ArticleDevelopmental biology2007
Proteolytic processing of phospholipase Czeta and [Ca2+]i oscillations during mammalian fertilization.
Article in Developmental biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Mammalian PI-Phospholipase C Isozymes: Structural and Functional Insights and Roles in Health and Disease.Medicina (Kaunas, Lithuania) · 2025Review
- Oocyte activation with phospholipase Cζ mRNA induces repetitive intracellular CaThe Journal of reproduction and development · 2024Article
- Molecular Mechanism of Oocyte Activation in Mammals: Past, Present, and Future Directions.Biomolecules · 2024Review
- Phospholipase C Zeta 1 (PLCZ1): The Function and Potential for Fertility Assessment and In Vitro Embryo Production in Cattle and Horses.Veterinary sciences · 2023Review
- Ouabain-induced activation of phospholipase C zeta and its contributions to bovine sperm capacitation.Cell and tissue research · 2021Article
- Deletion of TRPV3 and CaV3.2 T-type channels in mice undermines fertility and Ca2+ homeostasis in oocytes and eggs.Journal of cell science · 2021Article
- Role of Satb1 and Satb2 Transcription Factors in the Glutamate Receptors Expression and CaInternational journal of molecular sciences · 2021Article
- Voltage Dependent N Type Calcium Channel in Mouse Egg Fertilization.Development & reproduction · 2020Article
- A homozygous nonsense mutation of PLCZ1 cause male infertility with oocyte activation deficiency.Journal of assisted reproduction and genetics · 2020Article
- FRET-based sensor for CaMKII activity (FRESCA): A useful tool for assessing CaMKII activity in response to CaThe Journal of biological chemistry · 2019Article
- Calcium influx and sperm-evoked calcium responses during oocyte maturation and egg activation.Oncotarget · 2017Review
- Sperm contributions to oocyte activation: more that meets the eye.Journal of assisted reproduction and genetics · 2016Review
- Subcellular localization of phospholipase Cζ in human sperm and its absence in DPY19L2-deficient sperm are consistent with its role in oocyte activation.Molecular human reproduction · 2015Article
- Protein phospholipase C Zeta1 expression in patients with failed ICSI but with normal sperm parameters.Journal of assisted reproduction and genetics · 2014Article
- Regulation of endoplasmic reticulum Ca(2+) oscillations in mammalian eggs.Journal of cell science · 2013Article
- Ca2+ influx and the store-operated Ca2+ entry pathway undergo regulation during mouse oocyte maturation.Molecular biology of the cell · 2013Article
- Oocyte activation and phospholipase C zeta (PLCζ): diagnostic and therapeutic implications for assisted reproductive technology.Cell communication and signaling : CCS · 2012Article
- Conserved properties of Drosophila and human spermatozoal mRNA repertoires.Proceedings. Biological sciences · 2012Article
- The phospholipase C isozymes and their regulation.Sub-cellular biochemistry · 2012Review
- Loss of activity mutations in phospholipase C zeta (PLCζ) abolishes calcium oscillatory ability of human recombinant protein in mouse oocytes.Human reproduction (Oxford, England) · 2011Article
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Authors and funding
6 authors.
Funding
Abstract
Phospholipase Czeta (PLCzeta) is a sperm-specific PLC capable of causing repetitive intracellular Ca2+ ([Ca2+]i) release ([Ca2+]i oscillations) in mammalian eggs. Accumulating evidence suggests that PLCzeta is the sperm factor responsible for inducing egg activation. Nevertheless, some sperm fractions devoid of 72-kDa PLCzeta showed [Ca2+]i oscillation-inducing and PLCzeta-like PLC activity (Kurokawa et al., (2005) Dev. Biol. 285, 376-392). Here, we report that PLCzeta remains functional after proteolytic cleavage at the X-Y linker region. We found that N-terminal (33 and 37 kDa) and C-terminal fragments (27 kDa), presumably the result of PLCzeta cleavage at the X-Y linker region, were present in fresh sperm as well as in sperm extracts and remained associated as functional complexes. Protease V8 cleaved 72-kDa PLCzeta into 33/37 and 27 kDa fragments, while PLC activity and [Ca2+]i oscillation-inducing activity persisted until degradation of the fragments. Immunodepletion or affinity depletion of these fragments abolished PLC activity and [Ca2+]i oscillation-inducing activity from sperm extracts. Lastly, co-expression of cRNAs encoding residues 1-361 and 362-647 of mouse PLCzeta, mimicking cleavage at the X-Y linker region, induced [Ca2+]i oscillations and embryo development in mouse eggs. Our results support the hypothesis that PLCzeta is the sole mammalian sperm factor and that its linker region may have important regulatory functions during mammalian fertilization.
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