterization of the PGE2 receptor on human monocytes creates a basis for the study of the clinical significance of changes in PGE2-receptor binding in disease states involving PGE2-monocyte interactions such as various immunological disorders and bone resorption.
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Eriksen et al. (1985) studied this question. Prostaglandin E2 (PGE2) vs. PGF2 alpha and arachidonic acid was evaluated on Receptor binding characteristics (Kd, Bmax) and intracellular cyclic AMP. Prostaglandin E2 receptor binding on human peripheral blood monocytes was saturable and specific, with a Kd of 1.1 X 10(-9) mol/l and 240 binding sites per cell.
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