title: Dissecting the protective effect of the seminal plasma spermadhesin PSP-I/PSP-II on boar sperm functionality.
abstract: To dissect the protective activity of PSP-I/PSP-II, the effect of the isolated subunits PSP-I and PSP-II and their affinity-purified tryptic peptide and glycan fractions on the viability, mitochondrial activity, and motility of highly diluted boar spermatozoa was investigated. High dilution exerted a negative effect on control spermatozoa. Incubation of spermatozoa with PSP-I/PSP-II or with its PSP-II subunit had a protective effect on sperm functionality, high mitochondrial membrane potential, and sperm motility. These effects were less pronounced when spermatozoa were incubated with the PSP-I subunit. It was noteworthy that motility was abolished by incubation of spermatozoa with isolated PSP-I. Trypsin-degraded PSP-I/PSP-II, PSP-I, and PSP-II reproduced the effects of the native proteins. Incubating spermatozoa with the glycan-depleted tryptic-peptide fraction of PSP-I/PSP-II for 5 hours preserved a higher percentage of viable spermatozoa than when sperm was incubated for the same time with the native heterodimer, trypsin-digested PSP-I/PSP-II, the glycan fraction or without added proteins. However, sperm motility decreased as the concentration of added peptide fraction increased. On the other hand, spermatozoa incubated with the glycan fraction showed lower values than spermatozoa incubated with the peptide fraction. We concluded that the subunits of the PSP-I/PSP-II heterodimeric spermadhesin exert different activities on sperm functions. The finding that the beneficial effect of the native PSP-I/PSP-II on the functionality of highly diluted boar spermatozoa is largely preserved in its isolated PSP-II subunit and does not appear to require the glycan moiety points to a peptide moiety as a potential sperm function-preserving additive of highly diluted boar spermatozoa.
authors.affiliation: Departamento de Medicina y Cirugía Animal, Facultad de Veterinaria, Universidad de Murcia, Campus de Espinardo, 30071 Murcia, Spain.
authors.forename: Eva M
authors.initials: EM
authors.lastname: Garcia
authors.forename: Juan M
authors.initials: JM
authors.lastname: Vázquez
authors.forename: Juan J
authors.initials: JJ
authors.lastname: Calvete
authors.forename: Libia
authors.initials: L
authors.lastname: Sanz
authors.forename: Ignacio
authors.initials: I
authors.lastname: Caballero
authors.forename: Inmaculada
authors.initials: I
authors.lastname: Parrilla
authors.forename: Maria A
authors.initials: MA
authors.lastname: Gil
authors.forename: Jordi
authors.initials: J
authors.lastname: Roca
authors.forename: Emilio A
authors.initials: EA
authors.lastname: Martinez
mesh_terms: D000818:Animals; D019483:Disintegrins / Q000494:pharmacology; D006020:Glycopeptides / Q000494:pharmacology; D008297:Male; D010446:Peptide Fragments / Q000494:pharmacology; D020836:Protein Structure, Quaternary; D029607:Seminal Vesicle Secretory Proteins / Q000502:physiology*; D013081:Sperm Motility / Q000187:drug effects; D013094:Spermatozoa / Q000187:drug effects / Q000502:physiology*; D013552:Swine; D014357:Trypsin / Q000378:metabolism
chemical_list: D019483:Disintegrins; D006020:Glycopeptides; D010446:Peptide Fragments; D029607:Seminal Vesicle Secretory Proteins; C074521:seminal vesicle secretory protein II, porcine; C074520:seminal vesicle secretory protein 109, porcine; D014357:Trypsin