Histochemical analysis of glycoconjugates in the domestic cat testis.
The localization and characterization of oligosaccharide sequences in the cat testis was investigated using 12 lectins in combination with the beta-elimination reaction, N-Glycosidase F and sialidase digestion. Leydig cells expressed O-linked glycans with terminal alphaGalNAc (HPA reactivity) and N-glycans with terminal/internal alphaMan (Con A affinity). The basement membrane showed terminal Neu5Acalpha2,6Gal/GalNAc, Galbeta1,3GalNAc, alpha/betaGalNAc, and GlcNAc (SNA, PNA, HPA, SBA, GSA II reactivity) in O-linked oligosaccharides, terminal Galbeta1,4GlcNAc (RCA120 staining) and alphaMan in N-linked oligosaccharides; in addition, terminal Neu5acalpha2,3Galbeta1,4GlcNac, Forssman pentasaccharide, alphaGal, alphaL-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-Galbeta1,4GlcNAc, Neu5Ac-betaGalNAc as well as internal GlcNAc in O-linked glycans, alphaMan in N-linked glycoproteins and terminal Neu5Acalpha2,6Gal/ GalNAc in both O- and N-linked oligosaccharides. Spermatogonia exhibited cytoplasmic N-linked glycoproteins with alphaMan residues. The spermatocytes cytoplasm expressed terminal Neu5Acalpha2,3Galbeta1,4 GlcNAc and Galbeta1,3GalNAc in O-linked oligosaccharides, terminal Galbeta1,4GlcNAc and alpha/betaGalNAc in N-linked glycoconjugates. The Golgi region showed terminal Neu5Acalpha2,3Galbeta1,4GlcNac, Galbeta1,4GlcNAc, Forssman pentasaccharide, and alphaGalNAc in O-linked oligosaccharides, alphaMan and terminal betaGal in N-linked oligosaccharides. The acrosomes of Golgi-phase spermatids expressed terminal Galbeta1,3GalNAc, Galbeta1,4GlcNAc, Forssmann pentasaccharide, alpha/betaGalNAc, alphaGal and internal GlcNAc in O-linked oligosaccharides, terminal alpha/betaGalNAc, alphaGal and terminal/internal alphaMan in N-linked glycoproteins. The acrosomes of cap-phase spermatids lacked internal Forssman pentasaccharide and alphaGal, while having increased alpha/betaGalNAc. The acrosomes of elongated spermatids did not show terminal Galbeta1,3GalNAc, displayed terminal Galbeta1,4GlcNAc and alpha/betaGalNAc in N-glycans and Neu5Ac-Galbeta1,3GalNAc in O-linked oligosaccharides.
Desantis
S
S
Department of Animal Health and Well-being, Faculty of Veterinary Medicine, University of Bari, Italy.
Ventriglia
G
G
Zubani
D
D
Deflorio
M
M
Megalofonou
P
P
Acone
F
F
Zarrilli
A
A
Palmieri
G
G
De Metrio
G
G
D000177:Acrosome / Q000737:chemistry; D000818:Animals; D001485:Basement Membrane / Q000737:chemistry; D002415:Cats; D006001:Glycoconjugates / Q000032:analysis*; D006056:Golgi Apparatus / Q000737:chemistry; D006651:Histocytochemistry; D037102:Lectins; D007985:Leydig Cells / Q000737:chemistry / Q000166:cytology; D008297:Male; D009844:Oligosaccharides / Q000032:analysis*; D011134:Polysaccharides / Q000032:analysis*; D012670:Seminiferous Epithelium / Q000737:chemistry; D012708:Sertoli Cells / Q000737:chemistry / Q000166:cytology; D013087:Spermatids / Q000737:chemistry / Q000166:cytology; D013090:Spermatocytes / Q000737:chemistry / Q000166:cytology; D013091:Spermatogenesis; D013093:Spermatogonia / Q000737:chemistry / Q000166:cytology; D013379:Substrate Specificity; D013737:Testis / Q000737:chemistry* / Q000166:cytology
D006001:Glycoconjugates; D037102:Lectins; D009844:Oligosaccharides; D011134:Polysaccharides