Characterization of Fibronectin on Human Spermatozoa

Vuento, Matti; Kuusela, Pentti; Virkki, Marika; Koskimies, Aarne I.

doi:10.1515/bchm2.1984.365.2.757

Cited by 34 publications

(24 citation statements)

References 9 publications

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“…Fibronectin or fibronectin-related polypeptides have been found on human and rabbit ejaculated sperm membranes, predominantly overlying the head region (Koehler et al, 1980;Vuento et al, 1984;Glander et al, 1987). More conclusive comparisons await further characterization of the plasma membrane heparinbinding proteins.…”

Section: Heparin-binding Proteins On Spermmentioning

confidence: 99%

Carbohydrates and fertilization in animals

Miller

1990

Molecular Reproduction Devel

120

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A frequently used mechanism for sperrn-egg recognition in many species involves complementary protein-carbohydrate interaction. The usual paradigm includes complex glycoconjugates in reproductive tract fluids or on the eggs which are recognized by carbohydratebinding proteins on the sperm surface. Various glycoconjugates are utilized in the steps of sperm capacitation, sperm binding to the egg extracellular matrix and vitelline membrane and induction of the acrosome reaction. Several types of complex glycoconjugates are involved in these processes, including proteoglycans, lactosaminoglycans, sulfated fucose-containing glycoconiugates, and glycoproteins. There appear to be some structural similarities between active glycoconjugates; they are large in molecular weight and complex, and they are often sulfated, fucosylated, and attached to a protein through serine or threonine residues. In some species, the protein core of the glycoconjugates also participates in the interaction by limiting the binding of carbohydrates to sperm only of the relevant species, likely by providing the proper steric arrangement for the interaction. In other cases the protein core seems to serve more as a crosslinker of the carbohydrate moieties. This review discusses the types of glycoconjugates implicated in fertilization and the complementary lectinlike proteins found on sperm.Key Words: Sperm, Eggs, Glycosaminoglycans, Glycoconjugates, Glycoproteins, Zona pellucida, Capacitation, Acrosorne reaction, Fertilization cess differ between species, there is remarkable conservation in the ability of sperm to use glycoconjugates in reproductive tract secretions or in the egg extracellular matrix and vitelline membrane for fertilization-related events. This review summarizes research from various animals in which glycoconjugates are important in sperm-egg interaction. It contrasts differences between species at the point of the fertilization process where carbohydrates interact with sperm. Furthermore, a structural comparison between each of the carbohydrates is presented.An understanding of fertilization-related events is necessary prior to a discussion of the potential molecules involved in sperm-egg interaction. There are differences between species in the events occurring both before and during sperm-egg interaction. These events are best understood in sea urchins and mice, although there is recent information from other species. A diagram of sperm-egg interaction in sea urchins is shown in Figure

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Section: Heparin-binding Proteins On Spermmentioning

confidence: 99%

Carbohydrates and fertilization in animals

Miller

1990

Molecular Reproduction Devel

120

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“…The presence of a fibronectin fragment in this complex suggests that fibronectin fragment may remain bound to PIP and promote the assembly of other proteins. Fibronectin also interacts with integrin [42] and promotes cell adhesion and it might be working here as a bridge between sperm cell [43,44] and this complex, although ZAG and PIP are known to bind to sperm on their own as well [ 45,46]. In a recent finding, fibronectin was found to induce the sperm acrosome reaction by a signal transduction mechanism [47] and ZAG is known to modulate sperm motility [46,48].…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of a native zinc‐binding high molecular weight multiprotein complex from human seminal plasma

Yadav

Kumar

Chhikara

et al. 2011

J of Separation Science

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The seminal plasma comprises secretions from various accessory sex glands. During fertilization spermatozoa undergo complex sequences of precisely timed events that are regulated by the activation of different intracellular signaling pathways. The precision and efficacy of these pathways are often influenced by the assembly and interactions of multiprotein complexes, thereby directing the flow of regulatory information. Our knowledge about these protein complexes present in human seminal plasma (HuSP) is limited. Here we report the identification and characterization of a native high molecular weight zinc-binding multiprotein complex from HuSP by utilizing 2-DE followed by MS. Twenty-six proteins representing isoforms and/or fragments of 11 different proteins were found to be assembled in this complex. Prostate-specific antigen, zinc α2-glycoprotein, prostatic acid phosphatase, and prolactin inducible protein were the major proteins of this complex. Dynamic light scattering experiments revealed changes in aggregation pattern accompanied with deviation from physiological pH and in presence of SDS. However, no significant changes were observed in the presence of physiological ligands such as zinc and fructose. The present study will be useful and contribute to guide the future studies performed for elucidation of biological significance of this native complex in HuSP.

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“…The existence of integrins and matrix proteins on human spermatozoa was previously demonstrated by flow cytometry (Glander & Schaller, 1992, 1993a. Studies on localization of cell adhesion molecules on spermatozoa by using fluorescence microscopy exist only for fibronectin and vitronectin (Vuento et al, 1984;Glander et al, 1987).…”

Section: Discussionmentioning

confidence: 99%

“…The matrix proteins fibronectin and laminin as well as a3, a4, a5, a6 chains of pl integrins and inconstantly pl chain and LFA-3 could be detected on human spermatozoa by flow cytometry (Fusi et al, 1992;Glander & Schaller, 1992, 1993a. Fibronectin had also been detected by fluorescence microscopy as having an equatorial expression pattern on spermatozoa membrane (Vuento et al, 1984;Glander et al, 1987).…”

Section: Introductionmentioning

confidence: 99%

Localization of adhesion molecules on human spermatozoa by fluorescence microscopy

Trübner

Glander

Schaller³

2009

Andrologia

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The expression of adhesion molecules on human spermatozoa of healthy probands was analysed. The localization patterns of adhesion molecules (AM) on the spermatozoal surface were documented by fluorescence microscopy. Spermatozoa were incubated with antibodies against a1 (CD49a), a2 (CD49b), a 3 (CD49c), a4 (CD49d), a5 (CD49e), a6 (CD49f) chains of pl integrins, 81 (CD29), p2 (CD18), aV (CD51), p3 (CD61) and p4 integrin chains, the LFA-3 (Lymphocyte function antigen, CD58) from the immunoglobulin superfamily and the extracellular matrix proteins laminin, fibronectin and collagen IV. For collagen IV, a1 and a2 chains no expression could be noticed. Laminin was detected at the acrosomal membrane, fibronectin and p4 chain mainly at the equatorial membrane. The fibronectin receptors a3, a4 and a5 chains of the p 1 integrins were mainly located on acrosomal and equatorial membrane areas. Laminin receptor a6 chain was located postacrosomal and less frequently acrosomal. p2 chain and vitronectin receptors aV and p3 chains had a mainly postacrosomal localization pattern. LFA-3 was found constantly on postacrosomal membrane areas. Double staining technique was used to prove the simultaneous occurrence of fibronectin and its integrin receptors a3, a4 and a5 chains and of aV and p2 chains on spermatozoa. The localization patterns of integrins on double stained spermatozoa were similar to the patterns described for single stained spermatozoa. The localization of fibronectin appeared to be influenced by the presence of integrins: the typical equatorial fibronectin band disappeared in case of an equatorial localization of integrins.

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Characterization of Fibronectin on Human Spermatozoa

Cited by 34 publications

References 9 publications

Carbohydrates and fertilization in animals

Carbohydrates and fertilization in animals

Purification and characterization of a native zinc‐binding high molecular weight multiprotein complex from human seminal plasma

Localization of adhesion molecules on human spermatozoa by fluorescence microscopy

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