Immunolocalization and Quantitation of Acidic Seminal Fluid Protein (aSFP) in Ejaculated, Swim-up, and Capacitated Bull Spermatozoa

Dostálová, Zuzana; Calvete, Juan J.; Sanz, Libia; Hettel, Christiane; Riedel, Diana; Schöneck, C.; Einspanier, Ralf; Töpfer‐Petersen, Edda

doi:10.1515/bchm3.1994.375.7.457

Cited by 52 publications

(41 citation statements)

References 21 publications

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“…The most characteristic features of the CUB domain are the existence of three or four conserved Cys residues that form two disulfide bonds and the existence of various hydrophobic and aromatic amino acid residues that participate in the formation of the antiparallel ␤-barrel topography of the molecule. CUB domains in mammalian spermadhesin are known to be involved in sperm binding to the zona pellucida (15)(16)(17)(18). Our present results showing that the C-terminal CUB domain 1 of ascidian proacrosin is involved in the binding to the vitelline coat coincide well with the above-mentioned fact regarding the CUB domain in mammalian spermadhesin.…”

Section: Discussionmentioning

confidence: 99%

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cDNA Cloning and Functional Analysis of Ascidian Sperm Proacrosin

Kodama

Baba

Yokosawa

et al. 2001

Journal of Biological Chemistry

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cDNA cloning and functional analysis of proacrosin from the ascidian Halocynthia roretzi were undertaken. The isolated cDNA of the ascidian preproacrosin consists of 2367 nucleotides, and an open reading frame encodes 505 amino acids, which corresponds to the molecular mass of 55,003 Da. The mRNA of proacrosin was found to be specifically expressed in the gonad by Northern blotting and in the spermatocytes or spermatids by in situ hybridization. The amino acid sequences around His 76 , Asp 132 , and Ser 227 , which make up a catalytic triad, showed high homology to those of the trypsin family. Ascidian acrosin has paired basic residues (Lys 56 -His 57 ) in the N-terminal region, which is one of the most characteristic features of mammalian acrosin. This region seems to play a key role in the binding of (pro)acrosin to the vitelline coat, because the peptide containing the paired basic residues, but not the peptide substituted with Ala, was capable of binding to the vitelline coat. Unlike mammalian proacrosin, ascidian proacrosin contains two CUB domains in the C-terminal region, in which CUB domain 1 seems to be involved in its binding to the vitelline coat. Four components of the vitelline coat that are capable of binding to CUB domain 1 in proacrosin were identified. In response to sperm activation, acrosin was released from sperm into the surrounding seawater, suggesting that ascidian acrosin plays a key role in sperm penetration through the coat. These results indicate that ascidian sperm contains a mammalian acrosin homologue, a multi-functional protein working in fertilization.In fertilization, sperm must bind to and penetrate through the extracellular glycoprotein matrix surrounding the egg, which is called the zona pellucida in mammals and the vitelline coat in marine invertebrates. After this process, membrane fusion occurs between the sperm and egg. Upon primary binding of the sperm to the vitelline coat, it undergoes an acrosome reaction, which is an exocytosis of the acrosomal vesicle located on the tip of the sperm head. A lytic agent called lysin is exposed on the surface of the sperm head and partially released into the surrounding seawater during the acrosome reaction. In mammals, it has been believed that a trypsin-like enzyme called acrosin (EC 3.4.21.10) is a zona lysin (1, 2). However, recent studies using acrosin-gene knockout mice have revealed that acrosin is not essential for mouse fertilization, although a significant delay (about 30 min) in sperm penetration through the zona pellucida was observed (3, 4). From these results it is currently thought that sperm proteases other than acrosin may participate in sperm penetration through the mammalian egg coat and that acrosin may be involved in the dispersal of the acrosomal matrix (5).Ascidians (Urochordata) occupy a phylogenetic position between vertebrates and "true" invertebrates. Although all ascidians are hermaphrodites, several ascidians including Halocynthia roretzi are strictly self-sterile. The vitelline-coat lysin system is thought...

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Section: Discussionmentioning

confidence: 99%

“…In addition, ascidian proacrosin, but not mammalian proacrosin, has two CUB domains in the C-terminal region. It is known that CUB domains are involved in sperm binding to the zona pellucida in the mammalian spermadhesin molecule (15)(16)(17)(18).…”

Section: Cdna Cloning and Functional Analysis Of Ascidian Sperm Proacmentioning

confidence: 99%

cDNA Cloning and Functional Analysis of Ascidian Sperm Proacrosin

Kodama

Baba

Yokosawa

et al. 2001

Journal of Biological Chemistry

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“…Aggregated spermadhesins could then become coated on top of this first layer, serving as stabilizing factors that protect the acrosome membrane from premature acrosome reaction. 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%

“…They are immunostimulatory for lymphocyte activity in vitro (Nimtz et al, 1999) and prevent possible infections of the lower reproductive tract and provide a foreign cell-free uterine environment for the descending early embryos (Assreuy et al, 2003). The bovine spermadhesin aSFP binds only loosely to the surface of ejaculated bovine sperm and is quantitatively released during in vitro capacitation (Dostàlovà et al, 1994). This protein appears to stimulate in a dose-dependent manner (in the ng/ml range) in vitro cell division of lymphocytes and progesterone secretion by bovine endometrium and ovarian granulosa cells (Einspanier et al, 1991).…”

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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“…Bovine aSFP is a typical component of the ASG fluid (Moura et al, 2007b;Wempe et al, 1992), although evidence exists that it is expressed in the cauda epididymal fluid as well (Moura et al, 2010). aSFP has redox activity superior to that of glutathione peroxidase (Einspanier et al, 1993;Schoneck et al, 1996), binds to ejaculated bovine sperm (Dostalova et al, 1994) and inhibits sperm motility in a reversible manner (Schoneck et al, 1996). Thus, aSFP protects sperm against oxidative stress in both pre-and post-ejaculation media and its inhibition of motility may be of importance during sperm storage in the cauda epididymis.…”

Section: Proteome Of Seminal Fluidmentioning

confidence: 99%