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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
1-subunit, but not the
2- or
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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