Reproduction Abstracts

A Disintegrin and Metalloprotease Domain-containing protein 10 (ADAM10) is a cell surface protein with a unique structure possessing potential adhesion and protease domains. However, the role of ADAM10 is not known during early embryo development. In this study, we investigated the expression patterns and biological function of Adam10 in mouse preimplantation embryos. The transcription level of Adam10 increased from the two-cell stage onward. Immunostaining revealed that Adam10 was localized to the apical region of the outer cells in blastocyst embryos. Knockdown (KD) of Adam10 using siRNA significantly affected blastocyst development. FITC-dextran uptake assay in Adam10 KD showed defect of paracellular permeability sealing, and ICC demonstrated aberrant localization and expression of TJ complex constituents. Particularly, Cxadr is mainly detected in the nuclei of blastomears at the blastocyst stage in the KD embryos rather than apical region. However, TJ associated genes were not changed at the transcription level. An in situ proximity ligation assay demonstrated direct interaction of ADAM10 with CXADR, supporting the involvement of ADAM10 in TJ assembly. In conclusion, our findings strongly suggest that ADADM10 is important for blastocyst formation rather than compaction in mouse preimplantation development. This work was supported by Next-Generation BioGreen21 Program (PJ011213), Rural Development Administration (RDA), Republic of Korea.