Mapping the heparin‐binding domain of boar spermadhesins

Calvete, Juan J.; Dostálová, Zuzana; Sanz, Libia; Adermann, Knut; Thole, Hubert; Töpfer‐Petersen, Edda

doi:10.1016/0014-5793(95)01513-2

Cited by 34 publications

(30 citation statements)

References 33 publications

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“…The findings of our previous study demonstrated the presence of high molecular weight zinc-binding protein ligands in boar and canine seminal plasma (18,19). Under the influence of denaturing and reducing agents, they dissociate to low molecular weight polypeptides that together with sperm-adhesive properties are also present in large quantities in boar, bull, and stallion seminal plasma (8,9,31). The spermadhesins' structure and function are well-documented, in contrast to canine seminal plasma proteins with almost unknown properties.…”

Section: Discussionmentioning

confidence: 99%

Effect of seminal plasma zinc–binding proteins on motility and membrane integrity of canine spermatozoa stored at 5°C

Mogielnicka-Brzozowska

Dziekońska

Strzeżek

et al. 2014

Bulletin of the Veterinary Institute in Pulawy

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Sperm surface binding sites for non-zinc-binding proteins (nZnBPs) and zinc-binding proteins (ZnBPs) were studied by the fluorescence technique with biotin-labelled proteins. The nZnBPs binding pattern was unspecific, no characteristic sites on plasmalemma were found. ZnBPs were attached mainly to the acrosomal region of sperm head and to the sperm flagellum. ZnBPs added to the incubation mixture of the canine spermatozoa allowed the preservation of higher valu es for total motility, progressive motility, curvilinear line velocity, straight line velocity, and beat cross frequency (P < 0.05), both at time 0 and after 1 h incubation at 5ºC. The addition of nZnBPs to the incubation mixture caused only weak positive effects when compared with control sample (PBS). A higher percentage of canine-ejaculated spermatozoa with intact membranes were observed when ejaculate was incubated with ZnBPs in comparison to control sample stored with PBS (P < 0.05) or nZnBPs (P < 0.05). Spermatozoa diluted with ZnBPs and nZnBPs exhibited a higher percentage of cells with active mitochondria when compared with control, both at time 0 and after 1 h; however, no statistical differences were observed. Our results emphasise the role of seminal plasma protein in securing the correct quantity and availability of zinc ions as a component regulating the motility of canine spermatozoa. The protective effect of ZnBPs against the cooling effect may be due to their ability of preventing sperm membrane damage.

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Section: Discussionmentioning

confidence: 99%

Effect of seminal plasma zinc–binding proteins on motility and membrane integrity of canine spermatozoa stored at 5°C

Mogielnicka-Brzozowska

Dziekońska

Strzeżek

et al. 2014

Bulletin of the Veterinary Institute in Pulawy

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“…These spermadhesins are thought to stabilize the plasma membrane over the acrosomal vesicle and are mainly released from the spermatozoal surface during capacitation (Sanz et al, 1993;Dostàlovà et al, 1994;Calvete et al, 1997). A phosphorylethanolamine-binding region has been mapped to a discontinuous region of AWN comprising residues 6-12 and 104-108 (Ensslin et al, 1995), and a conformational heparin-binding surface, which partly overlaps with the phosphorylethanolaminebinding region, resides in an opposite location to the carbohydrate-binding region of the spermadhesin (Calvete et al, 1996a).…”

Section: Sperm-oviduct Interactionmentioning

confidence: 99%

Glycobiology of fertilization in the pig

Töpfer‐Petersen¹,

Ekhlasi-Hundrieser²,

Tsolova³

2008

Int. J. Dev. Biol.

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By adopting internal fertilization, the meeting of both gametes -the sperm and the egg -and thus the highly coordinated sequence of interactions leading to fertilization, occur in the female reproductive tract. In mammals, the oviduct has been shown to translate the requirements of the female, coordinating sperm activation (capacitation) and sperm transport with the arrival of the ovulated egg. A hierarchy of carbohydrate-based interactions accompanies these events ranging from the binding of uncapacitated sperm to the oviductal epithelium (establishment of the female sperm reservoir), to the primary and secondary binding processes contributing to gamete recognition and sperm penetration of the oocyte zona pellucida. The current perspective will focus on the carbohydrate-recognition systems in the binding events during fertilization in the pig. The roles of the major carbohydrate-binding proteins, the spermadhesins and the acrosomal serine proteinase, pro/acrosin are discussed under consideration of recent structural data. The glycans and the glycoproteins of the porcine oviduct with a focus on the candidate sperm receptors as well as the zona pellucida N-glycans of prepuberal pigs have been characterized by a mass spectrometric approach. Furthermore, some preliminary data supporting the hypothesis that the zona pellucida has to undergo a maturation process during oocyte development are presented. KEY WORDS: gamete interaction, spermadhesin, acrosin, zona pellucida, glycoprotein, glycan A short review of mammalian fertilizationThe fertilization of an egg by a sperm is the fundamental event in life, as it culminates in the creation of a new individual. In mammals, the meeting of the fertilizing competent sperm and the ovulated egg is the beginning of a highly coordinated sequence of cellular interactions between the haploid gametes, which leads to the formation of the diploid zygote and initiates embryonic development.The first contact between sperm and egg takes place at the outer surface of the surrounding extracellular matrix of the egg, the zona pellucida (ZP). By binding to distinct oligosaccharides of the ZP glycoproteins, the fertilizing sperm recognizes the egg. Upon anchoring the sperm to the egg through the ZP carbohydrates the signaling cascade leading to acrosomal exocytosis of the sperm is activated allowing the sperm to pass through the zona pellucida. The acrosome-reacted sperm in the end interacts and fuses with the egg plasma membrane, which in turn enables the egg to complete meiosis, to initiate the mechanisms to prevent Int.

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“…the N-terminal domain of TSG-6, and not with the full-length protein (19 -23). However, the CUB domain, known as a GAG-binding domain from studies with other proteins, may also affect the binding of TSG-6 to GAGs (17,24,25). Therefore, the binding of full-length, glycosylated TSG-6 protein to GAGs deserves additional study.…”

Section: Tnfmentioning

confidence: 99%

TSG-6 Protein Binding to Glycosaminoglycans

Wisniewski

Snitkin

Mindrescu

et al. 2005

Journal of Biological Chemistry

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TSG-6 protein, up-regulated in inflammatory lesions and in the ovary during ovulation, shows anti-inflammatory activity and plays an essential role in female fertility. Studies in murine models of acute inflammation and experimental arthritis demonstrated that TSG-6 has a strong anti-inflammatory and chondroprotective effect. TSG-6 protein is composed of the N-terminal link module that binds hyaluronan and a C-terminal CUB domain, present in a variety of proteins. Interactions between the isolated link module and hyaluronan have been studied extensively, but little is known about the binding of full-length TSG-6 protein to hyaluronan and other glycosaminoglycans. We show that TSG-6 protein and hyaluronan, in a temperature-dependent fashion, form a stable complex that is resistant to dissociating agents. The formation of such stable complexes may underlie the activities of TSG-6 protein in inflammation and fertility, e.g. the TSG-6-dependent cross-linking of hyaluronan in the cumulus cell-oocyte complex during ovulation. Because adhesion to hyaluronan is involved in cell trafficking in inflammatory processes, we also studied the effect of TSG-6 on cell adhesion. TSG-6 binding to immobilized hyaluronan did not interfere with subsequent adhesion of lymphoid cells. In addition to immobilized hyaluronan, full-length TSG-6 also binds free hyaluronan and all chondroitin sulfate isoforms under physiological conditions. These interactions may contribute to the localization of TSG-6 in cartilage and to its chondroprotective and anti-inflammatory effects in models of arthritis.

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Mapping the heparin‐binding domain of boar spermadhesins

Cited by 34 publications

References 33 publications

Effect of seminal plasma zinc–binding proteins on motility and membrane integrity of canine spermatozoa stored at 5°C

Effect of seminal plasma zinc–binding proteins on motility and membrane integrity of canine spermatozoa stored at 5°C

Glycobiology of fertilization in the pig

TSG-6 Protein Binding to Glycosaminoglycans

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