Select boar seminal plasma (SP) components and their relation to semen quality were investigated. Thirty nine boars from three artificial insemination (AI) centers were divided into group A (GA: > 80% normal sperm and >70% motility) and group B (GB: < 80% normal sperm and < 70% motility). Each ejaculate was collected and semen volume, concentration, sperm motility (computer aided semen analysis; CASA), morphology, and vitality (both eosin nigrosin staining) were investigated. The SP was separated and analyzed for aspartate-amino-transferase (AST), γ-glutamyl-transferase (GGT), alkaline phosphatase (ALP) activity, and the concentrations of sodium (Na), potassium (K), chloride (Cl), calcium (Ca), phosphate (PO 4 3-), magnesium (Mg), selenium (Se) and zinc (Zn) were assessed. Repeated measures (2 months interval) were conducted in eight boars of GA from one AI center. The activity of GGT (r = -0.482) and ALP (r = -0.459) was moderately associated ( p < 0.05) with ejaculate volume and strongly associated with concentration (r = 0.580 and r = 0.618, respectively; p = 0.000). Moderate associations ( p < 0.05) were found between ALP (r = 0.439), GGT (r = 0.387), Na (r = -0.428), K (r = 0.354), and Se (r = 0.354) with progressive motility. The SP concentration of Na (r = -0.401), Cl (r = -0.521), and K (r = 0.350) was associated ( p < 0.05) with normal morphology. Only Mg was associated ( p < 0.05) with membrane damage (r = -0.335). The concentration of Na, Cl, and Zn (1681.0 vs. 1701.0 µg/dL) was different between groups ( p < 0.05). Repeated measures showed significant differences in time but only for Na, Mg, and Zn ( p < 0.05). In conclusion, several biochemical components of SP were related to semen quality. The analysis of biochemical parameters could provide extra information about reproductive health of AI boars.

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In this study, we report for the first time on a possible contribution of metalloproteases in sperm passage through the cumulus matrix in pigs. The presence of 20 mM 1,10-phenanthroline (1,10-PHEN), inhibitor of zinc-dependent metalloproteases, strongly inhibited the degree of sperm penetration in cumulus-intact (CI), but not in cumulus-free (CF), porcine oocytes during IVF. The inhibitory effect of 1,10-PHEN was due to the chelation of metal ions as a non-chelating analog (1,7-PHEN) did not affect IVF rates. Furthermore, incubation with 1,10-PHEN did not affect sperm binding to the zona pellucida nor sperm motility, membrane integrity, or acrosomal status. These findings led to the assumption that 1,10-PHEN interacts with a sperm-or cumulus-derived metalloprotease. Metalloproteases are key players in physiological processes involving degradation or remodeling of extracellular matrix. In vivo, their proteolytic activity is regulated by tissue inhibitors of metalloproteases (TIMP1-TIMP4). We tested the effect of TIMP3 on fertilization parameters after porcine IVF. Similar to 1,10-PHEN, TIMP3 inhibited total fertilization rate of CI but not CF oocytes and did not influence sperm quality parameters. Although the inhibitory effect was stronger in CI oocytes, TIMP3 also reduced the degree of sperm penetration in CF oocytes, suggesting the involvement of a metalloprotease in a subsequent step during fertilization. In conclusion, our results indicate the involvement of TIMP3-sensitive, zinc-dependent metalloprotease activity in sperm passage through the cumulus oophorus in pigs. The results should provide the basis for further biochemical research toward the localization and identification of the metalloprotease involved.

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