Korean J Physiol Pharmacol.  1998 Oct;2(5):601-609.

Role of phospholipase A2 in oxidant-induced alteration in phosphate transport in primary cultured rabbit renal proximal tubule cells

Affiliations
  • 1Department of Physiology, College of Medicine, Pusan National University, Pusan 602-739, Korea.

Abstract

The present study was undertaken to examine the role of phospholipase A2 (PLA2) in oxidant-induced inhibition of phosphate transport in primary cultured rabbit renal proximal tubule cells. Uptakes of phosphate and glucose were dose-dependently inhibited by an oxidant t-butylhydroperoxide (tBHP), and the significant inhibition appeared at 0.025 mM of tBHP, whereas tBHP-induced alterations in lipid peroxidation and cell viability were seen at 0.5 mM. tBHP stimulated arachidonic acid (AA) release in a dose-dependent fashion. A PLA2 inhibitor mepacrine prevented tBHP-induced AA release, but it did not alter the inhibition of phosphate uptake and the decrease in cell viability induced by tBHP. tBHP-induced inhibition of phosphate transport was not affected by a PKC inhibitor, staurosporine. tBHP at 0.1 mM did not produce the inhibition of Na+-K+-ATPase activity in microsomal fraction, although it significantly inhibited at 1.0 mM. These results suggest that tBHP can inhibit phosphate uptake through a mechanism independent of PLA2 activation, irreversible cell injury, and lipid peroxidation in primary cultured rabbit renal proximal tubular cells.

Keyword

Phosphate uptake; Oxidant; PLA2; Proximal tubular cells

MeSH Terms

Arachidonic Acid
Cell Survival
Glucose
Lipid Peroxidation
Phospholipases A2*
Phospholipases*
Quinacrine
Staurosporine
tert-Butylhydroperoxide
Arachidonic Acid
Glucose
Phospholipases
Phospholipases A2
Quinacrine
Staurosporine
tert-Butylhydroperoxide
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