ArticleCell and tissue research2018
Modifications of the 26S proteasome during boar sperm capacitation.
Article in Cell and tissue research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
18 citing papers in PubMed, 34 citations in OpenAlex.
- Capacitation of ram spermatozoa promotes changes in energy metabolism and aquaporin 3 and is affected by individual testosterone variations.Andrology · 2025Article
- A century of andrology in Cell & Tissue Research: looking back while moving forward.Cell and tissue research · 2025Review
- Methods of Mammalian In Vitro Sperm Capacitation to Study Sperm Physiology.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Bottom-up approach to deciphering the targets of the ubiquitin-proteasome system in porcine sperm capacitation.Scientific reports · 2024Article
- Comparative Proteomic Identification of Ram Sperm before and after In Vitro Capacitation.Animals : an open access journal from MDPI · 2024Article
- Biomarker-based human and animal sperm phenotyping: the good, the bad and the ugly†.Biology of reproduction · 2024Review
- PSMB2 plays an oncogenic role in glioma and correlates to the immune microenvironment.Scientific reports · 2024Article
- The Ubiquitin-Proteasome System Participates in Sperm Surface Subproteome Remodeling during Boar Sperm Capacitation.Biomolecules · 2023Article
- Zinc is a master-regulator of sperm function associated with binding, motility, and metabolic modulation during porcine sperm capacitation.Communications biology · 2022Article
- Hyperactivation is sufficient to release porcine sperm from immobilized oviduct glycans.Scientific reports · 2022Article
- Quantitative phosphoproteomics analyses reveal the regulatory mechanisms related to frozen-thawed sperm capacitation and acrosome reaction in yak (Frontiers in physiology · 2022Article
- A Non-Synonymous Point Mutation in a WD-40 Domain Repeat of EML5 Leads to Decreased Bovine Sperm Quality and Fertility.Frontiers in cell and developmental biology · 2022Article
- Oxidant-Sensitive Inflammatory Pathways and Male Reproductive Functions.Advances in experimental medicine and biology · 2022Article
- Progesterone induces porcine sperm release from oviduct glycans in a proteasome-dependent manner.Reproduction (Cambridge, England) · 2021Article
- The activation of the chymotrypsin-like activity of the proteasome is regulated by soluble adenyl cyclase/cAMP/protein kinase A pathway and required for human sperm capacitation.Molecular human reproduction · 2019Article
- Compartmentalization of the proteasome-interacting proteins during sperm capacitation.Scientific reports · 2019Article
- Pharmacologic treatment with CPI-613 and PS48 decreases mitochondrial membrane potential and increases quantity of autolysosomes in porcine fibroblasts.Scientific reports · 2019Article
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Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Protein ubiquitination is a stable, reversible post-translational modification, targeting proteins for degradation/recycling by the 26S proteasome in a well-characterized enzymatic cascade. Studies have revealed the role of UPS in the regulation of fertilization, including sperm-zona pellucida interactions and the early event of sperm capacitation. The present study investigates the changes in proteasome compartmentalization, subunit composition and post-translational modifications during in vitro capacitation of fresh boar spermatozoa. We observed capacitation-dependent shedding of both 20S core and 19S regulatory particles from the acrosome that was associated with decreased plasma membrane integrity, independent of proteasomal inhibition. Subunits PSMA1-7 of the 20S core did not appear to undergo post-translational modifications during capacitation, based on invariant molecular masses before and after capacitation; however, we observed multiple PSMD4 forms of 19S regulatory particles (50, 53, 70, 115-140, 160 and >176 kDa) sequentially released from spermatozoa. PSMD4 subunit was found to be post-translationally modified during the course of capacitation, resulting in changes of apparent molecular mass, some of which were dependent on proteasomal inhibition. These results show that the sperm proteasomes are being modified during sperm capacitation. Additional studies of individual 26S proteasome subunits will be required to elucidate these modifications and to understand how UPS modulates sperm capacitation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.