Isolation and Proteomic Characterization of the Mouse Sperm Acrosomal Matrix

Guyonnet, Benoît; Zabet-Moghaddam, Masoud; SanFrancisco, Susan

doi:10.1074/mcp.a112.020339

Cited by 11 publications

(16 citation statements)

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“…The acrosomal matrix was eventually described in spermatozoa of all species examined, including hamster (review by Olson et al 1998), guinea pig (reviewed by Westbrook-Case et al 1994;Buffone et al 2008;Kim et al 2011), mouse (Buffone et al 2009a) and confirmed in bovine (epididymal) spermatozoa (NagDas et al 2010). With mass spectrometry and proteomic techniques, it is now possible to identify an unexpected diversity of acrosomal proteins, although their precise location and roles may remain unknown (Byrne et al 2012;Guyonnet et al 2012). It was suggested that the acrosomal matrix includes several cytoskeletal components (review and own results by Zepeda-Bastida et al 2011), although it is unusual for, e.g., F-actin to be located inside a secretory vesicle.…”

Section: Acrosomal Exocytosismentioning

confidence: 97%

The acrosome of eutherian mammals

Fléchon

2015

Cell Tissue Res

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The acrosome is not just a bag of enzymes, most of which, if not all, are singly non-essential for sperm-oocyte interaction. The Golgi-derived acrosomal cap reveals some extraordinary development and structure particularities. The acrosome of eutherian spermatozoa basically consists of two parts, the anterior and equatorial segments; the present review is devoted to the former, the initial actor in fertilization. Its occasional fanciful morphological changes during epididymal maturation are analyzed, together with its heterogeneous contents: enzymes, zona binding proteins, structural proteins (matrix) and yet to be chemically characterized crystalloids. The plasma and acrosomal membranes present stabilized ordered domains, whereas glycoprotein-free areas appear during capacitation and before fusion. Exocytosis, induced by the cumulus oophorus and/or the zona pellucida, may generally start proximally and progress anteriorly, resulting in the detachment of a hybrid membrane shroud, whose entity is probably maintained by the bound matrix. Immediately released soluble enzymes must be active during the first interactions of the gametes, whereas other lysins, bound to the matrix or stored as proenzymes, are only progressively released. Zona binding is probably achieved via the shroud and/or the IAM (depending on species). Penetration along an incurved slit through the stratified zona is allowed by the rigid and denuded head tip and flagellar hyperactivity, and assisted by the local proteolytic activity of proteasomes bound to the IAM, the unique essential zona lysin system.

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Section: Acrosomal Exocytosismentioning

confidence: 97%

The acrosome of eutherian mammals

Fléchon

2015

Cell Tissue Res

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“…In addition to a lysosomal storage disease phenotype in the epididymis, CRES KO mice also exhibit reduced fertility in vitro as spermatozoa are unable to undergo a progesterone‐induced acrosome reaction (Chau & Cornwall, ). However, this phenotype is detected in both young and older mice and we believe it is a result of alterations in CRES‐containing amyloid structures in the mouse sperm acrosome rather than the epididymal luminal amyloid matrix (Guyonnet et al ., ).…”

Section: Alterations In the Epididymal Amyloid Matrix Are Associated mentioning

confidence: 97%

The epididymal amyloid matrix: structure and putative functions

et al. 2019

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Background: We previously demonstrated the normal mouse epididymal lumen contains a non-pathological amyloid matrix that surrounds spermatozoa and plays important roles in sperm maturation and protection. Objective: The objective herein was to present a review of this work, including studies showing the amyloid structures of four members of the CRES (cystatin-related epididymal spermatogenic) subgroup are integral and essential components of the amyloid matrix. Methods: We used conformation-dependent reagents that recognize the cross-b-sheet structure characteristic of amyloid, including thioflavin S (ThS), thioflavin T (ThT), anti-amyloid antibodies, and X-ray diffraction, as well as negative-stain transmission electron microscopy (TEM) to visualize amyloid structures in the epididymal lumen. Antibodies that specifically detect each CRES subgroup family member were also used in indirect immunofluorescence analysis. Results and Discussion: The epididymal lumen contains an amyloid matrix that surrounds maturing spermatozoa and represents a functional amyloid. Alterations in the structure of the amyloid matrix by the loss of the CRES subgroup members or the overexpression of cystatin C result in epididymal pathologies, including infertility. Preliminary data suggest the epididymal amyloid matrix is structurally and functionally similar to bacterial biofilms. Conclusion: Together, these results suggest the amyloid matrix serves important roles in epididymal function including sperm maturation and protection.

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“…The sperm proteomic study of different model organisms is also providing catalogues of the corresponding sperm proteins resulting in very valuable information relevant to understand the different functions of the sperm cell and the conserved key elements. Mammalian sperm proteomic profiles are now available for mouse (Baker et al ., ; Nixon et al ., ; Asano et al ., ; Dorus et al ., ; Chauvin et al ., ; Guyonnet et al ., ) (just to give some examples), rat (Baker et al ., ; Maselli et al ., ), bull (Peddinti et al ., ; Byrne et al ., ; Soggiu et al ., ), boar (Park et al ., ) and macaque (Skerget et al ., ). In addition, proteomic approaches have also been applied for the identification of sperm proteins in invertebrates and plants.…”

Section: Sperm Nuclear Proteome In Model Speciesmentioning

confidence: 99%

Sperm nuclear proteome and its epigenetic potential

2013

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SUMMARYThe main function of the sperm cell is to transmit the paternal genetic message and epigenetic information to the embryo. Importantly, the majority of the genes in the sperm chromatin are highly condensed by protamines, whereas genes potentially needed in the initial stages of development are associated with histones, representing a form of epigenetic marking. However, so far little attention has been devoted to other sperm chromatin-associated proteins that, in addition to histones and protamines, may also have an epigenetic role. Therefore, with the goal of contributing to cover this subject we have compiled, reviewed and report a list of 581 chromatin or nuclear proteins described in the human sperm cell. Furthermore, we have analysed their Gene Ontology Biological Process enriched terms and have grouped them into different functional categories. Remarkably, we show that 56% of the sperm nuclear proteins have a potential epigenetic activity, being involved in at least one of the following functions: chromosome organization, chromatin organization, protein-DNA complex assembly, DNA packaging, gene expression, transcription, chromatin modification and histone modification. In addition, we have also included and compared the sperm cell proteomes of different model species, demonstrating the existence of common trends in the chromatin composition in the mammalian mature male gamete. Taken together, our analyses suggest that the mammalian sperm cell delivers to the offspring a rich combination of histone variants, transcription factors, chromatin-associated and chromatin-modifying proteins which have the potential to encode and transmit an extremely complex epigenetic information.

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Isolation and Proteomic Characterization of the Mouse Sperm Acrosomal Matrix

Cited by 11 publications

References 0 publications

The acrosome of eutherian mammals

The acrosome of eutherian mammals

The epididymal amyloid matrix: structure and putative functions

Sperm nuclear proteome and its epigenetic potential

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