A plasma membrane-associated hyaluronidase is localized to the posterior acrosomal region of stallion sperm and is associated with spermatozoal function.
Abstract: Sperm hyaluronidase has been implicated in sperm penetration of the extracellular matrix of the cumulus oophorus and may play a crucial role in gamete interaction and fertility in mammals. The objectives of this study were to characterize the enzyme activity of equine sperm hyaluronidase and to investigate its cellular distribution. Zymography of stallion sperm plasma membrane extracts was used to identify hyaluronidase activity in protein bands. Affinity-purified polyclonal IgG raised against equine sperm hyaluronidase was used to label fresh and capacitated stallion sperm, followed by indirect immunofluorescence. Equine sperm plasma membrane extracts displayed 3 major protein bands with potent hyaluronidase activity of approximately 54, 59, and 83 kDa. Under reducing conditions, a single protein band was observed at 62 kDa, although the reduced sample exhibited no enzyme activity. The polyclonal IgG labeled the postacrosomal region of stallion sperm and was redistributed over the acrosomal region during in vitro capacitation in a significant percentage of sperm cells. These studies suggest that a specific protein localized to the equine sperm head displays hyaluronidase activity, gets redistributed over the acrosomal region during capacitation, and may be important in fertility in this species.
Publication Date: 1999-07-20 PubMed ID: 10411525DOI: 10.1095/biolreprod61.2.444Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
- Research Support
- U.S. Gov't
- Non-P.H.S.
Summary
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The research article explores the role and characteristics of sperm hyaluronidase, a protein associated with fertilization, in stallion sperm. This study is significant for understanding the protein’s involvement in equine fertility.
Study Objectives
- The study aimed to characterize the enzyme activity of equine sperm hyaluronidase. This enzyme has been linked to sperm penetration of the extracellular matrix of the cumulus oophorus, a group of cells that surround the egg in most mammals. Therefore, understanding its properties could offer insights into mammalian fertility processes.
- Another objective was to investigate the cellular distribution of hyaluronidase in stallion sperm. Knowing where this enzyme is located could help elucidate its role in the sperm and fertilization process.
Methodology and Findings
- The researchers used zymography, a technique used to detect enzyme activity, of stallion sperm plasma membrane extracts to identify hyaluronidase activity in protein bands.
- Affinity-purified polyclonal IgG, a type of antibody, against equine sperm hyaluronidase was used to label stallion sperm. This labeling allowed for visualization under indirect immunofluorescence.
- The research observed 3 major protein bands with potent hyaluronidase activity and their corresponding molecular weight.
- A single protein band was observed under reducing conditions. However, this reduced sample displayed no enzyme activity. The discrepancy points to the potential importance of environmental conditions on enzyme activity.
- The polyclonal IgG was found to label the posterior acrosomal region of stallion sperm, which is a part of the sperm cell that releases digestive enzymes during fertilization.
- During in vitro capacitation, a process that prepares the sperm for fertilization, the enzyme redistributed across the acrosomal region in a significant number of sperm cells.
Implications of the Study
- The findings suggest that hyaluronidase in stallions is a specific protein located in the equine sperm head. It displays enzymatic activity, undergoes redistribution during capacitation, and may play a crucial role in equine fertility.
- The study could help researchers understand processes related to fertility in horses, with the potential for comparative studies on fertility in other mammals.
Cite This Article
APA
Meyers SA, Rosenberger AE.
(1999).
A plasma membrane-associated hyaluronidase is localized to the posterior acrosomal region of stallion sperm and is associated with spermatozoal function.
Biol Reprod, 61(2), 444-451.
https://doi.org/10.1095/biolreprod61.2.444 Publication
Researcher Affiliations
- Gamete Biology Laboratory, Department of Clinical Studies, New Bolton Center, School of Veterinary Medicine, University of Pennsylvania, Kennett Square, Pennsylvania 19348-0692, USA. smeyers@ucdavis.edu
MeSH Terms
- Acrosome / drug effects
- Acrosome / enzymology
- Animals
- Cell Membrane / enzymology
- Exocytosis / drug effects
- Fluorescent Antibody Technique, Indirect
- Horses / physiology
- Hyaluronoglucosaminidase / metabolism
- Male
- Progesterone / pharmacology
- Sperm Capacitation
- Spermatozoa / enzymology
- Spermatozoa / physiology
Citations
This article has been cited 8 times.- Service CA, Puri D, Hsieh TC, Patel DP. Emerging concepts in male contraception: a narrative review of novel, hormonal and non-hormonal options. Ther Adv Reprod Health 2023 Jan-Dec;17:26334941221138323.
- Kumar A, Yadav B, Swain DK, Anand M, Madan AK, Yadav RKS, Kushawaha B, Yadav S. Dynamics of HSPA1A and redox status in the spermatozoa and fluid from different segments of goat epididymis. Cell Stress Chaperones 2020 May;25(3):509-517.
- Schiza C, Korbakis D, Panteleli E, Jarvi K, Drabovich AP, Diamandis EP. Discovery of a Human Testis-specific Protein Complex TEX101-DPEP3 and Selection of Its Disrupting Antibodies. Mol Cell Proteomics 2018 Dec;17(12):2480-2495.
- Guyonnet B, Zabet-Moghaddam M, SanFrancisco S, Cornwall GA. Isolation and proteomic characterization of the mouse sperm acrosomal matrix. Mol Cell Proteomics 2012 Sep;11(9):758-74.
- Reid AT, Redgrove K, Aitken RJ, Nixon B. Cellular mechanisms regulating sperm-zona pellucida interaction. Asian J Androl 2011 Jan;13(1):88-96.
- Suri A. Sperm specific proteins-potential candidate molecules for fertility control. Reprod Biol Endocrinol 2004 Mar 10;2:10.
- Abou-Haila A, Tulsiani DR. Evidence for the capacitation-associated membrane priming of mouse spermatozoa. Histochem Cell Biol 2003 Mar;119(3):179-87.
- Koilpillai JN, Nunan E, Butler L, Pinaffi F, Butcher JT. Reversible Contraception in Males: An Obtainable Target?. Biology (Basel) 2024 Apr 25;13(5).
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