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  • 1
    Electronic Resource
    Electronic Resource
    Functional Morphology of the Zona Pellucida (2001)
    Oxford UK : Blackwell Science Ltd.
    Anatomia, histologia, embryologia 30 (2001), S. 0 
    Details
    ISSN: 1439-0264
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The zona pellucida (ZP) is an extracellular matrix surrounding the oocyte and the early embryo that exerts several important functions during fertilization and early embryonic development. The ZP of most mammalian species is composed of three major glycoproteins that show considerable heterogeneity due to extensive post-translational modifications. Sodium dodecyl sulphate polyacrylamide gel electrophoresis of the ZP reveals three to four glycoproteins which have been nominated ZP1, ZP2, ZP3 and ZP4. As cloning and characterization of the ZP genes of a variety of mammalian species including domestic animals show a high homology, three classes of ZP genes, ZPA, ZPB and ZPC can be discerned. The corresponding proteins were named ZPA, ZPB and ZPC. Whereas in the mouse ZPB is the primary sperm receptor, the situation is more complicated in other species. For instance, in the pig ZPA has been shown to possess receptor activity. Interaction between gametes during fertilization is at least in part regulated by carbohydrate moieties of the ZP and carbohydrate-binding proteins of the sperm surface. In domestic animals zona proteins are expressed in both the oocyte and granulosa cells in a stage-specific pattern and may play a role in granulosa cell differentiation. The role of ZP glycoproteins in immunocontraception is briefly discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1439-0264.2001.00337.x
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  • 2
    Electronic Resource
    Electronic Resource
    Immunocytochemical characterization of porcine zona pellucida during follicular development (1995)
    Springer
    Anatomy and embryology 191 (1995), S. 41-46 
    Details
    ISSN: 1432-0568
    Keywords: Zona pellucida ; Glycoproteins Immunocytochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Sections of bovine ovaries fixed in Bouin's fluid or methanol-acetic acid and embedded in paraffin were incubated with chicken polyclonal antibodies to HPLC-purified zona glycoproteins ZP3α and ZP3β. Oocytes of primordial follicles as well as of primary follicles showed weak labelling with anti-ZP3α and anti-ZP3β. No immunostaining could be observed in the follicle cells. The ZP of primary follicles displayed distinct immunoreactivity for both ZP3α and ZP3β. In secondary follicles, distinct labelling with anti-ZP3β and weak labelling with anti-ZP3α could be seen in the oocyte. The ZP showed immunoreactivity with antibodies to ZP3α and ZP3β. Both antibodies labelled single follicle cells. In tertiary follicles, the oocytes were weakly labelled with anti-ZP3α and anti-ZP3β. Some granulosa cells showed staining for ZP3α and ZP3β. The ZP displayed strong immunoreactivity for ZP3β and ZP3α. Cells of the corona radiata were strongly immunopositive for ZP3α and ZP3β. Similar histotopography of immunoreactive cells could be seen in preovulatory follicles. The characteristic pattern observed for the distribution of ZP3α and ZP3β strongly suggests that in the porcine ovary both the oocyte and the follicle cells contribute to the synthesis of the ZP, perhaps in sequence.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00215296
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  • 3
    Electronic Resource
    Electronic Resource
    Boar sperm membranes antigens (1990)
    Springer
    Histochemistry and cell biology 93 (1990), S. 491-495 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The dynamics of the cell surface during the process of capacitation is impressively shown by means of a monoclonal antibody directed against the P86/5 antigen. This glycoprotein was located in the sperm plasma membrane using the colloidal gold method in combination with specimen preparation in toto. The antigen is absent at the rostral tip of non-capacitated spermatozoa, but forms clusters over the principal segment and the equatorial segment after induction of capacitation. This formation of microdomains with different properties may be a prerequisite for the onset of the acrosome reaction (AR). During AR the diffusion barrier for the P86/5 antigen breakes down and the antigen occupies now the rostral crescent-like area of the sperm head. These observations are discussed with respect to zona binding and induction of the AR in boar spermatozoa.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00266406
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  • 4
    Electronic Resource
    Electronic Resource
    Boar sperm membranes antigens (1990)
    Springer
    Histochemistry and cell biology 93 (1990), S. 485-490 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A monoclonal antibody, designated mAb P86/5, was generated by immunization of female Balb/c mice with a membrane vesicle fraction composed of the outer acrosomal membrane and plasma membrane (PM-OAM). As determined by fluorescence microscopy and electron microscopy P86/5 recognizes a sperm plasma membrane antigen that is restricted to the sperm head. In intact spermatozoa the P86/5-antigen is distributed over the surface of the sperm head with the exception of the rostral region. By comparing the antibody binding pattern generated at 4° C and 25° C, it could be shown that the P86/5-antigen is capable to diffuse freely within the cell membrane overlying the acrosome whereas its lateral mobility is restricted to the post-acrosomal region. The P86/5-antigen had a molecular weight of about 78 kDa as revealed by SDS-PAGE and western blotting. The glycoprotein nature of the P86/5-antigen was established by lectin affinity chromatography.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00266405
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  • 5
    Electronic Resource
    Electronic Resource
    Immunocytological characteriziation of the outer acrosomal membrane (OAM) during acrosome reaction in boar (1985)
    Springer
    Histochemistry and cell biology 82 (1985), S. 113-120 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary In order to study the acrosome reaction in boar, spermatozoa were incubated in a calcium-containing medium in the presence of the calcium ionophore A23187. The time course of the acrosome reaction was assessed by phasecontrast microscopy and correlated with the movement characteristics of the spermatozoa determined by means of multiple-exposure photography (MEP). Different stages of the acrosome reaction could be observed by indirect immunofluorescence using an antibody fraction raised in rabbits against the isolated outer acrosomal membrane (OAM). At the start of the acrosome reaction, a bright fluorescence located exclusively at the acrosomal cap of the sperm head could be observed, whereas after 60–120 min, the fluorescence vanished, indicating the complete loss of the OAM. However, to gain more insight into the stages of the plasma membrane and OAM during the acrosome reaction, immunoelectron-microscopical studies were performed using anti-OAM antibodies detected by the protein-A gold method. Ultrathin sections and total preparations in combination with transmission electron microscopy (TEM) confirmed, that boar spermatozoa start their acrosome reaction by a vesiculation of the plasma membrane, thus exposing the heavily labelled OAM, which is then lost as sheets or large vesicles. The newly exposed inner acrosomal membrane did not show any labelling with gold, thereby indicating clear differences in the antigenicity of both acrosomal membranes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00708194
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  • 6
    Electronic Resource
    Electronic Resource
    Electron microscopic localization of a fucose-binding protein in acrosome reacted boar spermatozoa by the fucosyl-peroxydase-gold method (1987)
    Springer
    Histochemistry and cell biology 86 (1987), S. 297-303 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary In this study we have examined the behaviour and the localization of the fucose-binding protein (FBP) in boar spermatozoa during ionophore induced acrosome reaction (AR) by means of normal TEM and specimen preparation in toto. During early stages of AR the FBP is first localized at the border between equatorial segment and anterior acrosome. With the propagation of the AR the FBP is dramatically expressed and visible over the entire surface of the acrosome and equatorial segment. TEM pictures of this stages show that the FBP is associated with the OAM. At later stages of AR, when acrosomal ghost formation occur, the FBP is associated with the acrosomal ghost, and equatorial segment and to a very low degree also with the IAM. It is concluded from this data that the FBP is responsible for the specific binding of the ghost-sperm unit to the zone pellucida.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00490262
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  • 7
    Electronic Resource
    Electronic Resource
    Fracture labelling of boar spermatozoa for the fucose-binding-protein (FBP) (1987)
    Springer
    Histochemistry and cell biology 87 (1987), S. 181-183 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Labelling of fractured boar spermatozoa with the FUC-HRP gold method for a fucose-binding-protein (FBP) gave evidence the FBP is localized in the acrosomal matrix. All fracture faces through the acrosome from the rostral end towards the equatorial segment show similar labelling pattern. This labelling is completely blocked by preincubation of the fractured tissue with focoidan.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00533403
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  • 8
    Electronic Resource
    Electronic Resource
    Immunohistochemical localization of spermadhesin AWN in the porcine male genital tract (1995)
    Springer
    Cell & tissue research 282 (1995), S. 175-179 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Immunohistochemistry ; Zona pellucida-binding protein ; Boar spermadhesin ; Pig
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. Boar spermadhesin (AWN) is a 14-kDa multifunctional protein, attached to the surface of the spermatozoa and involved in sperm capacitation and zona pellucida binding. The cellular origin of AWN was previously unknown. Moreover, the region of the male genital tract in which AWN becomes attached to the surface of spermatozoa was also uncertain. By using monospecific polyclonal antibodies against AWN, the immunohistochemical distribution pattern of AWN epitopes has been investigated in tissue sections of the porcine male genital tract. Our study has revealed that AWN is synthesized in the rete testis and in the epithelium of the seminal vesicles. The latter are also the major contributors of seminal plasma AWN. In addition, immunoblotting analysis has shown that AWN is present on epididymal spermatozoa. Our results indicate that the cellular origin of spermadhesins is species-specific. The attachment of AWN to epididymal spermatozoa is probably important in developing the capacity for fertilization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004410050470
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  • 9
    Electronic Resource
    Electronic Resource
    Immunohistochemical localization of spermadhesin AWN in the porcine male genital tract (1995)
    Springer
    Cell & tissue research 282 (1995), S. 175-179 
    Details
    ISSN: 1432-0878
    Keywords: Immunohistochemistry ; Zona pellucida-binding protein ; Boar spermadhesin ; Pig
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Boar spermadhesin (AWN) is a 14-kDa multifunctional protein, attached to the surface of the spermatozoa and involved in sperm capacitation and zona pellucida binding. The cellular origin of AWN was previously unknown. Moreover, the region of the male genital tract in which AWN becomes attached to the surface of spermatozoa was also uncertain. By using monospecific polyclonal antibodies against AWN, the immunohistochemical distribution pattern of AWN epitopes has been investigated in tissue sections of the porcine male genital tract. Our study has revealed that AWN is synthesized in the rete testis and in the epithelium of the seminal vesicles. The latter are also the major contributors of seminal plasma AWN. In addition, immunoblotting analysis has shown that AWN is present on epididymal spermatozoa. Our results indicate that the cellular origin of spermadhesins is species-specific. The attachment of AWN to epididymal spermatozoa is probably important in developing the capacity for fertilization.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00319144
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