title: Lectin affinity of the seminiferous epithelium in healthy and cryptorchid post-pubertal boars.
abstract: The present study describes the sugar content of the seminiferous epithelium, using lectin histochemistry, in healthy boars and in boars with unilateral and bilateral abdominal cryptorchidism. In healthy boars the apical cytoplasm of Sertoli cells exhibited abundant glucosyl (Con A and WGA lectins), galactosyl (HPA, DBA, SBA and PNA lectins), and fucosyl (AAA lectin) residues. Spermatogonia and spermatocytes contained abundant glucosyl (Con A and WGA lectins) and fucosyl (AAA lectin) residues. In spermatids, galactosyl (SBA and PNA lectins) and glucosyl (Con A and WGA lectins) residues increased progressively throughout spermiogenesis, and fucosyl (AAA lectin) residues decreased. As compared with healthy boars, the scrotal testis of unilateral cryptorchid boars showed decreased amounts of fucosyl (AAA lectin) and galactosyl (HPA and DBA lectins) residues on the Sertoli cell apical cytoplasm; spermatocytes exhibited higher content of glucosyl (Con A lectin) residues and spermatids showed altered nature of glucosyl (Con A and WGA lectins) and galactosyl (SBA and PNA lectins) complexes. In abdominal testes of unilateral and bilateral cryptorchid boars, immature Sertoli cells and spermatogonia showed decreased fucosyl (AAA lectin), and increased glucosyl (Con A and WGA lectins) and galactosyl (SBA and PNA lectins) contents. These results suggest that the seminiferous epithelium of healthy boars has polarized activity with the apical compartment implicated in germ cell-Sertoli cell adhesion and interaction, in transport of ions, substrates and fluids, and in acrosomal differentiation. In scrotal testes, unilateral abdominal cryptorchidism could lead to defective germ cell-Sertoli cell adhesion, impaired acrosomal differentiation and increased ionic transport in the apical compartment of the seminiferous epithelium. Unilateral and bilateral cryptorchidism could induce increased ionic transport and membrane permeability in the seminiferous epithelium of abdominal testes.
authors.affiliation: Reproductive Biology Unit, Department of Biology, Faculty of Sciences, University of Girona, Girona, Spain. dbepn@fc.udg.es
authors.forename: E
authors.initials: E
authors.lastname: Pinart
authors.forename: S
authors.initials: S
authors.lastname: Bonet
authors.forename: M
authors.initials: M
authors.lastname: Briz
authors.forename: L M
authors.initials: LM
authors.lastname: Pastor
authors.forename: S
authors.initials: S
authors.lastname: Sancho
authors.forename: N
authors.initials: N
authors.lastname: García
authors.forename: E
authors.initials: E
authors.lastname: Badia
authors.forename: J
authors.initials: J
authors.lastname: Bassols
mesh_terms: D000818:Animals; D050260:Carbohydrate Metabolism; D002240:Carbohydrate Sequence; D003456:Cryptorchidism / Q000378:metabolism / Q000473:pathology / Q000662:veterinary*; D006001:Glycoconjugates / Q000378:metabolism; D006651:Histocytochemistry / Q000662:veterinary; D007248:Infertility, Male / Q000378:metabolism / Q000473:pathology / Q000662:veterinary; D037102:Lectins / Q000378:metabolism*; D008297:Male; D008969:Molecular Sequence Data; D012670:Seminiferous Epithelium / Q000378:metabolism* / Q000473:pathology; D013379:Substrate Specificity; D013552:Swine; D013553:Swine Diseases / Q000378:metabolism* / Q000473:pathology
chemical_list: D006001:Glycoconjugates; D037102:Lectins