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1 November 2012 Testis-Specific Cell Adhesion Molecule, CEACAM6-L, Forms Homophilic Interaction at the Cell Adhesion Site in Vitro
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Ceacam6-L (carcinoembryonic antigen-related cell adhesion molecule 6-long) has recently been isolated from rat testis by differential display technique followed by RT-PCR and DNA sequence analysis. CEACAM6-L is a member of the immunoglobulin (Ig) superfamily and composed of an Ig-like domain, three IgCAM domains, a transmembrane region, and a short intracellular domain. We previously reported that CEACAM6-L was localized at the interface between Sertoli cells and elongating/elongated spermatids and might be an adhesion molecule contributing to apical ectoplasmic specialization in testis. In this study, we investigate the adhesive capacities and the complex structures of CEACAM6-L, using COS-7 cells as a study model. Transfection and immunoprecipitation experiments showed that CEACAM6-L expressed in the cells was distributed to the plasma membrane and interacted homophilically between transfected COS-7 cells. A chemical cross-linking experiment and a binding assay with recombinant CEACAM6-L proteins suggested that CEACAM6-L could form trans-tetra complexes, constructed by cis-homodimers at the adhesion site between COS-7 cells expressing CEACAM6-L. We hypothesized that CEACAM6-L expressed in both germ cells and Sertoli cells forms homophilic trans-tetra complexes between these cells in the seminiferous epithelium.

© 2012 Zoological Society of Japan
Hitoshi Kurio, Jae Man Lee, Takahiro Kusakabe, and Hiroshi Iida "Testis-Specific Cell Adhesion Molecule, CEACAM6-L, Forms Homophilic Interaction at the Cell Adhesion Site in Vitro," Zoological Science 29(11), 786-793, (1 November 2012).
Received: 23 April 2012; Accepted: 1 May 2012; Published: 1 November 2012

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