Function of the Egg's Extracellular Matrix

Cardullo, Richard A.; Thaler, Catherine D.

doi:10.1016/b978-012311629-1/50006-1

Cited by 5 publications

(7 citation statements)

References 170 publications

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“…4E and 6, A, B, O). The most striking feature of these ubiquitin-immunoreactive proteins was the fact that they were detected mainly on the outer face of the ZP, which is in contrast with the homogeneous distribution of major ZP components, ZP 1, 2, and 3 throughout the mammalian zona [24,25]. Certain types of sugar residues present in zona glycoproteins are concentrated on the inner face of the ZP, while others are dispersed evenly throughout it [45].…”

Section: Ubiquitinated Proteins Are Present On Outer Face Of Porcine mentioning

confidence: 92%

“…Targeted mutations and knockouts of several candidate acrosomal enzymes and sperm surface receptors did not eliminate the ability of mouse sperm to bind to and penetrate/digest the zona (reviewed in [24,25]). This suggests that a proteolytic system other than serine proteases exists in the sperm acrosome and contributes to the digestion of ZP during fertilization.…”

Section: Introductionmentioning

confidence: 98%

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Proteasomal Interference Prevents Zona Pellucida Penetration and Fertilization in Mammals1

Šutovský

Manandhar

McCauley

et al. 2004

Biology of Reproduction

114

122

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The ubiquitin-proteasome pathway has been implicated in the penetration of ascidian vitelline envelope by the fertilizing spermatozoon (Sawada et al., Proc Natl Acad Sci U S A 2002; 99:1223-1228). The present study provides experimental evidence demonstrating proteasome involvement in the penetration of mammalian zona pellucida (ZP). Using porcine in vitro fertilization as a model, penetration of ZP was completely inhibited by specific proteasomal inhibitors MG-132 and lactacystin. Three commercial rabbit sera recognizing 20S proteasomal core subunits beta-1i, beta-2i, alpha-6, and beta-5 completely blocked fertilization at a very low concentration (i.e., diluted 1/2000 to 1/8000 in fertilization medium). Neither proteasome inhibitors nor antibodies had any effects on sperm-ZP binding and acrosome exocytosis in zona-enclosed oocytes or on fertilization rates in zona-free oocytes, which were highly polyspermic. Consistent with a possible role of ubiquitin-proteasome pathway in ZP penetration, ubiquitin and various alpha and beta type proteasomal subunits were detected in boar sperm acrosome by specific antibodies, immunoprecipitated and microsequenced by MALDI-TOF from boar sperm extracts. Antiubiquitin-immunoreactive substrates were detected on the outer face of ZP by epifluorescence microscopy. This study therefore provides strong evidence implicating the ubiquitin-proteasome pathway in mammalian fertilization and zona penetration. This finding opens a new line of acrosome/ZP research because further studies of the sperm acrosomal proteasome can provide new tools for the management of polyspermia during in vitro fertilization and identify new targets for contraceptive development.

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Section: Ubiquitinated Proteins Are Present On Outer Face Of Porcine mentioning

confidence: 92%

Section: Introductionmentioning

confidence: 98%

Proteasomal Interference Prevents Zona Pellucida Penetration and Fertilization in Mammals1

Šutovský

Manandhar

McCauley

et al. 2004

Biology of Reproduction

114

122

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“…On its surface there are receptors for the attachment and binding of capacitated spermatozoa and it is involved in the subsequent induction of the acrosome reaction [26]. Moreover, modifications to the zona pellucida following fertilization prevent polyspermy [27]. Thus, the IVF assays using zona-free oocytes might be considered incomplete for assessing fertility, since sperm fertility can be described as the ability of the spermatozoon to bind and cross the zona pellucida, to perform the fusion of its membrane with oocyte's oolema, to achive the formation of the male pronucleus and to conduct to the zygote cleavage.…”

Section: Introductionmentioning

confidence: 99%

Heterologous in vitro fertilization is a good procedure to assess the fertility of thawed ram spermatozoa

et al. 2009

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“…Uncapacitated sperm are not able to penetrate the cumulus matrix surrounding the oocyte (Talbot, 1985;Corselli and Talbot, 1987), and although they are able to bind to the zona pellucida (ZP), they have a reduced ability to undergo ZP-induced acrosomal exocytosis and a reduced capacity to fertilize in vitro (Visconti et al, 1995a,b). Following capacitation, sperm acquire the capacity to undergo ZP-stimulated acrosomal exocytosis, penetrate the ZP, and fuse with the egg (Cardullo and Thaler, 2002).…”

Section: Introductionmentioning

confidence: 99%

Reorganization of mouse sperm lipid rafts by capacitation

Thaler

Thomas

Ramalie

2006

Molecular Reproduction Devel

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One of the hallmarks of mammalian sperm capacitation is the loss of cholesterol from the plasma membrane. Cholesterol has been associated with the formation of detergent insoluble membrane microdomains in many cell types, and sperm from several mammalian species have been shown to contain detergent-resistant membranes (DRMs). The change in cholesterol composition of the sperm plasma membrane during capacitation raises the question of whether the contents of DRMs are altered during this process. In this study, we investigated changes in protein composition of DRMs isolated from uncapacitated or capacitated mouse sperm. TX-100 insoluble membranes were fractionated by sucrose flotation gradient centrifugation and analyzed by Western and lectin blotting, and capacitation-related differences in protein composition were identified. Following capacitation, the detergent insoluble fractions moved to lighter positions on the sucrose gradients, reflecting a global change in density or composition. We identified several individual proteins that either became enriched or depleted in DRM fractions following capacitation. These data suggest that the physiological changes in sperm motility, ability to penetrate the zona pellucida (ZP), ZP responsiveness, and other capacitation-dependent changes, may be due in part to a functional reorganization of plasma membrane microdomains.

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Function of the Egg's Extracellular Matrix

Cited by 5 publications

References 170 publications

Proteasomal Interference Prevents Zona Pellucida Penetration and Fertilization in Mammals1

Proteasomal Interference Prevents Zona Pellucida Penetration and Fertilization in Mammals1

Heterologous in vitro fertilization is a good procedure to assess the fertility of thawed ram spermatozoa

Reorganization of mouse sperm lipid rafts by capacitation

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