Studies on acrosome labelling of mammalian spermatozoa by radioactive sugars

Kopečný, V.; Cechová, D; Železná, Blanka; Fléchon, J.‐E.; Motlík, Jan; Pech, V.

doi:10.1051/rnd:19840407

Cited by 7 publications

(4 citation statements)

References 23 publications

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“…In all species the staining with UEA I, which indicates the distribution of fucose residues, covered the whole sperm head. This observation is consistent with autoradiographic evidence for 3H-fucose distribution in guineapig spermatids over the acrosome (Kopecny et al, 1984), where it may become incorporated into acrosin. Besides the acrosome, 3Hfucose is possibly incorporated into multiple sites in the developing spermatocytes and spermatids, since at least 16 different glycoproteins have been identified (Grootegoed et al, 1982).…”

Section: Discussionsupporting

confidence: 89%

Comparison of lectin‐staining pattern in testis and epididymis of gerbil, guinea pig, mouse, and nutria

Arya

Vanha‐Perttula

1986

Am. J. Anat.

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The testis and epididymis of gerbil, guinea pig, nutria, and mouse were studied after staining with seven rhodamine-conjugated lectins to disclose the distribution of glycoproteins with different sugar residues. In the testis, the lectins showed a variable affinity for Leydig cells, tubular basement membrane, cytoplasm, acrosome, and plasma membrane of maturing spermatids as well as for Sertoli cell extensions. During acrosomal development, the staining pattern showed characteristic changes with different lectins indicating a gradual processing of the glycoprotein components. The staining in the Sertoli cell extensions displayed a cyclic change linked with the release of spermatozoa. A nuclear staining was prominent in zygotene and pachytene spermatocytes in the mouse, weak in the nutria, but absent in gerbil and guinea pig. The principal cells of epididymis showed a lectin-stained Golgi region as well as a similar staining in the apical surface, microvilli, and tubular contents. This staining was most prominent in the caput/corpus regions with some interspecies differences indicating the epididymal areas active in secretion. Narrow cells active in absorption of testis-derived material were lectin-positive in the initial segment of mouse, gerbil, and nutria epididymis. Large light cells with a strong affinity for some lectins were found in the proximal cauda of gerbil and guinea-pig epididymis. In the nutria, corresponding cells were arranged as islands within the low epithelium. The distal cauda of mouse, gerbil, and nutria was the site for lectin-stained light cells interspersed among the low principal cells. It is concluded that the high and low light cells may be active in the absorption and phagocytosis of residual bodies/cytoplasmic droplets and surplus epididymal secretory material, respectively. Thus, labeled lectins formed a useful tool in the analysis of glycoprotein distribution, processing, secretion, absorption, and degradation in the male reproductive tissues.

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Section: Discussionsupporting

confidence: 89%

Comparison of lectin‐staining pattern in testis and epididymis of gerbil, guinea pig, mouse, and nutria

Arya

Vanha‐Perttula

1986

Am. J. Anat.

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“…Using an indirect fluorescence staining technique acrosin, or its precursor proacrosin, was found to be synthesized during early spermiogenesis (Phi- Florke et al, 1983;Adahm et al, 1989). Kopecny et al (1984) used indirect labeling with 3Hfucose to localize proacrosin or its derivatives in the acrosomal matrix of guinea pig and rabbit spermatids 'D 1991 WILEY-LISS, INC. and suggested that these proteins were apparently the major targets for acrosomal protein glycosylation. de Vries et al (1985) localized acrosin in the equatorial segment of ejaculated porcine sperm and suggested that a change in acrosin localization was part of the process of epididymal maturation in porcine sperm.…”

Section: Introductionmentioning

confidence: 99%

Localization of boar sperm proacrosin during spermatogenesis and during sperm maturation in the epididymis

et al. 1991

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The localization of proacrosin was determined by using colloidal gold labeling and electron microscopy of boar germ cells during spermiogenesis to post-ejaculation. Proacrosin was first localized in round spermatids during the Golgi phase of spermiogenesis; it was associated with the electron-dense granule, or acrosomal granule that was conspicuous within the acrosome. It remained within the acrosomal granule during the cap and acrosome phases of spermiogenesis. At these stages, there was no apparent association of the proacrosin molecule with the acrosomal membranes. During the maturation phase of spermiogenesis, proacrosin was seen to become dispersed into all regions of the acrosome except the equatorial segment. When sperm from different segments of the epididymis and ejaculated sperm were examined, localization was observed throughout the acrosome except for the equatorial segment. Here proacrosin appeared to be localized on both the inner and outer acrosomal membranes as well as with the acrosomal matrix, although further studies are required to verify the membrane localization. No labeling was seen on the plasma membrane. These data suggest that the synthesis and movement of proacrosin to sites in the acrosome are controlled by an as yet unknown process. The absence of proacrosin on the plasma membrane of mature ejaculated sperm makes it unlikely that this enzyme plays a role in sperm-zona adhesion prior to capacitation.

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“…It is remarkable that acrosomal proacrosin of guinea pig, the precursor of the acrosin, a protease involved in fertilization, is a fucosylated glycoprotein (Anakwe et al 1991). The presence of Fuc in acrosome of guinea pig has also been shown by autoradiographs (Kopecny et al 1984). UEA-I histochemistry of Xenopus testis.…”

Section: Discussionmentioning

confidence: 92%

Identification of fucosylated glycoconjugates in Xenopus laevis testis by lectin histochemistry

Valbuena

Madrid

Hernández

et al. 2010

Histochem Cell Biol

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Glycoconjugates play roles in many physiological and pathological processes. Previous works have shown important functions mediated by glycans in spermatogenesis, and the carbohydrate composition of testis has been studied by several approaches, including lectin-histochemical methods. However, the testis of Xenopus laevis, an animal model extensively employed in biochemical, cell and developmental research, has not yet been analysed. The aim of this work was to carry out a histochemical study of the fucose (Fuc)-containing glycoconjugates of Xenopus testis by means of lectins, combined with deglycosylation pretreatments. Four Fuc-binding lectins were used: orange peel (Aleuria aurantia) lectin (AAL), gorse seed (Ulex europaeus) agglutinin-I (UEA-I), fresh water eel (Anguilla anguilla) agglutinin (AAA), and asparagus pea (Lotus tetragonolobus) agglutinin (LTA), each recognizing different forms of fucosylated glycans. Labelling with UEA-I, which preferably binds Fucalpha(1,2) containing oligosaccharides, did not show any appreciable staining. LTA, specific for Fucalpha(1,3), and AAA, which binds Fucalpha(1,2), labelled spermatocytes and spermatids, but no labelling was seen when the histochemical procedure was carried out after either beta-elimination (which removes O-linked oligosaccharides) or incubation with PNGase F (which removes N-linked oligosaccharides), suggesting that fucosylated glycans are of both N- and O-linked types. AAL, which has its highest affinity to Fucalpha(1,6), but also recognizes Fucalpha(1,2) and Fucalpha(1,3), labelled the whole testis, and the staining remained when the histochemical method was performed after either beta-elimination or incubation with PNGase F. Labelling with AAL could be explained by the fact that this lectin could be binding to diverse fucosylated glycans in N- and O-glycans, and even in glycolipids. The importance of these glycans is discussed.

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Studies on acrosome labelling of mammalian spermatozoa by radioactive sugars

Cited by 7 publications

References 23 publications

Comparison of lectin‐staining pattern in testis and epididymis of gerbil, guinea pig, mouse, and nutria

Comparison of lectin‐staining pattern in testis and epididymis of gerbil, guinea pig, mouse, and nutria

Localization of boar sperm proacrosin during spermatogenesis and during sperm maturation in the epididymis

Identification of fucosylated glycoconjugates in Xenopus laevis testis by lectin histochemistry

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