Proteasomes in human spermatozoa

Wojcik, Cezary; Benchaïb, Mehdi; Lornage, Jacqueline; Czyba, J. C.; Guérin, J. F.

doi:10.1046/j.1365-2605.2000.00223.x

Cited by 59 publications

(42 citation statements)

References 53 publications

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“…Although some discrepancies across species are reported, all studies report an implication of proteasome in events related to the acrosomal reaction (Morales et al 2003, Sutovsky et al 2004, Rawe et al 2008. Proteasomes have also been detected at the connecting piece between head and tail in bovine and human sperm (Wojcik et al 2000, Rawe et al 2008. It has been suggested that they play different roles during the post-fertilisation disassembly of the sperm tail connecting piece, sperm aster formation, pronuclear development and apposition (Rawe et al 2008).…”

Section: Proteomic Comparison Of Sperm Proteins From Bullsmentioning

confidence: 99%

Proteomic comparison of detergent-extracted sperm proteins from bulls with different fertility indexes

D’Amours

Frenette²,

Fortier³

et al. 2010

Reproduction

145

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Intrinsic factors such as proteins modulate the fertilising ability of male gametes. We compared detergent-extracted sperm protein composition of bulls with different fertility indexes in order to highlight putative fertility markers of sperm. Frozen semen from 23 Holstein bulls with documented fertility was used. According to their 'fertility solution' (SOL), as calculated by the Canadian dairy network, bulls were divided into four groups: high fertility (HF) (SOLO3.0; nZ6), medium-HF (2.9OSOLO2.0; nZ5), medium-low fertility (K2.8OSOLOK4.9; nZ8) and low fertility (LF; SOL!K5.0; nZ4), with a SOLZ0 being the average. Triton X-100 protein extracts from ejaculated spermatozoa were subjected to two-dimensional difference gel electrophoresis, and polypeptide maps were quantitatively analysed by ImageMaster software. Nine protein spots showed significant differences between the HF and LF groups, and eight of these proteins were identified by liquid chromatography-tandem mass spectrometry. T-complex protein 1 subunits 3 and q (CCT5 and CCT8), two isoforms of epididymal sperm-binding protein E12 (ELSPBP1), proteasome subunit a type-6 and binder of sperm 1 (BSP1) were more expressed in the LF group than in the HF group. On the other hand, adenylate kinase isoenzyme 1 (AK1) and phosphatidylethanolamine-binding protein 1 (PEBP1) were more expressed in the HF group than in the LF group. The presence and expression level of ELSPBP1, BSP1, AK1 and PEBP1 were confirmed by western blot. A linear regression model established that CCT5 and AK1 explained 64% (P!0.001) of the fertility scores. The reported functions of these proteins are in agreement with a putative involvement in defective sperm physiology, where lower or higher levels can jeopardise sperm ability to reach and fertilise the oocyte.

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Section: Proteomic Comparison Of Sperm Proteins From Bullsmentioning

confidence: 99%

Proteomic comparison of detergent-extracted sperm proteins from bulls with different fertility indexes

D’Amours

Frenette²,

Fortier³

et al. 2010

Reproduction

145

View full text Add to dashboard Cite

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“…data). Proteasomal subunits were also detected inside or near the sperm centriole (Bialy et al, 2001;Mochida et al, 2000;Wojcik et al, 2000). These could be either an inactive carryover of dismantled proteasomes and ubiquitinated centrosomal proteins or a part of the proteolytic apparatus that could be activated and instrumental in the release of the sperm centriole at fertilization.…”

Section: Ubiquitin In Spermatogenesismentioning

confidence: 99%

“…Ubiquitin (Fig. 1L) and the 26 S proteasomal-subunits localize to the centriolar region of the sperm tail (Wojcik et al, 2000) and to the other parts of the sperm tail midpiece (Mochida et al, 2000), and may be instrumental in this process. Fol- lowing the sperm aster formation, S-phase, and pronuclear apposition, the first embryonic mitosis is controlled by the ubiquitin-dependent degradation of cyclin B, a recurring component of the maturation promoting factor (Josefsberg et al, 2001).…”

Section: Fertilization Mitochondrial Inheritance and Early Embryonimentioning

confidence: 99%

“…Further work shows that proteasomal inhibitors, small peptides binding to proteasome's catalytic subunit, block fertilization not only in ascidians (Sawada et al, 2002b) and sea urchins (Matsumara and Aketa, 1991), but also in mouse (Wang et al, 2002) and pig, where ubiquitin-cross-reactive substrates can be detected on the outer face of the zona pelluciada in both follicular and ovulated oocytes (Sutovsky, McCauley, and Day, in prep.). Proteasomal subunits were detected in the human (Bialy et al, 2001;Wojcik et al, 2000), ascidian (Sawada et al, 2002b), pig (Sutovsky, McCauley, and Day, in prep. ), and sea urchin (Matsumara and Aketa, 1991) sperm.…”

Section: Fertilization Mitochondrial Inheritance and Early Embryonimentioning

confidence: 99%

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Ubiquitin‐dependent proteolysis in mammalian spermatogenesis, fertilization, and sperm quality control: Killing three birds with one stone

Šutovský

2003

Microscopy Res & Technique

254

181

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Ubiquitin and ubiquitin-like proteins control the degradation of substrates as diverse as cyclins, viral envelope proteins, plasma membrane receptors, and mRNAs. The ubiquitinated substrates are targeted towards the lysosomal or proteasomal degradation sites. The number and position of ubiquitin molecules bound to substrates' lysine residues and the number and position of ubiquitin molecules in polyubiquitin chains determine the astonishing substrate specificity of ubiquitin-mediated proteolysis. Ubiquitin is likely to be expressed in mammalian gametes and embryos at any given developmental step, but the information on ubiquitin dependence of gametogenesis and fertilization is sketchy. Ubiquitin ligases E1, E2, E3, and UBC4 are active in the testis. Ubiquitin and proteasomal subunits can be detected in the human sperm centrosome that undergoes dramatic reduction during spermatid elongation. Spermatid histones are ubiquitinated as they are being transiently replaced by transitional proteins and permanently by protamines. Ubiquitin tagging of the sperm mitochondrial membranes may serve as a death sentence for paternal mitochondria at fertilization, thus promoting the maternal inheritance of mitochondrial DNA (mtDNA) in mammals. The defective spermatozoa become surface-ubiquitinated during sperm descent down the epididymis. Finally, new evidence suggests the involvement of ubiquitin-proteasome pathway in the zona penetration by the acrosome-reacted spermatozoon. Such differential patterns of ubiquitination in the testis and epididymis, and inside the egg, may be necessary for reproductive success in humans and animals. Deciphering and eventually manipulating the ubiquitin-dependent proteolysis in the reproductive system could allow us to redirect the mode of mtDNA inheritance after cloning and ooplasmic transplantation, provide germ line therapy in some cases of male infertility, develop new contraceptives, manage polyspermia during in vitro fertilization, and establish objective markers for infertility diagnostics, semen evaluation, and prediction of future fertility.

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“…Sawada et al (1998) and(2002) proposed that the main component of the vitelline coat that exhibits sperm receptors was in fact multiubiquitinated and then degraded by the sperm ubiquitin-proteasome pathway during ascidian fertilization. Interestingly, multiple proteasomal subunits have been detected in the sperm acrosomes of various mammalian species including human, boar, bull, rat and mouse spermatozoa (Baker et al 2008a, b;Baska et al 2008;Biały et al 2001;Morales et al 2003Morales et al , 2004Sutovsky et al 2004;Wojcik et al 2000;Ziemba et al 2002). Additionally, multiple ubiquitin-specific proteases (Baker et al 2008a, b) and the ubiquitin conjugating enzyme E2 (Fischer et al 2005;Sutovsky et al 2000) have also been identified in the proteomes of mammalian spermatozoa.…”

Section: Proteasomes In Sperm-oocyte Interactionsmentioning

confidence: 99%

Proteasomal degradation of ubiquitinated proteins in oocyte meiosis and fertilization in mammals

2011

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Gametogenesis and fertilization are the key events in sexual reproduction. In the female, meiosis results in a large oocyte that is competent for fertilization and fundamental for the success of early embryonic development. Progression through meiosis is monitored by fine regulatory mechanisms. In this review, we focus on one of the most well-known regulatory elements, the E3 ligase APC/C, which mediates proteolytic degradation of a number of important substrates via the ubiquitin proteasome pathway (UPP). The UPP also indirectly regulates protein synthesis by affecting proteins involved in RNA metabolism, a process that is paramount for the transcriptionally silent oocyte. During the past few years, more evidence has accumulated to suggest that the UPP has an important role in zona pellucida penetration and gamete fusion in mammals. This review focuses on the function of the UPP in regulating oocyte meiotic maturation in mammals, with special attention to its role in chromosome segregation and polar body extrusion, its role in the acquisition of meiotic/developmental competence and recent advances in our understanding of the UPP role in fertilization.

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Proteasomes in human spermatozoa

Cited by 59 publications

References 53 publications

Proteomic comparison of detergent-extracted sperm proteins from bulls with different fertility indexes

Proteomic comparison of detergent-extracted sperm proteins from bulls with different fertility indexes

Ubiquitin‐dependent proteolysis in mammalian spermatogenesis, fertilization, and sperm quality control: Killing three birds with one stone

Proteasomal degradation of ubiquitinated proteins in oocyte meiosis and fertilization in mammals

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