Bicarbonate Is Required for Migration of Sperm Epididymal Protein DE (CRISP-1) to the Equatorial Segment and Expression of Rat Sperm Fusion Ability1

Ros, Vanina Gabriela Da; Munuce, María José; Cohen, Débora J.; Marı́n-Briggiler, Clara I.; Busso, Dolores; Visconti, Pablo E.; Cuasnicú, Patricia S.

doi:10.1095/biolreprod.103.022822

Cited by 33 publications

(36 citation statements)

References 42 publications

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“…In the same way as the principal piece, the cytoskeleton associated with PM in the acrosomal region is mainly composed of spectrin/F-actin, but with the difference that it is remodeled during capacitation. During capacitation and AR, proteins associated with PM as well as with membrane lipids compartmentalize in the acrosome region; they are redistributed inside the acrosome or distribute towards the equatorial segment and postacrosomal region as well (Rochwerger & Cuasnicu 1992, Da Ros et al 2004, Selvaraj et al 2007, Tsai et al 2007, Pasten-Hidalgo et al 2008. These molecules in some way are maintained as compartmentalized in the acrosome before capacitation.…”

Section: Discussionmentioning

confidence: 99%

Calpain modulates capacitation and acrosome reaction through cleavage of the spectrin cytoskeleton

Bastián¹,

Roa-Espitia²,

Mújica³

et al. 2010

Reproduction

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Research on fertilization in mammalian species has revealed that Ca 2C is an important player in biochemical and physiological events enabling the sperm to penetrate the oocyte. Ca 2C is a signal transducer that particularly mediates capacitation and acrosome reaction (AR). Before becoming fertilization competent, sperm must experience several molecular, biochemical, and physiological changes where Ca 2C plays a pivotal role. Calpain-1 and calpain-2 are Ca 2C-dependent proteases widely studied in mammalian sperm; they have been involved in capacitation and AR but little is known about their mechanism. In this work, we establish the association of calpastatin with calpain-1 and the changes undergone by this complex during capacitation in guinea pig sperm. We found that calpain-1 is relocated and translocated from cytoplasm to plasma membrane (PM) during capacitation, where it could cleave spectrin, one of the proteins of the PM-associated cytoskeleton, and facilitates AR. The aforementioned results were dependent on the calpastatin phosphorylation and the presence of extracellular Ca 2C . Our findings underline the contribution of the sperm cytoskeleton in the regulation of both capacitation and AR. In addition, our findings also reveal one of the mechanisms by which calpain and calcium exert its function in sperm.

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Section: Discussionmentioning

confidence: 99%

Calpain modulates capacitation and acrosome reaction through cleavage of the spectrin cytoskeleton

Bastián¹,

Roa-Espitia²,

Mújica³

et al. 2010

Reproduction

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“…However, those results will be presented in another report. The distribution of sperm surface antigens during capacitation and acrosome reaction has been well documented for proteins such as IZUMO1 (Sosnik et al 2009), CRISP1 (Da Ros et al 2004), and PH20 (Myles & Primakoff 1984), these proteins migrate after capacitation changing their localization. In a previous work, we have also shown that ADAM15 migrate from acrosome to the post-acrosomal region of mouse sperm before acrosome reaction (Pasten-Hidalgo et al 2008).…”

Section: P<0002mentioning

confidence: 99%

ADAM15 participates in fertilization through a physical interaction with acrogranin

et al. 2014

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Mammalian fertilization is completed by direct interaction between sperm and egg. This process is primarily mediated by both adhesion and membrane-fusion proteins found on the gamete surface. ADAM1, 2, and 3 are members of the ADAMs protein family, and have been involved in sperm-egg binding. In this study, we demonstrate the proteolytic processing of ADAM15 during epididymal maturation of guinea pig spermatozoa to produce a mature form a size of 45 kDa. We find that the size of the mature ADAM15, 45 kDa, in cauda epididymal spermatozoa indicates that the pro-domain and metalloprotease domain are absent. In addition, using indirect immunofluorescence, ADAM15 was found throughout the acrosome, at the equatorial region and along the flagellum of guinea pig spermatozoa. After acrosome reaction, ADAM15 is lost from the acrosomal region and retained in the equatorial region and flagellum. In this study, we also report the first evidence of a complex between ADAM15 and acrogranin. By immunoprecipitation, we detected a protein band of 65 kDa which co-immunoprecipated together ADAM15. Analysis of the N-terminal sequence of this 65 kDa protein has revealed its identity as acrogranin. In addition, using cell-surface labeling, ADAM15 was found to be present on the cell surface. Assays of heterologous fertilization showed that the antibody against acrogranin inhibited the sperm-egg adhesion. Interestingly, ADAM15 and acrogranin were also found associated in two breast cancer cell lines. In conclusion, our results demonstrated that ADAM15 and acrogranin are present on and associated with the surface of guinea pig spermatozoa; besides both proteins may play a role during sperm-egg binding.

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“…One possibility is that these domains are important for cell-surface binding and localization so as to target ICR domain actions. Evidence for this capacity comes from the fact that Crisp 1 binds to the mouse sperm surface in the epididymis and remains bound to the sperm in the female tract (Cohen et al 2000 ;Da Ros et al 2004 ;Roberts et al 2002Roberts et al , 2008. Its localization on the sperm and its binding lifetime are dependent on its glycosylation state.…”

Section: The Future Of Crisp Protein Relationships In Reproductionmentioning

confidence: 99%

“…The "D" form inhibits premature acrosome reaction in the male tract, but once in the female tract appears to unbind from the sperm during capacitation (Roberts et al 2008 ;Nixon et al 2006 ). In contrast, the "E" form of Crisp 1, having a different glycosylation pattern, binds to sperm in the epididymis, but is not easily removed even in the female tract (Da Ros et al 2004 ;Roberts et al 2008 ); rather, it migrates to the equatorial region of the sperm where it is thought to take part in sperm binding at the egg plasma membrane (Cohen et al 2008(Cohen et al , 2011.…”

Section: The Future Of Crisp Protein Relationships In Reproductionmentioning

confidence: 99%

“…Earliest reports of sperm-associated Crisp proteins demonstrated that the rodent epididymis secretes Crisp 1, which binds to the post-acrosomal region of the sperm head (Cohen et al 2011 ). This protein has been shown to migrate to the equatorial region of rat sperm during capacitation and to possibly participate in sperm-egg fusion (Cohen et al 2000(Cohen et al , 2007(Cohen et al , 2008Da Ros et al 2004 ;Roberts et al 2006Roberts et al , 2007Roberts et al , 2008Ellerman et al 2006 ). Antibodies raised against the protein inhibit sperm-egg fusion, and the protein has been demonstrated to bind to the egg surface (Cohen et al 2007 ;Ellerman et al 2006 ).…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Allurin: Exploring the Activity of a Frog Sperm Chemoattractant in Mammals

Burnett

Sugiyama

Washburn

et al. 2014

Sexual Reproduction in Animals and Plants

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Allurin, a 21-kDa protein secreted by the oviduct of female Xenopus frogs, is incorporated into the jelly layers of eggs as they pass single fi le on their way to the uterus and subsequent spawning. Hydration of the egg jelly layers at spawning releases allurin as a chemoattractant that binds to the midpiece of Xenopus sperm in a dose-dependent manner. Gradients of allurin elicit directed swimming across a porous membrane in two-chamber assays and preferential, up-gradient swimming of sperm in video-microscopic assays. Allurin, purifi ed from X. laevis or produced in recombinant form, also elicits chemotaxis by mouse sperm in twochamber and video microscopic assays. Allurin binds to mouse sperm at the midpiece and head, a pattern also seen in frog sperm. Western blots suggest the presence of an allurin-like protein in the follicular fl uid of mice and humans and peptides that mimic subdomains within allurin elicit chemoattractive behavior in both mouse and human sperm. By sequence homology, allurin is a truncated member of the CysteineRIch Secretory Protein (CRISP) family whose members include Crisps 1, 2, and 4, which have been demonstrated to modulate mammalian sperm functions including Dedication This chapter is dedicated to Allan L. Bieber, a long-time collaborator of ours who recently passed on. Allan was an expert biochemist who guided our purifi cation of allurin and characterization of its disulfi de bonding pattern using mass spectrometry. His long-term interest in venom proteins from snakes was culminated by his delight in fi nding that allurin is closely related to Crisp snake toxin proteins.

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Bicarbonate Is Required for Migration of Sperm Epididymal Protein DE (CRISP-1) to the Equatorial Segment and Expression of Rat Sperm Fusion Ability1

Cited by 33 publications

References 42 publications

Calpain modulates capacitation and acrosome reaction through cleavage of the spectrin cytoskeleton

Calpain modulates capacitation and acrosome reaction through cleavage of the spectrin cytoskeleton

ADAM15 participates in fertilization through a physical interaction with acrogranin

Allurin: Exploring the Activity of a Frog Sperm Chemoattractant in Mammals

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