Effect of fibronectin on proteasome activity, acrosome reaction, tyrosine phosphorylation and intracellular calcium concentrations of human sperm

Díaz, Emilce S.; Kong, Milene; Morales, Patricio

doi:10.1093/humrep/dem023

Cited by 47 publications

(57 citation statements)

References 69 publications

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“…Molecules on the sperm cell surface required for sperm-ZP binding might be sterically hindered by the glycoprotein sticking to the corresponding integrin receptor. Unlike in human (Diaz et al 2007) and pig (Mattioli et al 1998), incubation of bovine sperm with Fn did not seem to induce important levels of premature acrosome reaction, which could also have been a plausible explanation for a decrease in sperm-ZP binding. Combining all these results, it is very likely that Fn is not essential for successful sperm-ZP interaction in bovine.…”

Section: Discussionmentioning

confidence: 79%

See 1 more Smart Citation

Expression and putative function of fibronectin and its receptor (integrin α5β1) in male and female gametes during bovine fertilization in vitro

Thys¹,

Nauwynck²,

Maes³

et al. 2009

Reproduction

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Fibronectin (Fn) is a 440 kDa glycoprotein assumed to participate in sperm-egg interaction in human. Recently, it has been demonstrated that Fn -when present during bovine IVF -strongly inhibits sperm penetration. The present study was conducted firstly to evaluate the expression of Fn and its integrin receptor (a 5 b 1 ) on male and female bovine gametes using indirect immunofluorescence and secondly, to determine the function of Fn during bovine IVF. Endogenous Fn was detected underneath the zona pellucida (ZP) and integrin a 5 on the oolemma of cumulus-denuded oocytes. Bovine spermatozoa displayed integrin a 5 at their equatorial segment after acrosome reaction. We established that the main inhibitory effect of exogenously supplemented Fn was located at the sperm-oolemma binding, with a (concurrent) effect on fusion, and this can probably be attributed to the binding of Fn to spermatozoa at the equatorial segment, as shown by means of Alexa Fluor 488-conjugated Fn. Combining these results, the inhibitory effect of exogenously supplemented Fn seemed to be exerted on the male gamete by binding to the exposed integrin a 5 b 1 receptor after acrosome reaction. The presence of endogenous Fn underneath the ZP together with integrin a 5 expression on oolemma and acrosome-reacted (AR) sperm cell surface suggests a 'velcro' interaction between the endogenous Fn ligand and corresponding receptors on both (AR) sperm cell and oolemma, initiating sperm-egg binding.

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Section: Discussionmentioning

confidence: 79%

“…One of the final hurdles is the extracellular cumulus matrix surrounding the mammalian oocyte. This matrix is -like other extracellular matrices -composed of a variety of molecules among which adhesive glycoproteins such as laminin, fibronectin (Fn), and collagen type IV (Diaz et al 2007).…”

Section: Introductionmentioning

confidence: 99%

Expression and putative function of fibronectin and its receptor (integrin α5β1) in male and female gametes during bovine fertilization in vitro

Thys¹,

Nauwynck²,

Maes³

et al. 2009

Reproduction

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show abstract

“…Proteasome-specific proteolytic and deubiquitinating activities have been measured in live, intact spermatozoa by using specific fluorometric substrates (5,15). Fertilization has been shown to rely on proteasomal proteolysis by the application of a variety of proteasomespecific inhibitors and antibodies (7,12,(16)(17)(18). Phosphoproteome studies detected many UPS proteins undergoing phosphorylation during sperm capacitation and acrosome reaction in the mouse, boar, and rat (2,19,20).…”

mentioning

confidence: 99%

Transgenic pig carrying green fluorescent proteasomes

Miles

O’Gorman

Zhao

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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Among its many functions, the ubiquitin-proteasome system regulates substrate-specific proteolysis during the cell cycle, apoptosis, and fertilization and in pathologies such as Alzheimer's disease, cancer, and liver cirrhosis. Proteasomes are present in human and boar spermatozoa, but little is known about the interactions of proteasomal subunits with other sperm proteins or structures. We have created a transgenic boar with green fluorescent protein (GFP) tagged 20S proteasomal core subunit α-type 1 (PSMA1-GFP), hypothesizing that the PSMA1-GFP fusion protein will be incorporated into functional sperm proteasomes. Using direct epifluorescence imaging and indirect immunofluorescence detection, we have confirmed the presence of PSMA1-GFP in the sperm acrosome. Western blotting revealed a protein band corresponding to the predicted mass of PSMA1-GFP fusion protein (57 kDa) in transgenic spermatozoa. Transgenic boar fertility was confirmed by in vitro fertilization, resulting in transgenic blastocysts, and by mating, resulting in healthy transgenic offspring. Immunoprecipitation and proteomic analysis revealed that PSMA1-GFP copurifies with several acrosomal membrane-associated proteins (e.g., lactadherin/milk fat globule E8 and spermadhesin alanine-tryptophan-asparagine). The interaction of MFGE8 with PSMA1-GFP was confirmed through cross-immunoprecipitation. The identified proteasome-interacting proteins may regulate sperm proteasomal activity during fertilization or may be the substrates of proteasomal proteolysis during fertilization. Proteomic analysis also confirmed the interaction/coimmunoprecipitation of PSMA1-GFP with 13/14 proteasomal core subunits. These results demonstrate that the PSMA1-GFP was incorporated in the assembled sperm proteasomes. This mammal carrying green fluorescent proteasomes will be useful for studies of fertilization and wherever the ubiquitin-proteasome system plays a role in cellular function or pathology.

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“…Aitken et al theorize that this is caused by posttranslational modifi cations of certain subunits of the complex (α1-7, β1, and β4) that displayed charge shift signatures characteristic of tyrosine phosphorylation (Redgrove et al 2011 ). This fi nding is consistent with the proteasomal subunit phosphorylation reported in the acrosome that, according to Diaz et al, modulates the fertilizing capacity of human spermatozoa by inducing AE (Diaz et al 2007 ), suggesting that proteasome complexes may be differentially activated during the individual steps of fertilization.…”

Section: Proteasome Localization and Activity In Mammalian Spermatozoamentioning

confidence: 70%

Sperm Proteasome as a Putative Egg Coat Lysin in Mammals

Miles

Šutovský

2014

Sexual Reproduction in Animals and Plants

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During animal and human fertilization, the fertilizing spermatozoon creates and passes through a fertilization slit in the vitelline coat (VC) of the oocyte. It has been hypothesized that the penetration of the mammalian VC, the zona pellucida (ZP), is aided by a proteolytic enzyme capable of locally degrading ZP proteins. This putative "zona lysin" is predicted to reside within the sperm head acrosome and be released or exposed by ZP-induced acrosomal exocytosis. Evidence has been accumulating in favor of the 26S proteasome, the ubiquitin-dependent multi-subunit protease acting as the putative vitelline coat/zona lysin in humans and animals. To confi rm this hypothesis, three criteria must be met: (1) the sperm receptor on the ZP must be ubiquitinated, (2) proteasomes must be present, exposed, and enzymatically active in the sperm acrosome, and (3) sperm proteasomes must be able to degrade the sperm receptor on the egg coat/ZP during fertilization. This review discusses recent data from a number of mammalian and nonmammalian models addressing these predictions. These data shed light on the mechanisms controlling sperm interactions with VC and on the evolutionary conservation of the proteasome-assisted fertilization mechanisms.

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Effect of fibronectin on proteasome activity, acrosome reaction, tyrosine phosphorylation and intracellular calcium concentrations of human sperm

Abstract: These results suggest that Fn activates the proteasome and induces the acrosome reaction in human sperm. This effect may involve binding with specific receptors (integrins) on the sperm surface and the activation of tyrosine kinases.

Cited by 47 publications

References 69 publications

Expression and putative function of fibronectin and its receptor (integrin α5β1) in male and female gametes during bovine fertilization in vitro

Expression and putative function of fibronectin and its receptor (integrin α5β1) in male and female gametes during bovine fertilization in vitro

Transgenic pig carrying green fluorescent proteasomes

Sperm Proteasome as a Putative Egg Coat Lysin in Mammals

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