Equine spermadhesin HSP-7 is a 14 kDa protein isolated from stallion seminal plasma and present on the surface of spermatozoa. HSP-7 displays carbohydrate and zona-pellucida binding properties, but the physiological role in equine fertilization is not well defined. HSP-7 has 98% amino acid sequence homology with the well-studied boar spermadhesin, AWN. Currently, these two proteins are considered to have the same reproductive function. Immunofluorescence studies presented here show that the stallion and boar spermadhesins are localized to different segments on spermatozoa. The variation in molecular compartmentalization of spermadhesin molecules in different species suggests that these structurally related proteins could be involved in independent events of fertilization. While the variation in HSP-7 abundance was not statistically significant between fertile and subfertile stallions, capacitated spermatozoa displayed a marked increase in HSP-7 when compared to neat sperm (P < 0.05). These results indicate that rather than aiding in capacitation, HSP-7 is exposed with capacitation and may have a more significant role in the acrosome reaction and sperm-oocyte recognition than previously documented.

Interactions between proteins and saccharide moieties play an indispensable role in mammalian reproduction as they stand behind of such processes as maturation and mutual recognition of gametes and sperm oviductal reservoir formation. In my dissertation thesis I focused on activities of glycosidases from bovine and porcine follicular fluids and their changes connected with follicle development. Activities of five glycosidases were detected in tertiary and preovulatory follicles in both species. The most active enzymes were α-L-fucosidase in cow and α-D-mannosidase in sow and both enzymes also demonstrated the most pronounced increase in their activities during follicle maturation. Interestingly, both α-L-fucose in cow and α-D-mannose in sow were described as saccharides responsible for the formation of the sperm oviductal reservoir and we offered a hypothetical mechanism of synchronisation between sperm release from their reservoir with the time of ovulation based on a surge of activities of corresponding follicular glycosidases through the oviduct. Subsequently, it was demonstrated that β-D-galactosidase and α-D-mannosidase affect sperm-zona pellucida binding in pig, as they both decrease interaction between sperm receptors for zona pellucida and zona pellucida. This may explain the observation...

En la siguiente tesis se obtuvieron los siguientes resultados. La adición de plasma seminal a los espermatozoides altamente diluidos ejerce un efecto beneficioso variable dependiendo de la fuente de plasma seminal. El heterodímero PSP-I/PSP-II ejerce un efecto beneficioso sobre los espermatozoides altamente diluidos mediante su adhesión al acrosoma. La incubación produce la migración del heterodímero a la región post-acrosomal, siendo eliminado de la superficie espermática. La adición del heterodímero a los medios de cocultivo entre gametos disminuye significativamente la capacidad fecundante de los espermatozoides. La preincubación de los espermatozoides de verraco tanto frescos como congelados preserva la viabilidad y motilidad espermáticas no afecta a la capacidad fecundante de los espermatozoides frescos de verraco y disminuye la capacidad fecundante de los espermatozoides congelados, la cual puede ser restaurada parcialmente mediante un lavado a través de un gradiente de Percoll. / The addition of 10% of seminal plasma from certain boars maintains or enhances the viability of largely extended boar spermatozoa in vitro. The protective effect of the PSP-I/PSP-II heterodimer on highly-extended boar spermatozoa could be related to the adhesion of the heterodimer to the acrosome. Exposures of the gametes to the heterodimer during in vitro gamete co-incubation significantly decrease the sperm penetration rates and number of spermatozoa per oocytes in denuded oocytes. The effect could be mediated by exposed ZP receptors. Exposure of fresh or frozen-thawed boar spermatozoa to PSP-I/PSP-II preserves sperm viability and motility. Although there is no obvious influence of the heterodimer on the capability of fresh diluted boar spermatozoa to penetrate homologous oocytes, PSP-I/II exerts a deleterious effect when frozen-thawed spermatozoa are used to penetrate IVM-oocytes. A subsequent washing through a Percoll gradient estored sperm function in some of the cells.