title: CEACAM2-L on spermatids interacts with poliovirus receptor on Sertoli cells in mouse seminiferous epithelium.
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.
authors.affiliation: Laboratory of Zoology, Graduate School of Agriculture, Kyushu University, Higashiku Hakozaki 6-10-1, Fukuoka 812-8581 Japan (ES, AH, HI)Zoology Department, Faculty of Science, Sohag University, Sohag, Naser City, Egypt, PO.82524 (ES, AH)Department of Histology and Embryology, Graduate School of Medical Science, Kanazawa University, Kanazawa 920-8640, Japan (TW).
authors.forename: Elsaid
authors.initials: E
authors.lastname: Salaheldeen
authors.affiliation: Laboratory of Zoology, Graduate School of Agriculture, Kyushu University, Higashiku Hakozaki 6-10-1, Fukuoka 812-8581 Japan (ES, AH, HI)Zoology Department, Faculty of Science, Sohag University, Sohag, Naser City, Egypt, PO.82524 (ES, AH)Department of Histology and Embryology, Graduate School of Medical Science, Kanazawa University, Kanazawa 920-8640, Japan (TW).
authors.forename: Ali
authors.initials: A
authors.lastname: Howida
authors.affiliation: Laboratory of Zoology, Graduate School of Agriculture, Kyushu University, Higashiku Hakozaki 6-10-1, Fukuoka 812-8581 Japan (ES, AH, HI)Zoology Department, Faculty of Science, Sohag University, Sohag, Naser City, Egypt, PO.82524 (ES, AH)Department of Histology and Embryology, Graduate School of Medical Science, Kanazawa University, Kanazawa 920-8640, Japan (TW).
authors.forename: Tomohiko
authors.initials: T
authors.lastname: Wakayama
authors.affiliation: Laboratory of Zoology, Graduate School of Agriculture, Kyushu University, Higashiku Hakozaki 6-10-1, Fukuoka 812-8581 Japan (ES, AH, HI)Zoology Department, Faculty of Science, Sohag University, Sohag, Naser City, Egypt, PO.82524 (ES, AH)Department of Histology and Embryology, Graduate School of Medical Science, Kanazawa University, Kanazawa 920-8640, Japan (TW) iidahiro@agr.kyushu-u.ac.jp.
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Iida
mesh_terms: D000818:Animals; D019556:COS Cells; D015815:Cell Adhesion Molecules; D002450:Cell Communication; D002522:Chlorocebus aethiops; D003593:Cytoplasm / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism*; D008297:Male; D051379:Mice; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase / Q000378:metabolism; D011485:Protein Binding; D021381:Protein Transport; D011991:Receptors, Virus / Q000378:metabolism*; D012670:Seminiferous Epithelium / Q000378:metabolism*; D012708:Sertoli Cells / Q000166:cytology / Q000378:metabolism*; D013087:Spermatids / Q000166:cytology / Q000378:metabolism*
chemical_list: C087701:Ceacam2 protein, mouse; D015815:Cell Adhesion Molecules; D006023:Glycoproteins; D011991:Receptors, Virus; C066100:poliovirus receptor; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
keywords: CEACAM2; PVR; Sertoli cells; phagocytosis; spermatids; spermatogenesis