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Am J Physiol Regul Integr Comp Physiol 279: R287-R294, 2000;
0363-6119/00 $5.00
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Vol. 279, Issue 1, R287-R294, July 2000

Na+-K+-ATPase is distributed to microvillous and basal membrane of the syncytiotrophoblast in human placenta

M. Johansson, T. Jansson, and T. L. Powell

Perinatal Center, Department of Physiology and Pharmacology, Göteborg University, S-405 30 Göteborg, Sweden

Despite its importance for placental function, syncytiotrophoblast Na+-K+-ATPase has not been studied in detail. We purified syncytiotrophoblast microvillous (MVM) and basal (BM) membranes from full-term human placenta. Western blotting with isoform-specific antibodies demonstrated the presence of the alpha 1-subunit, but not the alpha 2- or alpha 3-subunits, in MVM and BM. Relative density per unit membrane protein in BM was 48 ± 1% (mean ± SE, n = 4, P < 0.02) of that in the MVM. The activity of Na+-K+-ATPase was lower in BM (1.4 ± 0.14 µmol · mg-1 · min-1, n = 8, P < 0.02) than in MVM (3.9 ± 0.25 µmol · mg-1 · min-1). Immunocytochemistry confirmed the distribution of Na+-K+-ATPase to MVM and BM. These findings suggest that the syncytiotrophoblast represents a type of transporting epithelium different from the classical epithelia found in the small intestine and kidney, where Na+-K+-ATPase is confined to the basolateral membrane only. This unique polarization of the Na+ pump does not, however, preclude a net transcellular transport of Na+ to the fetus.

fetus; sodium transport; 3-O-methylfluorescein phosphate


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