Acrosome Reaction of Mouse Epididymal Sperm on Oocyte Zona Pellucida

Yamashita, Misuzu; Yamagata, Kazuya; Tsumura, Keiko; Nakanishi, Teruyuki; Baba, Tadashi

doi:10.1262/jrd.18145

Cited by 18 publications

(26 citation statements)

References 28 publications

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“…In contrast, regardless of whether or not AR-sperm were permeabilized, TMEM190 seemed to partly relocate during the acrosome reaction from the inner-acrosomal membrane onto the equatorial segment surface. Interestingly, this relocation pattern was similar to that of mouse IZUMO1 (Kawai et al 1989, Yamashita et al 2007, Fujihara et al 2010, an essential protein for sperm-oocyte fusion (Inoue et al 2005).…”

Section: Mouse Sperm Tmem190supporting

confidence: 53%

“…One highly suggestive clue is that TMEM190 co-localizes with IZUMO1 (Kawai et al 1989, Yamashita et al 2007, Fujihara et al 2010, which is an essential protein for sperm-oocyte fusion (Inoue et al 2005). The relocation of both TMEM190 and IZUMO1 during the acrosome reaction is intriguing, since the final destination of these two proteins is the equatorial segment, where the gamete fusion occurs (Yanagimachi 1994).…”

Section: Mouse Sperm Tmem190mentioning

confidence: 99%

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Characterization of mouse sperm TMEM190, a small transmembrane protein with the trefoil domain: evidence for co-localization with IZUMO1 and complex formation with other sperm proteins

Nishimura¹,

Gupta²,

Myles³

et al. 2011

Reproduction

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TMEM190, a small transmembrane protein containing the trefoil domain, was previously identified by our proteomic analysis of mouse sperm. Two structural features of TMEM190, 'trefoil domain' and 'small transmembrane protein', led us to hypothesize that this protein forms a protein-protein complex required during fertilization, and we characterized TMEM190 by biochemical, cytological, and genetic approaches. We showed in this study that the mouse Tmem190 gene exhibits testis-specific mRNA expression and that the encoded RNA is translated into a 19-kDa protein found in both testicular germ cells and cauda epididymal sperm. Treatment of the cell surface with proteinase K, subcellular fractionation, and immunofluorescence assay all revealed that mouse TMEM190 is an inner-acrosomal membrane protein of cauda epididymal sperm. During the acrosome reaction, TMEM190 partly relocated onto the surface of the equatorial segment, on which sperm-oocyte fusion occurs. Moreover, TMEM190 and IZUMO1, which is an immunoglobulin-like protein required for gamete fusion, co-localized in mouse sperm both before and after the acrosome reaction. However, immunoprecipitates of TMEM190 contained several sperm proteins, but did not include IZUMO1. These findings suggest that a mouse sperm protein complex(es) including TMEM190 plays an indirect role(s) in sperm-oocyte fusion. The role(s), if any, is probably dispensable since Tmem190-null male mice were normally fertile.

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Section: Mouse Sperm Tmem190supporting

confidence: 53%

Section: Mouse Sperm Tmem190mentioning

confidence: 99%

Characterization of mouse sperm TMEM190, a small transmembrane protein with the trefoil domain: evidence for co-localization with IZUMO1 and complex formation with other sperm proteins

Nishimura¹,

Gupta²,

Myles³

et al. 2011

Reproduction

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“…The use of acrosomally targeted GFP as a reporter of membrane integrity was a major advance but our results indicate that acrosomal matrix proteins can be exposed in individual sperm without the complete or immediate loss of the GFP (Kim and Gerton, 2003). More recently, immunodetection of the exposure of the inner acrosomal membrane protein IZUMO1 has been used as another approach to assess acrosomal status (Yamashita et al, 2007). The main point to keep in mind is that it is difficult to compare studies that have not used the same method for assessing acrosomal integrity.…”

Section: Acrosome Transitions and Differential Release Of Acrosomal Pmentioning

confidence: 99%

The role of the acrosomal matrix in fertilization

Buffone

Foster²,

Gerton³

2008

Int. J. Dev. Biol.

112

107

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Mammalian sperm must have properly formed acrosomes to be fully functional in the process of binding and penetrating the zona pellucida (ZP), the extracellular matrix surrounding the egg. There is much evidence to raise doubts about the old "bag of enzymes" paradigm of acrosomal function, although this is the model that seems to prevail. We concur with other scientists that acrosomal exocytosis is not an all or none event where the acrosome is either "intact" or "reacted". As determined by transmission electron microscopy of human sperm undergoing acrosomal exocytosis, six stages can be identified, with the intermediate ones involving loss of acrosomal matrix material. In the mouse, there is a temporal relationship among four stages of acrosomal exocytosis. Numerous evidences suggest a more complex role for the acrosome in fertilization in which the acrosomal matrix is a scaffold for sperm-ZP interactions that self-regulates by a controlled disassembly mechanism.

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“…2 panel A). Acrosomal contents include a variety of proteases that can digest zona pellucida proteins after exocytosis [23,24], and the predominant enzyme is acrosin [25]. Indeed, some major sperm proteins were digested by APMSF-sensitive proteases during freezing-rapid thawing (Fig.…”

Section: Mechanism For Increase Of Tyrp32mentioning

confidence: 99%

A 32-kDa Tyrosine-phosphorylated Protein Shows a Protease-dependent Increase in Dead Boar Spermatozoa

Tabuchi

Shidara

Harayama

2008

Journal of Reproduction and Development

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Abstract. Boar sperm TyrP32 is a 32-kDa tyrosine-phosphorylated protein that increases during the capacitation and acrosome reaction and during cryocapacitation. However, it is still unclear whether the increase in TyrP32 is an event that is limited to the process of sperm fertilization, including cryocapacitation. The aims of the present study were to demonstrate that TyrP32 is increased in dead spermatozoa after freeze-thawing without a cryoprotectant and to find the causal factors for this increase. Washed spermatozoa were resuspended in a salt solution and then frozen. The frozen samples were rapidly thawed in a warm water bath and then used for sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis (PAGE)/Western blotting to detect TyrP32, SDS-PAGE/silver staining of sperm proteins and staining of acrosomal contents with fluorescein isothiocyanate (FITC)-conjugated peanut agglutinin (PNA). In the samples before freezing, TyrP32 was barely detectable, and the distribution of the acrosomal contents was normal in most spermatozoa. One cycle of freeze-thawing induced an increase in TyrP32, a decrease in major sperm proteins and disorder in the acrosomal contents. However, the addition of a protease inhibitor (APMSF, 1 mM) suppressed the increase in TyrP32 and the decrease in the major sperm proteins, although it did not have any influence on the disorder in the acrosomal contents. Additionally, the spermatozoa did not exhibit any flagellar movement after freeze-thawing, which showed that almost all of them were dead. These results indicate that TyrP32 can show a protease-dependent increase in dead spermatozoa after freeze-thawing without a cryoprotectant even though the dead spermatozoa do not undergo cryocapacitation. Key words: Acrosome, Boar, Peanut agglutinin (PNA), Protease, Sperm, Tyrosine (J. Reprod. Dev. 54: [502][503][504][505][506][507] 2008) n mammalian spermatozoa, a variety of tyrosine-phosphorylated proteins increase during incubation under capacitationsupporting conditions. These proteins have been considered to be involved in regulation of fertilization-related events [1,2]. It is generally believed that the increase in tyrosine-phosphorylated proteins results from activation of protein tyrosine kinases and inactivation of protein tyrosine phosphatases that are controlled by cyclic adenosine 3',5'-monophosphate (cAMP)/protein kinase A (PKA) signaling [1,[3][4][5]. However, a cAMP-dependent increase in 32-kDa tyrosine-phosphorylated protein (called TyrP32 or p32) in boar spermatozoa is exceptionally suppressed by inhibition of tyrosine phosphatases and barely affected by inhibition of protein tyrosine kinases [6]. This tyrosine-phosphorylated protein is primarily found as a capacitation-related protein [7][8][9] and has recently been identified as a (pro)acrosin-binding protein [10,11]. We have previously shown that the cAMP-dependent increase in TyrP32 is greater in samples containing many spermatozoa that undergo calcium-dependent changes in acrosomal morphology (acrosome reaction) ...

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Acrosome Reaction of Mouse Epididymal Sperm on Oocyte Zona Pellucida

Cited by 18 publications

References 28 publications

Characterization of mouse sperm TMEM190, a small transmembrane protein with the trefoil domain: evidence for co-localization with IZUMO1 and complex formation with other sperm proteins

Characterization of mouse sperm TMEM190, a small transmembrane protein with the trefoil domain: evidence for co-localization with IZUMO1 and complex formation with other sperm proteins

The role of the acrosomal matrix in fertilization

A 32-kDa Tyrosine-phosphorylated Protein Shows a Protease-dependent Increase in Dead Boar Spermatozoa

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