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• W2109214244 abstract "The removal of excess cytoplasm from elongated spermatids by Sertoli cells is the last essential step in spermatogenesis. It requires cell-to-cell recognition between a Sertoli cell and an elongating spermatid through protein-protein interactions. CEACAM2-L, an adhesion molecule of the immunoglobulin superfamily (IgSF), is present at the plasma membrane covering the excess cytoplasm of elongated spermatids, and is possibly involved in the cell-to-cell recognition. In this study, we investigated the interaction between CEACAM2-L and Poliovirus receptor (PVR), which is also from the IgSF and is expressed by Sertoli cells. Immunohistochemical analysis showed that CEACAM2-L expressed on elongated spermatids was in close contact with PVR-positive cell processes of Sertoli cells. Immunoprecipitation experiments both in vivo and in vitro demonstrated a direct heterophilic interaction between CEACAM2-L and PVR. We show that the N-terminal Ig domain of CEACAM2-L was critical for its interaction with PVR. In addition, we found that CEACAM2-L formed heterophilic trans-tetramers with PVR in transfected COS-7 cells. From these data, we propose that Sertoli cells recognize the excess cytoplasm of elongated spermatids through the PVR-CEACAM2-L interaction in mouse testis." @default.
• W2109214244 created "2016-06-24" @default.
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• W2109214244 date "2014-06-19" @default.
• W2109214244 modified "2023-10-17" @default.
• W2109214244 title "CEACAM2-L on Spermatids Interacts with Poliovirus Receptor on Sertoli Cells in Mouse Seminiferous Epithelium" @default.
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• W2109214244 doi "https://doi.org/10.1369/0022155414542653" @default.
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