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Rapid Effects of 1,25-Dihydroxyvitamin D₃ and Extracellular Ca²⁺ on Phospholipid Metabolism in Dispersed Porcine Parathyroid Cells

Centre National de la Recherche Scientifique URA 583, Uniuersite Paris V, Groupe Hospitalier Necker Enfants Malades Paris, Franec

Address all correspondence and requests for reprints to: Dr. Agnès Bourdeau, Centre National de la Recherche Scientifique URA 583, Hôpital des Enfants Malades, 149 rue de Sèvres, 75015 Paris, France.

Abstract

We examined the rapid effects (<120 sec) of 1,25(OH)₂D₃ on membrane phospholipid hydrolysis in porcine parathyroid cells and compared these effects to those produced by extracellular Ca²⁺. Cells were labeled with [³H] myo-inositol or [¹⁴C]arachidonic acid for 3 h, then exposed to various 1,25(OH)₂D₃ concentrations in 0.5 mM Ca²⁺ for different time periods or to 2 mM [Ca²⁺]. Parathyroid cells showed a biphasic increase in diacylglycerol (DAG), monoacylglycerol (MG), phosphatidic acid (PA), and inositol trisphosphate (IP3) in response to 1,25(OH)₂D₃ (10^-12-10 M) or to 2 mM [Ca²⁺]. This effect was rapid (within 5 sec) and dose-dependent, with a maximal stimulation with 10 pM of 1,25(OH)²D³. At this concentration, the first peak of DAG, MG, and IP3 was at 5 sec and reached 176 ± 9%, 134 ± 4%, and 154 ± 13%, respectively us. basal levels. For PA, the first maximum increase was at 20 sec (130 ± 6%). At 30 sec MG, PA, and IP₃ returned to basal levels, whereas the decrease in DAG was under the basal level (–25 ± 5%). The second peak reached a maximum at 60 sec for the four products (145 ± 8%, 119 ± 5%, 125 ± 6%, and 175 ± 20%, respectively) then decreased to basal level at 120 sec. High extracellular Ca²⁺ (2 mM) and fluoride (5 mM) also produced similar increase in phosphatidylinositol metabolites, except that DAG levels returned to basal level at 30 sec. In conclusion, the present data shows the existence of rapid effects of 1,25(OH)₂D₃ in porcine parathyroid cells. The short time sequence suggests that they are mediated by a direct interaction with the membrane, possibly through a receptor-mediated process linked to phospholipase C by a G-protein. (Endocrinology 127: 2738–2743,1990)

Received July 11, 1990.

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