Anatomic distribution of lectin-binding sites in mouse testis and epididymis

Lee, Man-Chi; Damjanov, Ivan

doi:10.1111/j.1432-0436.1984.tb01410.x

Cited by 59 publications

(43 citation statements)

References 22 publications

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“…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.…”

Section: Discussionsupporting

confidence: 74%

“…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.…”

Section: Discussionmentioning

confidence: 99%

“…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.…”

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confidence: 99%

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

Morigaki

Kurohmaru

Kanai

et al. 2000

Journal of Reproduction and Development

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Abstract. Lectin binding patterns in the testes of the Java fruit bat, Pteropus vampyrus, and the Japanese lesser horseshoe bat, Rhinolophus cornutus, were investigated by light microscopy. Binding patterns were similar in both species, except for some slight differences. UEA-I, SBA, DBA and BSL-I revealed no reaction in the testes of either species. Con A and WGA gave a diffuse reaction all over the seminiferous epithelium in both species. In addition to this binding pattern, PHA-E exhibited a granular reaction within the cytoplasm of pachytene spermatocytes. PNA and RCA-I gave an intense reaction in the acrosomal region from Golgi to acrosome-phase spermatids in both species, but, in addition to this binding pattern, RCA-I reacted in the cytoplasm of spermatocytes and spermatids in the Java fruit bats. PSA revealed a granular reaction in the cytoplasm of spermatids in the Japanese lesser horseshoe bats. These binding patterns were similar to those of mammals studied before, except that a few specific bindings were detected in the bats.

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Section: Discussionsupporting

confidence: 74%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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

Morigaki

Kurohmaru

Kanai

et al. 2000

Journal of Reproduction and Development

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“…This is consistent with strong staining of wild-type mouse testes with Grifornia simpliciforia agglutinin II (GSAII), which recognizes GlcNAc-terminated carbohydrates (Lee and Damjanov, 1984). In MX -/-testes, however, the levels of GlcNAc-terminated oligosaccharides are reduced (Akama et al, 2002) and thus MX -/-testes were not stained with GSAII.…”

Section: Role Of N-glycans In Spermatogenesissupporting

confidence: 48%

The role of N-glycans in spermatogenesis

2003

Cytogenet Genome Res

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Many proteins, in particular those in the plasma membranes, are glycosylated with carbohydrates, which are grouped into O-glycans and N-glycans. O-glycans are synthesized step by step by glycosyltransferases, whereas N-glycans are synthesized by en-bloc transfer of the so-called high-mannose-type oligosachharide from lipid-linked precursor to polypeptide. The high-mannose-type N-glycans are then modified by processing α-mannosidases. Alpha-mannosidase IIx (MX) was identified as the gene product of processing α-mannosidase II (MII)-related gene. MX apparently plays subsidiary role for MII in many cell types, as N-glycan patterns of MX null mouse tissues are not altered significantly. Surprisingly MX null male mice are infertile due to a failure of spermatogenesis. This review provides a brief overview of the in vivo role of N-glycans which are revealed by the gene knockout mouse approach, and introduce our studies on the MX gene knockout mouse. The MX gene knockout experiments unveiled a novel function of a specific N-glycan, which is N-acetylglucosamine-terminated and has a fucosylated triantennary structure, in the adhesion between germ cells and Sertoli cells. The study of MX is a good example of how the in vivo roles of an apparently redundant gene product are determined by the gene knockout approach.

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“…Recent progress in lectin histochemistry and immunohistochemistry (IHC) using fluorescent dye-conjugated molecules appears to have solved such problems. For example, the lectin peanut agglutinin (PNA) is currently being used to visualize the acrosomes of spermatids (Lee and Damjanov 1984;Arya and Vanha-Perttula 1986) and, when combined with nuclear staining with DNA-binding fluorescent dyes such as 4',6-diamidino-2-phenylindole (DAPI), the stages and cell numbers can be easily determined. Furthermore, antibodies against zinc finger-and BTB domain-containing 16 (ZBTB16) (Buaas et al 2004;Meistrich and Hess 2013), synaptonemal complex protein 3 (SYCP3) (Lammers et al 1994), and GATA binding protein 4 (GATA4) (Imai et al 2004) mainly visualize the nuclei of type A spermatogonia, spermatocytes, and Sertoli cells, respectively, thereby contributing to the precise determination of cell populations in seminiferous tubules.…”

Section: Research-article2014mentioning

confidence: 99%

Quantitative Analysis of the Cellular Composition in Seminiferous Tubules in Normal and Genetically Modified Infertile Mice

Nakata

Wakayama

Takai

et al. 2014

J Histochem Cytochem.

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SummaryThe aim of this study was to establish a quantitative standard for the cellular composition in seminiferous tubules at each stage of spermatogenesis in the mouse testis, and thereby evaluate abnormalities in the infertile mouse testis. We applied a combination of lectin histochemistry for acrosomes and immunohistochemistry for various specific cell markers, both of which were visualized with fluorescence, on paraffin sections of the testis. We first examined seminiferous tubules from normal mice and counted the number of each cell type at each stage of spermatogenesis. We then examined seminiferous tubules from genetically modified mice deficient (-/-) for one of the cell adhesion molecules, nectin-2 or nectin-3, and compared the number of each cell type at each stage of spermatogenesis with the corresponding value in normal mice. In both nectin-2 -/-and nectin-3 -/-mice, which are infertile despite the apparently normal morphology of the seminiferous epithelia, we measured a progressive loss in the later-step spermatids, with significantly lower numbers of step 11-16 spermatids in nectin-3 -/-mice and step 15-16 spermatids in nectin-2 -/-mice as compared with that in normal control mice. The present study demonstrated that a quantitative analysis of cellular compositions at different stages in seminiferous tubules was useful for evaluating abnormalities in spermatogenesis. (J Histochem Cytochem 63:99-113, 2015)

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Anatomic distribution of lectin-binding sites in mouse testis and epididymis

Cited by 59 publications

References 22 publications

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

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

The role of N-glycans in spermatogenesis

Quantitative Analysis of the Cellular Composition in Seminiferous Tubules in Normal and Genetically Modified Infertile Mice

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