The localization and characterization of oligosaccharide sequences in the cat testis was investigated using 12 lectins in combination with the ßelimination reaction, N-Glycosidase F and sialidase digestion. Leydig cells expressed O-linked glycans with terminal aGalNAc (HPA reactivity) and N-glycans with terminal/internal aMan (Con A affinity). The basement membrane showed terminal Neu5Aca2,6Gal/GalNAc, Galß1,3GalNAc, a/ßGalNAc, and GlcNAc (SNA, PNA, HPA, SBA, GSA II reactivity) in O-linked oligosaccharides, terminal Galß1,4GlcNAc (RCA120 staining) and aMan in N-linked oligosaccharides; in addition, terminal Neu5Aca2,3Galß1,4GlcNac, Forssman pentasaccharide, aGal, aL-Fuc and internal GlcNAc (MAL II, DBA, GSA I-B4, UEA I, KOH-sialidase-WGA affinity) formed both O- and N-linked oligosaccharides. The Sertoli cells cytoplasm contained terminal Neu5Ac- Galß1,4GlcNAc, Neu5Ac-ßGalNAc as well as internal GlcNAc in O-linked glycans, aMan in N-linked glycoproteins and terminal Neu5Aca2,6Gal/ GalNAc in both O- and N-linked oligosaccharides. Spermatogonia exhibited cytoplasmic N-linked glycoproteins with aMan residues. The spermatocytes cytoplasm expressed terminal Neu5Aca2,3Galß1,4 GlcNAc and Galß1,3GalNAc in O-linked oligosaccharides, terminal Galß1,4GlcNAc and a/ßGalNAc in N-linked glycoconjugates. The Golgi region showed terminal Neu5aca2,3Galß1,4GlcNac, Galß1,4GlcNAc, Forssman pentasaccharide, and aGalNAc in O-linked oligosaccharides, aMan and terminal ßGal in N-linked oligosaccharides. The acrosomes of Golgi-phase spermatids expressed terminal Galß1,3GalNAc, Galß1,4GlcNAc, Forssmann pentasaccharide, a/ßGalNAc, aGal and internal GlcNAc in O-linked oligosaccharides, terminal a/ßGalNAc, aGal and terminal/internal aMan in N-linked glycoproteins. The acrosomes of cap-phase spermatids lacked internal Forssman pentasaccharide and aGal, while having increased a/ßGalNAc. The acrosomes of elongated spermatids did not show terminal Galß1,3GalNAc, displayed terminal Galß1,4GlcNAc and a/ßGalNAc in N-glycans and Neu5Ac-Galß1,3GalNAc in O-linked oligosaccharides.
Histochemical analysis of glycoconjugates in the domestic cat testis
DESANTIS, Salvatore;VENTRIGLIA, GIANLUCA;
2006-01-01
Abstract
The localization and characterization of oligosaccharide sequences in the cat testis was investigated using 12 lectins in combination with the ßelimination reaction, N-Glycosidase F and sialidase digestion. Leydig cells expressed O-linked glycans with terminal aGalNAc (HPA reactivity) and N-glycans with terminal/internal aMan (Con A affinity). The basement membrane showed terminal Neu5Aca2,6Gal/GalNAc, Galß1,3GalNAc, a/ßGalNAc, and GlcNAc (SNA, PNA, HPA, SBA, GSA II reactivity) in O-linked oligosaccharides, terminal Galß1,4GlcNAc (RCA120 staining) and aMan in N-linked oligosaccharides; in addition, terminal Neu5Aca2,3Galß1,4GlcNac, Forssman pentasaccharide, aGal, aL-Fuc and internal GlcNAc (MAL II, DBA, GSA I-B4, UEA I, KOH-sialidase-WGA affinity) formed both O- and N-linked oligosaccharides. The Sertoli cells cytoplasm contained terminal Neu5Ac- Galß1,4GlcNAc, Neu5Ac-ßGalNAc as well as internal GlcNAc in O-linked glycans, aMan in N-linked glycoproteins and terminal Neu5Aca2,6Gal/ GalNAc in both O- and N-linked oligosaccharides. Spermatogonia exhibited cytoplasmic N-linked glycoproteins with aMan residues. The spermatocytes cytoplasm expressed terminal Neu5Aca2,3Galß1,4 GlcNAc and Galß1,3GalNAc in O-linked oligosaccharides, terminal Galß1,4GlcNAc and a/ßGalNAc in N-linked glycoconjugates. The Golgi region showed terminal Neu5aca2,3Galß1,4GlcNac, Galß1,4GlcNAc, Forssman pentasaccharide, and aGalNAc in O-linked oligosaccharides, aMan and terminal ßGal in N-linked oligosaccharides. The acrosomes of Golgi-phase spermatids expressed terminal Galß1,3GalNAc, Galß1,4GlcNAc, Forssmann pentasaccharide, a/ßGalNAc, aGal and internal GlcNAc in O-linked oligosaccharides, terminal a/ßGalNAc, aGal and terminal/internal aMan in N-linked glycoproteins. The acrosomes of cap-phase spermatids lacked internal Forssman pentasaccharide and aGal, while having increased a/ßGalNAc. The acrosomes of elongated spermatids did not show terminal Galß1,3GalNAc, displayed terminal Galß1,4GlcNAc and a/ßGalNAc in N-glycans and Neu5Ac-Galß1,3GalNAc in O-linked oligosaccharides.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.