Localization of transferrin on the surface of the human placenta by electron microscopic immunocytochemistry

Abstract

During the course of gestation, a large amount of iron is transferred rapidly and unidirectionally from mother to fetus across the placenta. It has been postulated that one of the first steps involved in placental iron transfer involves binding of the maternal transferrin-iron complex to the surface of the placenta and the subsequent removal of iron and release of transferrin back into the maternal circulation. To determine if transferrin is present on the surface of human placental villi, two different immunocytochemical methods have been used: (1) an unlabeled antibody, peroxidase-antiperoxidase (PAP) method utilizing rabbit antiserum to human transferrin, goat anti-rabbit IgG and rabbit peroxidase-antiperoxidase complex or; (2) a peroxidase-labeled antibody method utilizing goat antiserum to human transferrin and peroxidase-conjugated rabbit anti-goat IgG. The peroxidase was then localized by incubation in a diaminobenzidine-hydrogen peroxide medium. Examination of the tissue in the electron microscope revealed the reaction product deposited as discrete patches or particles on the microvillous surface of human syncytial trophoblast. Controls using non-immune serum or an antiserum adsorbed with purified human transferrin showed no reaction product on the surface. The results provide morphological confirmation for the presence of transferrin on the surface of human syncytial trophoblast lining the maternal blood spaces.