Lectin histochemistry of the human testis

Abstract

The oligosaccharide sequences of glycoconjugates and the nature of the saccharide linkage were investigated in normal human testes by means of lectin histochemistry studies, at light and electron microscopy levels. Reaction to WGA was intense in the seminiferous epithelium and interstitium. MAA showed light reactivity in all cell types of the human seminiferous epithelium, the lamina propria and Leydig cells. UEA-I lectin labelled the lamina propria intensely and the seminiferous epithelium and Leydig cells slightly. A slight reaction to AAA was found in the seminiferous epithelium and in Leydig cells. ConA was labelled in Sertoli cells, germ cells and Leydig cells. The reaction to GNA lectin was similar although less intense. PNA labelling was slight in Sertoli cells, spermatogonia, and Leydig cells, and more intense in spermatocytes, spermatids and peritubular cells. Reaction to DSA was intense in the seminiferous epithelium and Leydig cells. HPA labelled all cell types in the seminiferous epithelium and Leydig cells slightly, and labelled peritubular cells intensely. SBA lectin showed a strong reaction in spermatids and a slight reaction in the lamina propria. The reactions to SNA, LTA, and DBA were negative in all testicular cell types. After beta-elimination pre-treatment, MAA, UEA-I, AAA, PNA, DSA, HPA and SBA reactions were all negative. Endo F/PNGase digestion suppressed reactivity to ConA y GNA. Staining for WGA decreased with Endo F/PNGase digestion and also after beta-elimination. Desialization increased reactivity to PNA, SBA and HPA lectins. These results indicate that the terminal sequences of oligosaccharide side-chains in spermatocytes and, principally, in spermatids are: fucose, mannose, Neu5Ac2,3Gal1,3GalNAc, Gal1,3GalNAc, Gal1,4GlcNAc, Neu5AcGalNAc and GalNAc (in O-glycosylated proteins); mannose (in N-glycosylated proteins) and GlcNAc (in both protein types). A sialic acid residue is added to galactose and GalNAc residues. Present findings also indicate that Sertoli cell glycoproteins are similar to those of spermatids, and that the terminal sugar residues in Leydig cells are GlcNAc, fucose, mannose, Neu5Ac2,3Gal1,3GalNAc, Gal1,3GalNAc, and Gal1,4GlcNAc. The lectin pattern of the lamina propria suggests the presence of GlcNAc, galactose, fucose and GalNAc.

Lectin-Binding Patterns in the Testes of the Java Fruit Bat (Pteropus vampyrus) and the Japanese Lesser Horseshoe Bat (Rhinolophus cornutus).

“…Therefore, such differences in lectin bindings in the acrosomal region may reflect different acrosomal components of sugar residues in each mammalian species. In contrast to the variation in lectin bindings in acrosome, PNA had a conserved binding pattern in the acrosomal region of all mammalian species examined so far [1][2][3][4][5][6][7][8][9][10][11][12][13]. In concurrence, the present study also showed an intense reaction in the acrosomal region of bats.…”

“…The UEA-I reaction, representing the appearance of α-Fucose residues, have been reportedly detected in the acrosomal region of the rat [5,6], mouse [7,8], nutria [8] and bull [12], but no reaction was or has previously been observed in the testes of the Java fruit bat, the Japanese lesser horseshoe bat, the guinea pig [9] or the musk shrew [10]. It has been demonstrated that SBA reacts strongly in the acrosomal region of many mammalian species, such as man [1][2][3][4], rat [5,6], mouse [7,8], nutria [8], guinea pig [9], common tree shrew [11], bull [12] and shiba goat [13], but this reaction could not be detected in either the Java fruit bat or the Japanese lesser horseshoe bat. The DBA binding pattern has varied among the various species.…”

“…Until now, several studies have been done on lectin-binding patterns in the testes of mammalian species, such as the man [1][2][3][4], rodents [5][6][7][8][9], insectivore [10], common tree shrew [11], bull [12] and goat [13], but, there are no reports on the Order Chiroptera. In this study, two kinds of bats were selected: one (Java fruit bat) belongs to the Suborder Megachiroptera, and the other (Japanese lesser horseshoe bat) belongs to the Suborder Microchiroptera.…”

STUDI HISTOKIMIA LEKTIN PADA SEL-SEL SPERMATOGENIK TESTIS MUNCAK (Muntiacus muntjak muntjak) (Lectin Histochemical Study of Testicular Spermatogenic Cells in Muntjak (Muntiacus muntjak muntjak))

“…Aplikasi yang sama juga dilakukan pada rodensia laboratorium (Söderström et al, 1987), testis manusia (Arenas et al, 1998), babi (Calvo et al, 2000), dan babi rusa (Agungpriyono et al, 2007). Dari data yang diperoleh pada penelitian terdahulu, ditemukan adanya modifikasi yang luas pada saat pembentukan spermatozoa yang diekspresikan oleh perbedaan pola ikatan antara glikokonjugat dan lektin.…”

Morphological and histochemical characterization of the seminiferous epithelial and Leydig cells of the turkey

“…Plant lectins, which are most easily characterized by their affinities for specific, terminal glycosidic residues associated with glycolipids and glycoproteins, and c-kit, a known marker for mammalian spermatogonia, were evaluated for their possible use as markers for specific cell-types in the SE of the turkey. Lectins have been used to describe glycoprotein components of germ and somatic cells in the mammalian SE and to elucidate patterns of glycoprotein synthesis, secretion, and absorption in the cells of the mammalian SE and epididymis Vanha-Perttula, 1984, 1986a,b;Arenas et al, 1998;Pastor et al, 2003).…”