Placental alkaline phosphatase is related to human IgG internalization in HEp2 cells.

The biological function(s) of placental alkaline phosphatase has not yet been unraveled. The low catalytic activity of the enzyme at physiological pH, and the lack of "natural substrates", bring about the necessity of a more structure-related conception of its role. We have observed an interaction between placental alkaline phosphatase and human IgG. In this report we show that this isozyme is the major membrane protein able to bind IgG in a IgG-internalizing cell line (HEp2). Pretreatment of these cells with Fab fragments of anti placental alkaline phosphatase antibodies blocks the internalization of IgG without perturbing the endocytosis of other ligands. Our results indicate that placental alkaline phosphatase has the ability not only to bind human IgG, but also to promote its internalization in HEp2 cells.