ArticleHistochemistry and cell biology2017
Identification of sperm equatorial segment protein 1 in the acrosome as the primary binding target of peanut agglutinin (PNA) in the mouse testis.
Article in Histochemistry and cell biology, 2017. 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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Who cites it
18 citing papers in PubMed, 29 citations in OpenAlex.
- Loss-of-Function SSFA2 Variants Disrupt Fertility Through Impaired Acrosome Formation and Sperm Function.Andrology · 2026Article
- The topographical distribution of spermatogonial subpopulations during the cycle of seminiferous epithelium in Macaca Fascicularis.Biology of reproduction · 2026Article
- Testis-specific lncRNA Teshl regulates acrosome biogenesis to maintain sperm structure and function.Cell & bioscience · 2026Article
- Exploration of Novel Markers in Tan Sheep Spermatogenesis.Animals : an open access journal from MDPI · 2026Article
- Intraflagellar transport-associated CCDC92 is required for spermiogenesis and male fertility in mice.Journal of molecular cell biology · 2025Article
- JADE1 is not essential for spermatogenesis and male fertility in mice.Molecular biology reports · 2025Article
- ELAPOR1 is a copper-dependent tethering factor driving proacrosomal vesicle fusion during acrosome biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- SERINC4 is dispensable for male fertility and spermatogenesis in mice.American journal of translational research · 2025Article
- Testis-enrichedAmerican journal of translational research · 2025Article
- ARF6, a component of intercellular bridges, is essential for spermatogenesis in mice.Developmental biology · 2024Article
- Steps of spermiogenesis in the ostrich (Struthio camelus).Cell and tissue research · 2023Article
- The SLC9C2 Gene Product (NaInternational journal of molecular sciences · 2023Article
- The piRNA-pathway factor FKBP6 is essential for spermatogenesis but dispensable for control of meiotic LINE-1 expression in humans.American journal of human genetics · 2022Article
- Quantitative evaluation of spermatogenesis by fluorescent histochemistry.Histochemistry and cell biology · 2022Review
- cAMP-specific phosphodiesterase 8A and 8B isoforms are differentially expressed in human testis and Leydig cell tumor.Frontiers in endocrinology · 2022Article
- Article
- Three-Dimensional Analysis of Busulfan-Induced Spermatogenesis Disorder in Mice.Frontiers in cell and developmental biology · 2020Article
- In focus in HCB.Histochemistry and cell biology · 2017Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peanut agglutinin (PNA), a plant lectin protein that recognizes the galactose β (1 -> 3) N-acetylgalactosamine carbohydrate sequence, has been widely used as a sperm acrosome-specific marker; however, the acrosomal glycoproteins that specifically bind to PNA have yet to be identified. We herein purified and identified PNA-binding glycoproteins in the mouse testis using biotinylated PNA and streptavidin-coupled magnetic beads, and liquid chromatography-tandem mass spectrometry (LC-MS/MS), respectively. In six repeated experiments, sperm equatorial segment protein 1 (SPESP1) was detected most frequently as a PNA-binding glycoprotein, followed by dipeptidase 3, proacrosin-binding protein, and acrosin prepropeptide. The identification of SPEPS1 in the testis lysate and its PNA-bound fraction was verified with lectin and Western blot analyses, and the co-localization of PNA and SPEPS1 in acrosomes was confirmed with lectin- and immunohistochemistry. Since the PNA reactivity of sperm acrosomes was observed not only in normal mice, but also in SPESP1-deficient mice, although at lower levels, PNA was also considered to bind to other candidate glycoproteins. The present study identified SPESP1 in the acrosome as the primary binding target of PNA in the mouse testis. Further defining the specific lectin-glycoprotein relationships in individual cells will enhance the value of lectin histochemistry.
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