We have characterized a high-affinity folate receptor in human molar placenta tissue. Radioligand binding exhibited characteristics typical of other high-affinity folate binding proteins. Those included, positive cooperativity, a tendency to increased binding affinity with decreasing receptor concentration, a slow ligand dissociation at pH 7.4 becoming rapid at pH 3.5, and inhibition by folate analogues. The folate receptor cross-reacted with antibodies against human milk folate binding protein, e.g. the syncytothrophoblastic layer of molar placenta tissue sections showed strongly positive immunostaining. The gel filtration profile contained two radioligand-bound peaks (25 and 100 kDa), however, with considerable overlap. Only a single band of 70 kDa was seen on SDS-PAGE immunoblotting. The folate receptor in placental tissue may play a crucial role in the transfer of folate from maternal circulation to the fetus.
Characterization of the folate receptor in human molar placenta
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Jan Holm, Steen Ingemann Hansen, Carl W. Nichols, Mimi Høier-Madsen, Poul Erik Helkjær; Characterization of the folate receptor in human molar placenta. Biosci Rep 1 October 1996; 16 (5): 379–389. doi: https://doi.org/10.1007/BF01207263
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