title: Lectin-binding pattern of Senegalese sole Solea senegalensis (Kaup) testis.
abstract: The localization and characterization of oligosaccharide sequences in the testis of Senegalese sole Solea senegalensis was investigated using 12 lectins in combination with KOH saponification and sialidase digestion (K-s). The interstitial compartment contained all the sugar residues investigated, those bearing oligosaccharides terminating with sialic acid (Neu5Ac) alpha2,3Galbeta1,4GlcNAc, Neu5AcGalNAcalpha1,3(LFucbeta1,2) Galbeta1,3/4GlcNAcbeta1 and GalNAcalpha1,3(LFuc1,2) Galbeta1,3/4GlcNAcbeta1 being more abundant in the medullar region than in the cortex. The melano-macrophage centres found in the interstitial compartment displayed glycans terminating with Galbeta1,3GalNAc. The basal lamina separating the germinal and interstitial compartments exhibited glycans with terminal/internal mannose, internal betaGlcNAc, and terminal Neu5Acalpha2,6Gal/GalNAc, and Neu5AcGalbeta1,3GalNAc, Galbeta1,3GalNAc (PNA), Galbeta1,4GlcNAc, GalNAc, alphaGal, and alphaL-Fuc. In the germinal compartment, the Sertoli cells expressed only glycans terminating with Neu5Acalpha2,3Galbeta1,4GlcNAc in the apical and supra-nuclear lateral surface of the spermatonial cysts located in the distal part of the seminiferous lobules. Primary spermatocytes exhibited oligosaccharides terminating with Galbeta1,3GalNAc and alphaGalNAc in the cytoplasm and nucleus, respectively. The spermatids contained highly mannosylated glycans terminating with GalNac, alphaGal, and alphaL-Fuc. The head of spermatozoa expressed a more complex glycosylation pattern characterized by the additional presence of oligosaccharides terminating with Neu5Acalpha2,3Galbeta1,4GlcNAc, Neu5AcGalbeta1,3GalNAc, Neu5AcGalNAcalpha1,3(LFuca1,2)Galbeta1,3/4GlcNAcbeta1, GalNAcalpha1,3(LFucalpha1,2)Galbeta1,3/4GlcNAcbeta1. The comparison with previous lectin histochemical studies carried out in other fish species reveals a specific glycosylation pattern of Senegalese sole testicular structures and spermatozoa head.
authors.affiliation: Department of Animal Health and Well-being, Faculty of Veterinary Medicine, University of Bari, S.P. per Casamassima Km. 3, Bari, Italy. s.desantis@veterinaria.uniba.it
authors.forename: S
authors.initials: S
authors.lastname: Desantis
authors.forename: S
authors.initials: S
authors.lastname: Zizza
authors.forename: A
authors.initials: A
authors.lastname: García-López
authors.forename: V
authors.initials: V
authors.lastname: Sciscioli
authors.forename: E
authors.initials: E
authors.lastname: Mañanos
authors.forename: V G
authors.initials: VG
authors.lastname: De Metrio
authors.forename: C
authors.initials: C
authors.lastname: Sarasquete
mesh_terms: D000818:Animals; D001665:Binding Sites; D005412:Flatfishes; D006031:Glycosylation; D037102:Lectins / Q000378:metabolism*; D008297:Male; D011485:Protein Binding; D012708:Sertoli Cells / Q000378:metabolism; D012741:Sexual Maturation; D013077:Sperm Head / Q000378:metabolism; D013091:Spermatogenesis; D013094:Spermatozoa / Q000378:metabolism*; D013737:Testis / Q000166:cytology / Q000378:metabolism*
chemical_list: D037102:Lectins