Abstract
Epidermal growth factor receptor pathway substrate 8 (Eps8) is a novel regulator of cell adhesion and the blood-testis barrier integrity in the seminiferous epithelium (PDF) (HTML)
Lie,Pearl P.Y.; Mruk,Dolores D.; Lee,Will M.; Cheng,Chuen-yan
FASEB Journal 23(8): 2555-2567
Publication date: 2009
In the seminiferous epithelium, Eps8 is localized to actin-basedcell junctions at the blood-testis barrier (BTB) and the apicalectoplasmic specialization (ES) in stage V-VI tubulesbut is considerably diminished in stage VIII tubules. Eps8 down-regulationcoincides with the time of BTB restructuring and apical ES disassembly,implicating the role of Eps8 in cell adhesion. Its involvementin Sertoli-germ cell adhesion was substantiated in studies usingan in vivo animal model by treating rats with 1-(2, 4-dichlorobenzy)-1H-indazole-3-carbohydrazide (adjudin) to induce anchoring junctionrestructuring, during which Eps8 disappeared at the apical ESbefore germ cell departure. In Sertoli cell cultures with establishedpermeability barrier mimicking the BTB in vivo, the knockdownof Eps8 by RNAi led to F-actin disorganization and the mislocalizationof the tight junction proteins occludin and ZO-1, suggestingthe function of Eps8 in maintaining BTB integrity. In vivo knockdownof Eps8 in the testis caused germ cell sloughing and BTB damage,concomitant with occludin mislocalization, further validatingthat Eps8 is a novel regulator of cell adhesion and BTB integrityin the seminiferous epithelium.
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