Carbohydrate moieties of the interstitial and glandular tissues of the amphibian <i>Pleurodeles waltl</i> testis shown by lectin histochemistry

Sáez, Francisco José; Madrid, Juan Francisco; Aparicio, Raquel; Hernández, Francisco Velasco; Alonso, Edurne

doi:10.1046/j.1469-7580.2001.19810047.x

Cited by 11 publications

(2 citation statements)

References 39 publications

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“…), including amphibians (Sáez et al. , ,b, ,b, ), but no reports exist about the identification of NeuAc and GlcNAc in Xenopus testis. From our data, it could be concluded that terminal GlcNAc is more abundant than sialic acid, because labelling with GlcNAc‐binding lectins was generally stronger than labelling with NeuAc‐binding lectins.…”

Section: Discussionmentioning

confidence: 99%

Histochemical identification of sialylated glycans in Xenopus laevis testis

et al. 2012

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Carbohydrate chains of glycoprotein and glycosphingolipids are highly diverse molecules involved in many cell functions, including cell recognition, adhesion and signalling. Sialylated glycans are of special interest because the terminal position of sialic acid (NeuAc) in glycans linked by different ways to subterminal monosaccharides has been shown to be involved in several biological processes, as occurs with gangliosides, which have been reported as being essential in spermatogenesis in mammals. Some glycan-binding proteins, the lectins, which specifically recognize glycan sequences, have been extensively used to characterize tissue and cell carbohydrates by means of cytochemical techniques. The aim of the present work was to determine the presence of NeuAc by means of histochemical techniques in the testis of Xenopus laevis, an animal model widely used in cell and molecular biology research. However, considering that some NeuAc-binding lectins are capable of binding to N-acetylglucosamine (GlcNAc), other GlcNAc-binding lectins were also assayed. The results showed that NeuAc is mainly expressed in the interstitium, and only a weak labelling in the male germ cells was observed. Most NeuAc was located in O-linked oligosaccharides, but some masked NeuAc in N-glycans were identified in primary and secondary spermatogonia and spermatocytes. By contrast, GlcNAc was widely expressed in all germ cell types. Deglycosylative pre-treatments suggest that both N-and O-glycans and/or glycolipids could be responsible for this labelling. In addition, GlcNAc in O-linked oligosaccharides has been identified in spermatogonial cells. The acrosome of spermatids was always negative. Variations of glycan expression have been found in different cell types, suggesting that glycosylation is modified during spermatogenetic development.

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Section: Discussionmentioning

confidence: 99%

Histochemical identification of sialylated glycans in Xenopus laevis testis

et al. 2012

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“…Lectins, in combination with deglycosyolation techniques, have allowed the identification of carbohydrates in glycans of the testis of several species, mainly mammals (Arya and Vanha‐Perttula,1984,1985,1986; Craveiro and Bao,1995; Dor et al,2004; Ertl and Wrobel,1992; Kurohmaru et al,1991,1995,1996; Labate and Desantis,1995; Liguoro et al,2004; Malmi and Söderström,1987; Malmi et al,1987,1990). Some reports from our group have drawn attention to the glycan composition of amphibian testis (Sáez et al,1999,2000a,b,2001a,b,2004; Valbuena et al,2010,2011). Xenopus laevis is an animal model extensively employed in cell, molecular, and developmental biology, and so it is of interest to know their glycosidic composition.…”

Section: Introductionmentioning

confidence: 99%

Galactosides in glycoconjugates of Xenopus laevis testis shown by lectin histochemistry

Valbuena

Alonso

Madrid

et al. 2011

Microscopy Res & Technique

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The implication of galactosides and other glycoconjugates on spermatogenesis has been previously reported. Glycans show such a complex structure that it makes them very difficult to analyze. Lectin histochemistry is a helpful tool for the study of glycan composition. Lectin histochemistry can be combined with deglycosylation pretreatments to explore the glycan type to which carbohydrates are linked. The aim of the present work was the localization of galactose (Gal)-containing glycoconjugates in the testis of Xenopus laevis, a species widely used in cell, molecular and developmental biology. Gal specific lectins BPL, PNA, BSI-B4, MAA-I, and RCA-I, were used in combination with deglycosylation procedures. Except for BPL, all the lectins were reactive for several testicular tissues. Some of the lectins showed a different reactivity depending on the stage of spermatogenic development, suggesting that cell glycoconjugates are modified during spermatogenesis. The surface of primary spermatocytes was strongly labeled with lectins from peanut (PNA) and castor bean (RCA-I), which agrees with the presence of galactosyl-glycolipids reported in the cell membrane of mammalian spermatocytes. The acrosome was unexpectedly negative to all the lectins tested, whereas the acrosome of mammals and other amphibians has shown a high expression of glycoconjugates, including galactosides. The results obtained after deglycosylation by β-elimination or incubation with PNGase F, which respectively remove O- and N-linked oligosaccharides, allowed us to elucidate the nature of the labeled glycans. The strong expression of galactosides at the cell surface of spermatocytes and spermatids suggests the involvement of these glycans in cell adhesion mechanisms during spermatogenesis.

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Glycoconjugates of the urodele amphibian testis shown by lectin cytochemical methods

Sáez

Madrid

Cardoso

et al. 2004

Microscopy Res & Technique

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Lectin histochemistry is a useful method that allows the in situ identification of the terminal sugar moieties of the carbohydrates that form the glycoconjugates. Moreover, when it is combined with chemical or enzymatic deglycosylation pretreatments, lectin histochemistry can be employed to determine if carbohydrates are linked to the protein core by means of an N- or O-glycosidic linkage or, indeed, to partially sequence the sugar chains. One of the most interesting model organs for the study of spermatogenesis is the amphibian urodele testis. However, this organ has not been very widely investigated with lectin histochemical research. In the last few years, we have carried out a research project to identify and locate glycoconjugates in the testis of the urodele Pleurodeles waltl, the Spanish newt, as a first approach to identify possible carbohydrates with key roles in spermatogenesis. Our findings reveal some glycan chains located in a fusome-like structure in early (diploid) germ cells, oligosaccharides with terminal GalNAc in the acrosome, the occurrence of glycan modifications in the acrosomal contents during spermiogenesis, and changes in glycan composition of follicle and interstitial cells during the spermatogenetic cycle. Furthermore, the similar labeling pattern of follicle and duct cells supports the hypothesis for a common origin of both cell types.

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Carbohydrate moieties of the interstitial and glandular tissues of the amphibian Pleurodeles waltl testis shown by lectin histochemistry

Cited by 11 publications

References 39 publications

Histochemical identification of sialylated glycans in Xenopus laevis testis

Histochemical identification of sialylated glycans in Xenopus laevis testis

Galactosides in glycoconjugates of Xenopus laevis testis shown by lectin histochemistry

Glycoconjugates of the urodele amphibian testis shown by lectin cytochemical methods

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