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The Ca2+-binding protein (HCaBP) of the human placenta was studied with respect to its biochemical properties, tissue and cellular distribution, and possible involvement in placental Ca2+ transport. Optimal Ca2+ binding by the HCaBP occurs at pH 7-8 and in 100 mM-Na+ and 3 mM-Ca2+. The HCaBP possesses at least 10 Ca2+-binding sites with a Kd of 5 X 10(-6) M ([Ca2+]). Highly specific rabbit-derived anti-HCaBP antibodies were used for HCaBP immunoquantification and immunohistochemistry, which revealed that the HCaBP is localized in the chorionic villi and is primarily associated with the trophoblastic cells of the placenta. In addition, an 'in vitro' cell-free assay system for Ca2+ uptake was constructed with microsomal membranes isolated from term placental tissues. Ca2+ uptake by the placental microsomal fraction exhibited characteristics indicative of active Ca2+ transport such as temperature-dependence, saturability and energetic requirement. In this system, preincubation of microsomal membranes with anti-HCaBP antibodies inhibited Ca2+ uptake, suggesting that the HCaBP is functionally involved in placental membrane Ca2+ uptake.

Ca2+-binding protein of the human placenta. Characterization, immunohistochemical localization and functional involvement in Ca2+ transport