Participation of the Human Sperm Proteasome in the Capacitation Process and Its Regulation by Protein Kinase A and Tyrosine Kinase1

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

doi:10.1095/biolreprod.108.073924

Cited by 67 publications

(58 citation statements)

References 82 publications

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“…Sawada et al reported that in marine invertebrate such as ascidians and sea urchins, sperm proteasomes is responsible for sperm penetration of the vitelline envelope, and the proteasome is a lytic agent called lysin, which is essential for disintegration of the egg extracellular matrix (Sawada et al 2002a, Sakai et al 2003, Yokota & Sawada 2007a. A similar conclusion was drawn from mammalian fertilization, including that in mice, pigs, and man (Pasten et al 2005, Kong et al 2009, Zimmerman et al 2011.…”

Section: Introductionmentioning

confidence: 84%

Sperm proteasome degrades egg envelope glycoprotein ZP1 during fertilization of Japanese quail (Coturnix japonica)

Sasanami¹,

Sugiura²,

Tokumoto³

et al. 2012

Reproduction

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At the time of fertilization, the extracellular matrix surrounding avian oocytes, termed the perivitelline membrane (pvm), is hydrolyzed by a sperm-borne protease, although the actual protease that is responsible for the digestion of the pvm remains to be identified. Here, we show evidence that the ubiquitin-proteasome system is functional in the fertilization of Japanese quail. The activities for the induction of the acrosome reaction and binding to ZP3 as revealed by ligand blotting of purified serum ZP1 are similar to those of pvm ZP1. Western blot analysis of purified ZP1 and ZP3 by the use of the anti-ubiquitin antibody showed that only pvm ZP1 was reactive to the antibody. In vitro penetration assay of the sperm on the pvm indicated that fragments of ZP1 and intact ZP3 were released from the pvm. Western blot analysis using the anti-20S proteasome antibody and ultrastructural analysis showed that immunoreactive proteasome was localized in the acrosomal region of the sperm. Inclusion of specific proteasome inhibitor MG132 in the incubation mixture, or depletion of extracellular ATP by the addition of apyrase, efficiently suppressed the sperm perforation of the pvm. These results demonstrate for the first time that the sperm proteasome is important for fertilization in birds and that the extracellular ubiquitination of ZP1 might occur during its transport via blood circulation.

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Section: Introductionmentioning

confidence: 84%

Sperm proteasome degrades egg envelope glycoprotein ZP1 during fertilization of Japanese quail (Coturnix japonica)

Sasanami¹,

Sugiura²,

Tokumoto³

et al. 2012

Reproduction

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“…Proteasomal ubiquitin-dependent epididymal protein degradation is important for spermatogenesis [84], fertilization [85][86][87], and removal of DNA-damaged spermatozoa [88]. Furthermore, the response to unfolded proteins not only includes the protein refolding, a function conserved between the Low and High groups, but also the degradation of unfolded proteins by the ubiquitin system [89].…”

Section: Enriched Functions In the Low Sperm Dna Fragmentation Groupmentioning

confidence: 99%

Unraveling the sperm proteome and post-genomic pathways associated with sperm nuclear DNA fragmentation

Intasqui

Camargo

Giudice

et al. 2013

J Assist Reprod Genet

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Purpose Sperm DNA fragmentation has been suggested as a marker for infertility diagnosis and prognosis. Hence, understanding its impact on male physiology and post-genomic pathways would be clinically important. We performed the proteomics and functional enrichment analyses of viable spermatozoa from ejaculates with low and high sperm DNA fragmentation to identify protein expression and pathways altered in association with sperm DNA fragmentation. Methods Sperm DNA fragmentation using the Comet assay and the Komet 6.0.1 software was assessed in raw samples from 89 subjects from a human reproduction service. The Low and High sperm DNA fragmentation groups were formed according to the Olive Tail Moment variable. Spermatozoa proteins from these groups were pooled and analyzed by a shotgun proteomic approach (2D nanoUPLC-ESI-MS E ). Differentially expressed proteins were used for a functional enrichment study. Results Two hundred and fifty-seven proteins were identified or quantified in sperm from the Low and High sperm DNA fragmentation groups. Of these, seventy-one proteins were exclusively or overexpressed in the Low group, whereas twenty-three proteins were exclusively or overexpressed in the High group. One hundred and sixty-three proteins were conserved between these groups. We also functionally related the differentially expressed proteins in viable spermatozoa from the groups. Processes such as triacylglycerol metabolism, energy production, protein folding, response to unfolded proteins, and cellular detoxification were found to be altered in these cells. Conclusions Sperm DNA fragmentation is associated with differential protein expression in viable spermatozoa. These proteins may potentially be used as biomarkers for sperm DNA integrity.

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“…For example, multi-enzymatic sperm protease complexes with similar sedimentation coeffi cients as purifi ed proteasomes from other tissues have been isolated from mouse (Pasten et al 2005 ), pig (Zimmerman and Sutovsky 2009 ), and human (Morales et al 2003 ;Morales et al 2004 ;Baker et al 2007 ) spermatozoa. Accordingly, the substrate-specifi c enzymatic activities (trypsinlike, chymotrypsin-like, and peptidylglutamyl peptide-hydrolyzing activities) of these sperm proteasomes have been recorded in mice (Pasten et al 2005 ;Bedard et al 2011 ;Rivkin et al 2009 ), pigs (Sutovsky et al 2004 ;Yi et al 2007a ;Yi et al 2009 ), and humans (Morales et al 2003;Chakravarty et al 2008 ;Kong et al 2009 ).…”

Section: Proteasome Localization and Activity In Mammalian Spermatozoamentioning

confidence: 99%

“…Then, the intracellular and extracellular proteasomes would blend into the acrosomal shroud and participate during the AE. Sperm proteasomes have been shown to be essential for acrosomal function and sperm-zona penetration during fertilization in several mammalian species such as mouse, pig, and human (Pasten et al 2005 ;Kong et al 2009 ;Zimmerman et al 2011 ). It is possible that the proteasomes modulating these cellular events could participate in other steps of fertilization as well.…”

Section: Proteasome Localization and Activity In Mammalian Spermatozoamentioning

confidence: 99%

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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Participation of the Human Sperm Proteasome in the Capacitation Process and Its Regulation by Protein Kinase A and Tyrosine Kinase1

Cited by 67 publications

References 82 publications

Sperm proteasome degrades egg envelope glycoprotein ZP1 during fertilization of Japanese quail (Coturnix japonica)

Sperm proteasome degrades egg envelope glycoprotein ZP1 during fertilization of Japanese quail (Coturnix japonica)

Unraveling the sperm proteome and post-genomic pathways associated with sperm nuclear DNA fragmentation

Sperm Proteasome as a Putative Egg Coat Lysin in Mammals

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