Comparative distribution of short dystrophin superfamily products in various guinea pig spermatozoa domains

Hernández‐González, Enrique O.; Martínez-Rojas, Dalila; Mornet, Dominique; Rendón, Álvaro; Mújica, Adela

doi:10.1078/0171-9335-00202

Cited by 11 publications

(16 citation statements)

References 32 publications

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“…Different and important membrane domains are established in both the acrosome and flagella of mammalian sperm, which display distinct biochemical and physiological functions; however, little is known Calpain cleaves spectrin during capacitation about the role of the cytoskeleton in the establishment of these membrane domains. Our findings showing the localization of spectrin indicate that it could constitute and stabilize such domains, and also suggest that considering the cytoskeletal proteins associated with PM, flagella is formed by two different membrane subdomains: the middle piece, whose membrane cytoskeleton is mainly conformed by the short dystrophin Dp71/F-actin (Hernandez-Gonzalez et al 2001), and the principal piece, whose membrane cytoskeleton is mainly conformed by spectrin/F-actin. In particular, these cytoskeletons do not undergo changes during capacitation or AR.…”

Section: Discussionmentioning

confidence: 99%

“…Diverse cytoskeletal proteins have been found to be associated with these membrane domains, for instance F-actin (Castellani-Ceresa et al 1992, Moreno-Fierros et al 1992, Kann et al 1993, Spungin et al 1995, Yagi & Paranko 1995, spectrin (Virtanen et al 1984, Camatini et al 1991, HernandezGonzalez et al 2000, as well as dystrophin and utrophin (Hernandez-Gonzalez et al 2001. Interestingly, because F-actin and spectrin form a network associated with the plasma and outer acrosomal membranes (Hernandez-Gonzalez et al 2000) that may act as a physical barrier preventing membrane fusion (Spungin et al 1995, Hernandez-Gonzalez et al 2000, remodeling of the cortical actin cytoskeleton could facilitate capacitation and AR (Brener et al 2003, Cabello-Agueros et al 2003.…”

Section: Introductionmentioning

confidence: 99%

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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%

Section: Introductionmentioning

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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confidence: 99%

“…1). Some proteins containing the PDZ ligand domain have been found in mammalian spermatozoa such as: K + channels (Félix et al, 2002), Ca 2+ channels (Darszon et al, 1999), aquaporin-7 and -8 (Calamita et al, 2001) and neural nitric oxide synthase (nNOS) (Hernández-González et al, 2001) (Fig. 1).…”

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confidence: 99%

“…Dp71 and DAPs are also expressed in non-muscular tissues including the central nervous system (Dalloz et al, 2001), kidney, liver (Loh et al, 2001) and spermatozoa (Hernández-González et al, 2001). Dp71 isoforms and DAPs are localized in specific domains of mammalian spermatozoa and, interestingly, they only express a product of the DMD gene (Hernández-González et al, 2001). Protein components of the DAPC show different localizations in mammalian spermatozoa, α-syntrophin was located in the middle piece of both plasma membrane and flagellum, whereas β-dystroglycan was only located in the plasma membrane of the flagellar middle piece (Hernández-González et al, 2001).…”

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Absence of Dp71 in mdx3cv mouse spermatozoa alters flagellar morphology and the distribution of ion channels and nNOS

Hernández‐González

Mornet

Rendón

et al. 2005

Journal of Cell Science

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In muscle, the absence of dystrophin alters the dystrophin-associated protein complex (DAPC), which is involved in the clustering and anchoring of signaling proteins and ion and water channels. Here we show that mice spermatozoa express only dystrophin Dp71 and utrophin Up71. The purpose of this study was to explore the effect of the absence of Dp71 on the morphology and membrane distribution of members of the DAPC, ion channels and signaling proteins of spermatozoa obtained from dystrophic mutant mdx3cv mice. Our work indicates that although the absence of Dp71 results in a dramatic decrease in β-dystroglycan, it induces membrane redistribution and an increase in the total level of α-syntrophin, voltage-dependent Na+ (μ1) and K+ (Kv1.1) channels and neural nitric oxide synthase (nNOS). The short utrophin (Up71) was upregulated and redistributed in the spermatozoa of mdx3cv mice. A significant increase in abnormal flagella morphology was observed in the absence of Dp71, which was partially corrected when the plasma membrane was eliminated by detergent treatment. Our observations point to a new phenotype associated with the absence of Dp71. Abnormal flagellar structure and altered distribution of ion channels and signaling proteins may be responsible for the fertility problems of mdx3cv mice.

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Perinuclear theca during spermatozoa maturation leading to fertilization

Mújica

Hernández‐González

Juárez-Mosqueda

2003

Microscopy Res & Technique

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Mammalian spermatozoa acquire the capacity to fertilize the ovum and display motility during their passage through the epididymis. At the same time, they undergo changes in metabolic patterns, enzymatic activities, ability to bind to zona pellucida surface, and electrophoretic properties and, furthermore, stabilization of some sperm structures by the establishment of disulphide linkages takes place in several sperm structures. The cytoplasmic perinuclear theca (PT) is a unique extranuclear cytoskeletal element that surrounds the nucleus, which is proposed to be a structural scaffold to the sperm nucleus. The purpose of this review is to describe PT changes related to epididymal sperm maturation. We will focus mainly on the protein components of the PT of eutherian mammalian spermatozoa and on quantitative protein changes during sperm maturation. The protein constituents of the PT have not been completely defined and most of them are different from the cytoskeletal proteins of somatic cells. However, they are proteins with cytoskeletal features. The morphologic changes reported for PT and the proposed functions of PT are discussed.

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Comparative distribution of short dystrophin superfamily products in various guinea pig spermatozoa domains

Cited by 11 publications

References 32 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

Absence of Dp71 in mdx3cv mouse spermatozoa alters flagellar morphology and the distribution of ion channels and nNOS

Perinuclear theca during spermatozoa maturation leading to fertilization

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