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Am J Physiol Renal Physiol 278: F823-F829, 2000;
0363-6127/00 $5.00
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Vol. 278, Issue 5, F823-F829, May 2000

Arachidonic acid metabolic pathways regulating activity of renal Na+-K+-ATPase are age dependent

Dailin Li1, Roger Belusa1, Susana Nowicki1,2, and Anita Aperia1

1 Department of Woman and Child Health, Pediatric Unit, Karolinska Institute, S-171 76 Stockholm, Sweden; and 2 Centro de Investigaciones Endocrinologicas, Consejo Nacional de Investigaciones Cíentificas y Técnicas, 1425 Buenos Aires, Argentina

Locally formed arachidonic acid (AA) metabolites are important as modulators of many aspects of renal tubular function, including regulation of the activity of tubular Na+-K+-ATPase. Here we examined the ontogeny of the AA metabolic pathways regulating proximal convoluted tubular (PCT) Na+-K+-ATPase activity in infant and adult rats. Eicosatetraynoic acid, an inhibitor of all AA-metabolizing pathways, abolished this effect. AA inhibition of PCT Na+-K+-ATPase was blocked by the 12-lipoxygenase inhibitor baicalein in infant but not in adult rats and by the specific cytochrome P-450 fatty acid omega -hydroxylase inhibitor 17-octadecynoic acid in adult but not in infant rats. The lipoxygenase metabolite 12(S)-hydroxyeicosatetraenoic acid (HETE) and the cytochrome P-450 metabolite 20-HETE both inhibited PCT Na+-K+-ATPase in a protein kinase C-dependent manner, but the effect was significantly more pronounced in infant PCT. Lipoxygenase mRNA was only detected in infant cortex. Expression of renal isoforms of cytochrome P-450 mRNA was more prominent in adult cortex. In summary, the AA metabolic pathways that modulated the activity of rat renal proximal tubular Na+-K+-ATPase are age dependent.

renal cytochrome P-450; 12-lipoxygenase; protein kinase C; 12-hydroxyeicosatetraenoic acid; 20-hydroxyeicosatetraenoic acid


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