Modes of acrosin functioning during fertilization

Mao, Haitao; Yang, Wan-Xi

doi:10.1016/j.gene.2013.05.058

Cited by 33 publications

(22 citation statements)

References 44 publications

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“…In comparison to the limited variety of biochemical cleavage mechanisms, there is an impressively diverse cellular and extracellular repertoire of physiological substrates, as well as endogenous protease inhibitors which are called into action for the regulation of proteolysis in response to cellular conditions (Andrade et al 2011;Brix et al 2013;Dauth et al 2011a;Turk et al 2008). Locally and temporally controlled protease activities are already seen very early in life, such as the acrosomal process during fertilization of the egg cell (Mao and Yang 2013). Spatiotemporally controlled protease actions also contribute to cellular fate decisions leading to proliferation, differentiation, or death (Ashkenazi and Salvesen 2014;Flütsch and Grütter 2013;Repnik et al 2012;Turk and Turk 2009).…”

Section: The Protease Family Businessmentioning

confidence: 99%

Proteolysis mediated by cysteine cathepsins and legumain—recent advances and cell biological challenges

et al. 2014

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Proteases play essential roles in protein degradation, protein processing, and extracellular matrix remodeling in all cell types and tissues. They are also involved in protein turnover for maintenance of homeostasis and protein activation or inactivation for cell signaling. Proteases range in function and specificity, with some performing distinct substrate cleavages, while others accomplish proteolysis of a wide range of substrates. As such, different cell types use specialized molecular mechanisms to regulate the localization of proteases and their function within the compartments to which they are destined. Here, we focus on the cysteine family of cathepsin proteases and legumain, which act predominately within the endo-lysosomal pathway. In particular, recent knowledge on cysteine cathepsins and their primary regulator legumain is scrutinized in terms of their trafficking to endo-lysosomal compartments and other less recognized cellular locations. We further explore the mechanisms that regulate these processes and point to pathological cases which arise from detours taken by these proteases. Moreover, the emerging biological roles of specific forms and variants of cysteine cathepsins and legumain are discussed. These may be decisive, pathogenic, or even deadly when localizing to unusual cellular compartments in their enzymatically active form, because they may exert unexpected effects by alternative substrate cleavage. Hence, we propose future perspectives for addressing the actions of cysteine cathepsins and legumain as well as their specific forms and variants. The increasing knowledge in non-canonical aspects of cysteine cathepsin- and legumain-mediated proteolysis may prove valuable for developing new strategies to utilize these versatile proteases in therapeutic approaches.

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Section: The Protease Family Businessmentioning

confidence: 99%

Proteolysis mediated by cysteine cathepsins and legumain—recent advances and cell biological challenges

et al. 2014

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“…Biochemical studies identified the role of acrosome components during sperm–ova interactions, especially those involving the zona pellucida, and thus provided major advances in sperm cell biology. Acrosin functions during fertilization inducing secondary binding with the ZP, and hydrolysis of the ZP (Howes, Pascall, Engel, & Jones, ; Mao & Yang, ). However, it was recently reported that the 45‐kDa acrosin located on the plasma membrane is responsible for ZP binding, but is not important for the digestion of ZP proteins (Sasanami, Yoshizaki, Dohra, & Kubo, ).…”

Section: Introductionmentioning

confidence: 99%

Inhibition of PSMD4 alters ZP1 ubiquitination state and sperm–oocyte‐binding ability in pigs

Xuan

et al. 2018

Reprod Domestic Animals

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The aim of this study was to determine how the duration of culture affects the ubiquitination of zona pellucida (ZP) proteins (ZP1, ZP2 and ZP3) during porcine oocyte maturation in vitro. We analysed the changes in ZP protein ubiquitination under three conditions: (i) during oocyte maturation from stage GV to MII; (ii) in oocytes cultured for different periods of time; and (iii) in oocytes treated with an antibody against PSMD4. Our results show that ZP1 and ZP2 are ubiquitinated at the GV stage, while ZP1, ZP2 and ZP3 are ubiquitinated at the MII stage, and band intensities for these proteins were significantly different between the GV and MII stages (p < .05). We also found that ubiquitination occurs in ZP1, ZP2 and ZP3 after cultured for 46, 52, 58 and 64 hr, and that the level of ubiquitinated ZP1 was significantly different in oocytes that were cultured for different time periods. Finally, treatment with an antibody against PSMD4 resulted in a significant decrease in ZP1 ubiquitination (p < .05), without affecting ZP2 or ZP3. The number of attached sperms per oocyte was also significantly different between control and anti-PSMD4-treated groups. Thus, we concluded that ZP1 and ZP2 are ubiquitinated at the GV stage, and ZP1, ZP2 and ZP3 are ubiquitinated at the MII stage. As the duration of culture increases, the ubiquitination levels of ZP proteins decrease. We also found that PSMD4 improves ZP1 ubiquitination during in vitro culture of porcine oocytes and effectively inhibits sperm-oocyte binding.

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“…A number of proteases have been identified in the acrosome of mouse sperm including acrosin, an endoprotease with trypsin-like specificity located on the inner acrosomal membrane (IAM) [25, 26]. Acrosin is derived from the enzymatically inactive zymogen, proacrosin, which is converted to the active form as a result of AE [27].…”

Section: Introductionmentioning

confidence: 99%

Glycopolymer induction of mouse sperm acrosomal exocytosis shows highly cooperative self-antagonism

Rodolis

Huang

Sampson

2016

Biochemical and Biophysical Research Communications

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Identifying inducers of sperm acrosomal exocytosis (AE) to understand sperm functionality is important for both mechanistic and clinical studies in mammalian fertilization. Epifluorescence microscopy methods, while reproducible, are laborious and incompatible for high throughput screening. Flow cytometry methods are ideal for quantitative measurements on large numbers of samples, yet typically rely on the use of lectins that can interfere with physiologic AE-inducers. Here, we present an optimized triple stain flow cytometric method that is suitable for high-throughput screening of AE activation by glycopolymers. SYTO-17 and propidium iodide (PI) were used to differentiate cells based on their membrane integrity or viability, and membrane impermeable soybean trypsin inhibitor (SBTI) was used to monitor acrosome exocytosis. The SBTI/PI/SYTO-17 combination provides a positive screen for viability and AE of live sperm cells with minimal noise or false positives. A scattering gate enables the use of samples that may be contaminated with non-cellular aggregates, e.g., cryopreservation agents. This assay format enabled detailed analysis of glycopolymer dose response curves. We found that fucose polymer has a narrow effective dose range (EC50 = 1.6 µM; IC50 = 13.5 µM); whereas mannose polymer and β-N-acetylglucosamine polymer have broader effective dose ranges (EC50 = 1.2 µM and 3.4 µM, respectively). These results highlight the importance of testing inducers over a large concentration range in small increments for accurate comparison.

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Modes of acrosin functioning during fertilization

Cited by 33 publications

References 44 publications

Proteolysis mediated by cysteine cathepsins and legumain—recent advances and cell biological challenges

Proteolysis mediated by cysteine cathepsins and legumain—recent advances and cell biological challenges

Inhibition of PSMD4 alters ZP1 ubiquitination state and sperm–oocyte‐binding ability in pigs

Glycopolymer induction of mouse sperm acrosomal exocytosis shows highly cooperative self-antagonism

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