Histochemical analysis of rat testicular glycoconjugates. 2. Beta-galactosyl residues in O- and N-linked glycans in seminiferous tubules.

Summary Rat testes have been examined with a panel of lectins that bind specifically to oligosaccharide sequences having terminal or subterminal -galactosyl residues in O-linked glycans, or in the outer chains of complex N-linked glycans:Arachis hypogaea (peanut, AHA),Erythrina cristagalli (coral tree, ECA),Ricinus communis (castor bean, RCA120) andAbrus precatorius (jequirity bean, APA) agglutinins. Pretreatment of sections with neuraminidase, -galactosidase and removal of alkali-labile O-linked sequences by -elimination allowed the structure of these glycans to be further explored. In spermatogonia and spermatocytes there was little evidence of glycans terminating in -galactosyl residues, although these were present at non-reducing terminals as sialylgalactosides. The acrosome contained two subsets of O-linked glycans terminating in sialylgalactosides, while the nuclear cap showed at least two subsets of N-linked sialylgalactosyl as well as O-linked glycans. Spermatozoa exhibited minor changes in the pattern of glycosylation, although the overall pattern of -galactosyl expression was similar. Binding to Sertoli cells showed the presence of some unsubstituted -galactosyl terminals on O-linked glycans but few such N-linked residues, while terminal -galactosides were scanty in tubular basement membranes.