Lectin‐binding Pattern of Bull Testis and Epididymis

Abstract

Seven rhodamine-conjugated lectins (PNA, RCA I, SBA, Con A, WGA, UEA I, DBA) were used to study the distribution of glycoproteins in the testis and epididymis of immature, juvenile, and adult bulls. A marked change was found in the staining pattern of the lectins in the seminiferous tubules during acrosomal development, and the Sertoli cells seemed to have a cyclic affinity for some of the lectins. The distribution of lectin staining in six regions of the bull epididymis showed some typical differences that were associated with the secretory and absorptive functions of the organ. Region 1 was characterized by strong surface and villous staining and a patchy reaction in the principal cells. Regions 2 and 3 showed a strongly reactive apical Golgi zone and secretory material. In regions 4 and 5, the Golgi zone was subapical but strongly reactive with most lectins, while in region 6 a weakly reactive apical Golgi zone was found. During sexual maturation, an increasing number of basal cells with a strong affinity for some lectins was found at the periphery of the epithelium in regions 2 to 6. These regions also had lectin-stained material along the basal border of the principal cells. These findings suggest that the basal cells may be active in the digestion of absorbed material and that they derive from the principal cells, which may be active in transporting absorbed material to them. The staining pattern of the spermatozoa changed during their transit through the epididymis. The degenerating cells in the testis and epididymal tubules also showed an altered affinity for the lectins.

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.…”

“…These findings, therefore, suggest that PSA may detect some specific glycoconjugates in a certain organelle of the Japanese lesser horseshoe 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.…”

“…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.…”

The Rete Testis of the Goat, a Morphological Study

“…b: Acott and Hoskins. 1981: Arya and Vanha-Perttula. 1985 In order to establish baseline data on the morphology of caprine excurrent ducts as a first step toward our long term objective, the present study describes the histology and line structure of the rete testis epithelium, and dis cusses its structural-functional relationships in light of the information available in other species.…”

Cell- and region-specific expression of sugar chains in the mouse epididymal epithelium using lectin histochemistry combined with immunohistochemistry

“…Lectins are proteins which bind specifically to the carbohydrate residues of glycoconjugates due to their individual specific affinity to a particular sugar. Thus, they have been widely used in histochemistry for the detection of sugar chains and the characterization of cell populations in the epididymis in some species, including humans (Arenas et al, 1996(Arenas et al, , 1998 (Arya and Vanha-Perttula, 1985), hamsters (Calvo et al, 1995), horses (Parillo et al, 1997), boars (Calvo et al, 2000), dogs (Schick et al, 2009), and alpacas (Parillo et al, 2009).…”