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Efficient asymmetric carbocyclization processes may be one of the ultimate goals in organic synthesis. Among several potentially versatile methods, Diels-Alder reactions have been rather extensively studied, and in some cases high enantiomeric excesses were reported.1 We have been intrigued with the possibility of

Placental leucine aminopeptidase (P-LAP) is located preferentially in syncytiotrophoblasts in human placenta. Here we investigated P-LAP expression and the regulatory mechanisms in BeWo choriocarcinoma cells with forskolin (FSK)-induced di¡erentiation. Morphologically di¡erentiated cells revealed enhanced P-LAP staining. FSK signi¢cantly increased P-LAP activity and mRNA. Deletion or mutation of activator protein-2 (AP-2) binding site in the footprint-3 (3 3216 to 3 3172) of P-LAP promoter abrogated the stimulatory e¡ects of FSK on luciferase activity of the construct 3 3216/+49. In AP-2-de¢-cient Hep-G2 cells, FSK failed to stimulate luciferase activity of the construct 3 3216/+49. Among the isoforms, BeWo expressed AP-2K K and AP-2Q Q, while FSK increased only AP-2K K. These results suggest di¡erentiation-dependent P-LAP expression in trophoblasts, which involves increased AP-2K K binding.

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