ArticleMolecular & cellular proteomics : MCP2012
Isolation and proteomic characterization of the mouse sperm acrosomal matrix.
Article in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 60 citations in OpenAlex.
- Pervasive relaxed selection on spermatogenesis genes coincident with the evolution of polygyny in gorillas.eLife · 2026Article
- Multiple Roles of Protamine Kinase SRPK1 and Phosphatase PP1γ in Sperm Development.Proteomics · 2026Article
- Epididymal sperm maturation in mouse species with differing levels of sperm competition†.Biology of reproduction · 2026Article
- Towards a kingdom of reproductive life - the core sperm proteome.Reproduction (Cambridge, England) · 2025Article
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- Mapping the proteome landscape of Indian Zebu (Sahiwal) spermatozoa using high-resolution mass spectrometry andAnimal biotechnology · 2024Article
- Sperm acquire epididymis-derived proteins through epididymosomes.Human reproduction (Oxford, England) · 2022Article
- Using publicly available transcriptomic data to identify mechanistic and diagnostic biomarkers in azoospermia and overall male infertility.Scientific reports · 2022Article
- Biological Roles of Lipocalins in Chemical Communication, Reproduction, and Regulation of Microbiota.Frontiers in physiology · 2021Review
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- The epididymal amyloid matrix: structure and putative functions.Andrology · 2019Review
- Addressing the Compartmentalization of Specific Integrin Heterodimers in Mouse Sperm.International journal of molecular sciences · 2019Article
- Mechanism of Acrosome Biogenesis in Mammals.Frontiers in cell and developmental biology · 2019Review
- Glycogen Synthase Kinase-3 Regulates Sperm Motility and Acrosome Reaction via Affecting Energy Metabolism in Goats.Frontiers in physiology · 2019Article
- Characterization of the functions and proteomes associated with membrane rafts in chicken sperm.PloS one · 2017Article
- Identification of sperm equatorial segment protein 1 in the acrosome as the primary binding target of peanut agglutinin (PNA) in the mouse testis.Histochemistry and cell biology · 2017Article
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- Article
- Functional amyloids in the mouse sperm acrosome.Molecular and cellular biology · 2014Article
- Daddy issues: paternal effects on phenotype.Cell · 2012Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A critical step during fertilization is the sperm acrosome reaction in which the acrosome releases its contents allowing the spermatozoa to penetrate the egg investments. The sperm acrosomal contents are composed of both soluble material and an insoluble material called the acrosomal matrix (AM). The AM is thought to provide a stable structure from which associated proteins are differentially released during fertilization. Because of its important role during fertilization, efforts have been put toward isolating the AM for biochemical study and to date AM have been isolated from hamster, guinea pig, and bull spermatozoa. However, attempts to isolate AM from mouse spermatozoa, the species in which fertilization is well-studied, have been unsuccessful possibly because of the small size of the mouse sperm acrosome and/or its fusiform shape. Herein we describe a procedure for the isolation of the AM from caput and cauda mouse epididymal spermatozoa. We further carried out a proteomic analysis of the isolated AM from both sperm populations and identified 501 new proteins previously not detected by proteomics in mouse spermatozoa. A comparison of the AM proteome from caput and cauda spermatozoa showed that the AM undergoes maturational changes during epididymal transit similar to other sperm domains. Together, our studies suggest the AM to be a dynamic and functional structure carrying out a variety of biological processes as implied by the presence of a diverse group of proteins including proteases, chaperones, hydrolases, transporters, enzyme modulators, transferases, cytoskeletal proteins, and others.
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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.