The syncytiotrophoblast of human term placenta (HST) is a continuous, multi
nucleated structure with minimal tight junctions, which results from the fu
sion of the underlying cytotrophoblast cells. Consequently, the transport o
f metabolites, ions and water from mother to fetus could take place primari
ly via transcellular routes. Transcellular water flux may be facilitated by
aquaporins, membrane proteins functioning as water channels that are widel
y expressed in cells and tissues. Here, we report the presence of AQP3 and
AQP9 in the apical membranes of HST using RT-PCR, immunoblotting and immuno
histochemistry. Since AQP3 is not only a water channels, but also permits t
he rapid passage of both urea and glycerol, while AQP9 also mediates the pa
ssage of carbamides, polyols, purines, and pyrimidines, we have speculated
that these proteins could be involved in the transport of water and solutes
from mother to fetus. (C) 2001 Harcourt Publishers Ltd.