Spermadhesin PSP-I/PSP-II Heterodimer and Its Isolated Subunits Induced Neutrophil Migration into the Peritoneal Cavity of Rats1

Abstract

Spermadhesins are a group of (glyco)proteins from seminal fluid involved in various aspects of porcine fertilization. PSP-I/PSP-II, a heterodimer of glycosylated spermadhesins, is the major component of porcine seminal fluid. Its biological function remains, however, enigmatic. Using an in vitro chemotaxis assay, we showed that PSP-I/PSP-II and its isolated subunits induced migration of purified neutrophils. A possible proinflammatory activity of PSP-I/PSP-II induced upon injection of the spermadhesin heterodimer and its isolated subunits into the peritoneal cavity of rats was investigated. Lavage of peritoneal cavities, thioglycolate treatment, and mast cell depletion were done before spermadhesin administration, and neutrophil migration was evaluated 4 h after injections. Pharmacological modulation was also investigated. Resident cell depletion by lavage reduced the neutrophil migration induced by PSP-I/PSP-II and the PSP-II subunit but had no effect on that induced by isolated PSP-I. Both an increase of macrophage population by thioglycolate treatment and mast cell depletion potentiated the neutrophil migration induced by PSP-I/PSP-II and by PSP-II. The glucocorticoid dexamethasone but not indomethacin (cyclooxygenase inhibitor), MK886 (leukotriene inhibitor), and BN50739 (platelet activation factor [PAF] antagonist) inhibited neutrophil migration induced by PSP-I/PSP-II. Coincubation with mannose-6-phosphate (a PSP-II-specific ligand) inhibited neutrophil recruitment induced by PSP-II but did not alter the PSP-I activity. As a whole, the data suggested that enhancement of the neutrophil migration-inducing activity of PSP-I/PSP-II and PSP-II involved an indirect mechanism, i.e., via activation of resident cells, probably macrophages. On the other hand, PSP-I appeared to act directly on neutrophils. We hypothesize that the neutrophil migration-inducing effect displayed by PSP-II might be due to interaction of its lectin domain with cellular receptors and that neutrophil recruitment induced by PSP-I may involve protein-protein interactions.

Seminal Plasma Proteins as Potential Markers of Relative Fertility in Boars

“…PSP-I and AWN-1 are members of the spermadhesin protein family isolated from seminal plasma and may play an important role during fertilization (Tö pferPetersen et al, 1998;Yang et al, 1998;Maná sková et al, 2000;Assreuy et al, 2002). PSP-I has multiple forms because of differences in its carbohydrate moiety (Rutherfurd et al, 1992;Nimtz et al, 1999).…”

“…The major seminal plasma glycoprotein (PSP-I), isolated and identified from boar seminal plasma by Rutherfurd et al (1992), may prevent premature capacitation and the acrosome reaction (Kwok et al, 1993;Tö pfer-Petersen et al, 1998). This protein may also have immunoregulatory activity (Kwok et al, 1993;Yang et al, 1998;Assreuy et al, 2002Assreuy et al, , 2003. AWN-1 is another spermadhesin that affects zona pellucida-binding activity (Sanz et al, 1992;Rodríguez-Martínez et al, 1998) and may also have a role in the capacitation process (Calvete et al, 1997;Tö pfer-Petersen et al, 1998).…”

Dissecting the Protective Effect of the Seminal Plasma Spermadhesin PSP‐I/PSP‐II on Boar Sperm Functionality

“…Hence, PSP‐I and PSP‐II are immunostimulatory for lymphocyte activity in vitro (Nimtz et al, 1999), and binding of PSP‐I to lymphocyte has been demonstrated (Yang et al, 1998). Furthermore, the PSP‐I/PSP‐II heterodimer and its isolated subunits induce the recruitment of neutrophils into the peritoneal cavity of rats (Assreuy et al, 2002) and pigs (Rodríguez‐Martínez et al, 2005). The neutrophil migration‐inducing activity of PSP‐I/PSP‐II, and possibly of the PSP‐II subunit, is mediated by the stimulation of resident macrophages, which release a neutrophil chemotactic substance (Assreuy et al, 2002), whereas PSP‐I appears to act directly on neutrophils (Assreuy et al, 2003).…”

Evolution of the spermadhesin gene family

“…Therefore, they have been implicated in the carbohydrate-mediated events during sperm transport through the female reproductive tract and fertilization e.g. immunosuppression (PSP-I/PSP-II complex; Nimtz et al, 1999;Assreuy et al, 2002), spermoviduct interaction (AQN-1; Wagner et al, 2002;EkhlasiHundrieser et al, in press), and gamete interaction (Rodriguez-Martinez et al, 1998). The flexible glycan chains presented by the epithelial cells and the zona pellucida may anchor the entering sperm to the oviductal epithelium and the capacitating sperm to the gamete allowing then all down stream events.…”