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Am J Physiol Regul Integr Comp Physiol 282: R139-R146, 2002; doi:10.1152/ajpregu.00427.2001
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Vol. 282, Issue 1, R139-R146, January 2002

Regulation of transepithelial phosphate transport by PTH in chicken proximal tubule epithelium

Paul L. Dudas1, Alice R. Villalobos2, Gayle Gocek-Sutterlin3, Gary Laverty3, and J. Larry Renfro1

1 Department of Physiology and Neurobiology, University of Connecticut, Storrs, Connecticut 06269; 2 Department of Environmental Medicine, University of Rochester School of Medicine and Dentistry, Rochester, New York 14642; and 3 Department of Biological Sciences, University of Delaware, Newark, Delaware 19716

The effect of parathyroid hormone (PTH) and activation of protein kinase C (PKC) and protein kinase A (PKA) on transepithelial Pi transport was examined in monolayers of chick proximal tubule cells in primary culture (PTCs). Acute exposure of the PTCs to PTH (10-9 M, basolateral side) significantly decreased the net reabsorption of Pi by ~66%. There was no effect after the addition of PTH to the luminal side. Activation of PKC by phorbol 12-myristate 13-acetate (PMA; 0.1 µM) dramatically decreased net Pi reabsorption by ~60%. Bisindolylmaleimide I (BIM; 1 µM), a highly selective PKC inhibitor, prevented PMA-induced inhibition. Activation of adenylate cyclase/PKA by forskolin (10 µM) mimicked the effect of PTH by significantly reducing net Pi reabsorption by one-half. Addition of H-89 (10 µM), a potent inhibitor of PKA, abolished forskolin-induced inhibition. PTH inhibition was blocked by either BIM or H-89. Tissue electrophysiology remained stable after all treatments. There was a decreased immunoreactivity of the luminal Na+-Pi cotransporter NaPi-IIa after PTH treatment. These data indicate that PTH inhibition of Pi reabsorption in this in vitro system is mediated by PKC and PKA.

primary cultures; reabsorptive flux; secretory flux; luminal sodium-inorganic phosphate cotransporter NaPi-IIa; protein kinase C; protein kinase A


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