Synthesis of β 2 glycoprotein 1 by the human placenta

Abstract

Autoantibodies to negatively charged phospholipids (aPL) can cause fetal loss, including recurrent miscarriage and stillbirth. The immunopathogenic mechanism by which this occurs is unknown, but these antibodies are known to bind phospholipid via a protein cofactor, beta2 glycoprotein 1. This protein is localized on placental syncytiotrophoblast and enables the binding of aPL from maternal blood. In this study, reverse transcription and the polymerase chain reaction (RT-PCR) was used on mRNA isolated from normal human placental villous tissue and from human choriocarcinoma cell lines (Jeg-3, BeWo and JAr) to demonstrate that placental cells themselves synthesize beta2 glycoprotein 1 transcripts. Protein production was confirmed by immunoblotting experiments. Previous immunohistochemical studies were extended to demonstrate that beta2 GP1 is localized to extravillous cytotrophoblast in addition to syncytiotrophoblast. Production of beta2 glycoprotein 1 by fetal trophoblast indicates this protein is likely to have a physiological function in the placenta, and hence aPL may induce their pathological effect in pregnancy by inhibiting the function of placental beta2 glycoprotein 1.