Abstract
HNK-1 (Leu-7 antigen or CD57) is a unique carbohydrate moiety found in certain glycosphingolipids and several cell adhesion glycoproteins on the cell membrane. Previous studies have suggested that HNK-1 carbohydrates act as adhesive ligands in cell-cell interactions. Using a monoclonal antibody reactive to the HNK-1 moiety and an immunoperoxidase method on formalin-fixed paraffin-embedded tissue, the expression of the HNK-1 epitope in human placentae was confined to the intermediate trophoblast (IT) in trophoblastic columns. The number of HNK-1 immunoreactive IT cells increased from the proximal to the midportion of the trophoblastic column, and then disappeared at the junction of the column with the basal plate where IT infiltrates the endomyometrium and becomes extravillous IT. Neither cytotrophoblast nor syncytiotrophoblast reacted with the HNK-1 antibody. In hydatidiform moles, HNK-1 immunoreactivity was localized to areas that structurally resembled trophoblastic columns. In contrast, placental site trophoblastic tumours which do not contain structures analogous to trophoblastic columns did not express HNK-1 epitope. Expression of HNK-1 was only rarely observed in choriocarcinomas, being present in less than 5 per cent of trophoblastic cells in two of 13 cases. The murine placenta, which lacks trophoblastic columns, was negative for HNK-1. Thin-layer chromatography immunostaining demonstrated the HNK-1 reactive glycosphingolipids in placental lipid extracts, whereas Western blot analysis from placental protein extracts failed to reveal detectable glycoproteins that demonstrated HNK-1 immunoreacdvity. In conclusion, the specific localization of HNK-1 reactive glycosphingolipids in trophoblastic columns of the human placenta suggests that the HNK-1 moiety may play an important role in maintaining cohesion between intermediate trophoblastic cells in the trophoblastic columns thereby contributing to the structural integrity of the villi that anchor the placenta to the basal plate.
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