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      Prostasome-like vesicles stimulate acrosome reaction of pig spermatozoa

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          Abstract

          Background

          The presence of small membranous particles characterizes the male genital fluids of different mammalian species. The influence of semen vesicles, denominated prostasomes, on sperm functional properties has been well documented in humans, but their biological activity is scarcely known in other species. The present work investigated prostasome-like vesicles in pig semen for their ability to interact with spermatozoa and to affect acrosome reaction.

          Methods

          Prostasome-like vesicles have been isolated from pig seminal plasma by high-speed centrifugation and Sephadex G-200 gel chromatography. Morphology of purified vesicles has been checked by scanning electron microscopy while their protein pattern has been investigated by SDS-PAGE. Then prostasome- like vesicles have been incubated with pig spermatozoa and their ability to interact with sperm has been tested by the aminopeptidase assay. In addition, the efficiency of vesicles to influence the acrosome reaction has been investigated by assessing the sperm acrosomal status by the PI/FITC-PNA (propidium iodide/fluorescein isothiocyanate-labeled peanut agglutinin) stainings.

          Results

          Purified vesicles revealed a complex protein pattern with the occurrence of bands in the high, medium and low molecular weight range. However, the two major bands were observed at ~90 kDa and ~60 kDa. A vesicle-mediated transfer of aminopeptidase to sperm cells has been also detected. Furthermore, a significant increase of acrosome reaction extent has been revealed in spermatozoa incubated with prostasome-like vesicles in comparison to control sperm.

          Conclusion

          This is the first report demonstrating that pig prostasome-like vesicles are able, in vitro, to interact with spermatozoa and to stimulate the acrosome reaction. These findings lead to hypothesize a transfer of molecules from vesicles to sperm membrane, thus sensitizing male gametes to undergo the acrosome reaction

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          The prostasome: its secretion and function in man.

          Rachel I. Brody, G Ronquist (1985)
          An intact organelle, the prostasome, is secreted by the acinar epithelial cell of the human prostate gland. The ultrastructural location of the prostasome is within membrane-bound storage vesicles in the epithelial cells. Prostasomes are delivered into the glandular lumen by an exocytotic event, which is preceded by fusion of adjacent membranes belonging to the storage vesicle and the epithelial cell. Alternatively, the storage vesicle can be translocated in toto from the cell interior into the acinar lumen through the plasma membrane. This latter event has been designated diacytosis. Both phenomena seem to occur with approximately equal frequency in the human prostate gland. An ATPase system that is Mg2+ and Ca2+-dependent is firmly linked to the membranes encasing the prostasomes. The ATPase system may be the molecular basis for vectorial transport of calcium into these organelles. Also a protein kinase activity is located in the membranes. An increase in membrane thickness was observed on phosphorylation. The physiologic function of the prostasomes is not known. They may be important for promoting forward motility of spermatozoa.
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            Identification, proteomic profiling, and origin of ram epididymal fluid exosome-like vesicles.

            Jean-Luc Gatti, Sonia Métayer, Maya Belghazi … (2005)
            Small membranous vesicles, between 25- and 75-nm diameter, were collected by high-speed centrifugation from the ram cauda epididymal fluid and were found to be normal constituents of this fluid and of the seminal plasma. The SDS-PAGE protein pattern of these vesicles was specific and very different from that of the caudal fluid, seminal plasma, sperm extract, and cytoplasmic droplets. After two-dimensional electrophoresis separation and mass spectrometry analysis, several proteins were identified and grouped into i) membrane-linked enzymes, such as dipeptidyl peptidase IV (DPP-IV), neprilysin (NEP), phosphodiesterase-I (E-NPP3), and protein G-beta; ii) vesicle-associated proteins, such as lactadherin (MFEG8-PAS6/7) and vacuolar ATPase; iii) several cytoskeleton-associated proteins, such as actin, ezrin and annexin; and iv) metabolic enzymes. The presence of some of these proteins as well as several different hydrophobic proteins secreted by the epididymis was further confirmed by immunoblotting. These markers showed that the majority of the vesicles originated from the cauda epididymal region. The physical and biochemical characteristics of these vesicles suggest they are the equivalent of the exosomes secreted by several cell types and epithelium. The main membrane-linked proteins of the vesicles were not retrieved in the extract from cauda or ejaculated sperm, suggesting that these vesicles did not fuse with sperm in vivo.
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              Prostasome-like particles are involved in the transfer of P25b from the bovine epididymal fluid to the sperm surface.

              Robert Sullivan, Gilles Frenette (2001)
              In bulls, P25b is a sperm protein associated with the plasma membrane covering the acrosome. The amount of P25b bound to a constant number of spermatozoa varies from one individual to the other, low levels being associated with bull subfertility. In this study, we describe the epididymal origin of P25b using Western blot analysis. Whereas P25b was undetectable on caput spermatozoa, the amount of P25b associated to a constant number of spermatozoa increases from the corpus to the cauda. Prostasome-like particles were prepared by ultracentrifugation of epididymal fluid. P25b appears to be also associated with those membranous vesicles in increasing amounts along the epididymis. P25b is anchored to the plasma membrane of spermatozoa through glycosylphosphatidyl-inositol as shown by the ability of phospholipase C. but not of high salt treatment, to release P25b. Coincubation experiments revealed that prostasome-like particles are able to transfer P25b to spermatozoa, this process being more efficient at slightly acidic pH. P25b thus appears to be a marker of sperm epididymal maturation in bulls.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Reprod Biol Endocrinol
                Title: Reproductive biology and endocrinology : RB&E
                Publisher: BioMed Central
                ISSN (Electronic): 1477-7827
                Publication date Collection: 2008
                Publication date (Electronic): 30 January 2008
                Volume: 6
                Page: 5
                Affiliations
                [1 ]Department of Cell Biology, Faculty of Pharmacy, University of Calabria, Cosenza, Italy
                [2 ]Department of Experimental Medicine, Human Anatomy Section, University of Palermo, Italy
                Article
                Publisher ID: 1477-7827-6-5
                DOI: 10.1186/1477-7827-6-5
                PMC ID: 2266753
                PubMed ID: 18234073
                SO-VID: 026ce126-a132-483f-bca4-61abebad3b3c
                Copyright © Copyright © 2008 Siciliano et al; licensee BioMed Central Ltd.
                License:

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 28 November 2007
                Date accepted : 30 January 2008
                Categories
                Subject: Research

                ScienceOpen disciplines: Human biology
                Data availability:
                ScienceOpen disciplines: Human biology

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