Identification of carbohydrate-binding proteins in mammalian spermatozoa (human, bull, boar, ram, stallion and hamster) using [125I]fucoidin and [125I]neoglycoprotein probes.
Abstract: A protein-carbohydrate recognition system is thought to be involved in the early stages of fertilization in mammals. In this investigation carbohydrate-binding proteins have been identified in extracts of human, bull, boar, ram, stallion and hamster spermatozoa using [125I]fucoidin and [125I]neoglycoproteins (BSA-fucose and BSA-mannose) to probe Western blots. Results show that proacrosin is the major protein species recognized in extracts of human, bull, boar and ram spermatozoa. In hamster and stallion spermatozoa, carbohydrate-binding activity was associated with several low molecular weight proteins that may or may not be related to active forms of acrosin. These results support the hypothesis that proacrosin is involved in secondary or consolidated binding of mammalian spermatozoa to the zona pellucida by virtue of its carbohydrate-binding capacity.
Publication Date: 1989-07-01 PubMed ID: 2507577DOI: 10.1093/oxfordjournals.humrep.a136943Google Scholar: Lookup
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- Journal Article
Summary
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This research paper explores the role of carbohydrate-binding proteins in the early stages of mammalian fertilization, by examining extracts from various mammal sperm specimens. Findings suggest that proacrosin is the crucial protein implicated in the consolidation of sperm binding to the zona pellucida, a crucial step in fertilization.
Objective of the Study
- The research aimed to investigate the existence and role of carbohydrate-binding proteins in mammalian spermatozoa. The researchers theorized that these proteins are important in the early stages of fertilization, specifically in their ability to bind sperm to the zona pellucida, an essential element for a successful fertilization process.
Methodology
- Scientists studied extracts of sperm from various mammals, specifically human, bull, boar, ram, stallion, and hamster.
- These extracts were analyzed using [125I]fucoidin and [125I]neoglycoproteins (BSA-fucose and BSA-mannose) to probe Western blots, a common technique for identifying specific proteins.
Results
- Results from the study showed that proacrosin was the main protein species detected in human, bull, boar, and ram spermatozoa.
- In contrast, in hamster and stallion spermatozoa, carbohydrate-binding activity was associated with several low molecular weight proteins. The researchers tentatively identified these as potentially related to active forms of acrosin, a proteinase thought to be part of the fertilization process.
Conclusions
- The researchers concluded that their findings supported their initial hypothesis; proacrosin is most likely involved in the secondary or consolidated binding of mammalian spermatozoa to the zona pellucida, due to its carbohydrate-binding capacity.
- This suggests that proacrosin has a significant role in mammalian fertilization, contributing to our understanding of reproductive biology in mammals.
Cite This Article
APA
Jones R.
(1989).
Identification of carbohydrate-binding proteins in mammalian spermatozoa (human, bull, boar, ram, stallion and hamster) using [125I]fucoidin and [125I]neoglycoprotein probes.
Hum Reprod, 4(5), 550-557.
https://doi.org/10.1093/oxfordjournals.humrep.a136943 Publication
Researcher Affiliations
- Department of Molecular Embryology, AFRC Institute of Animal Physiology and Genetics Research, Babraham, Cambridge, UK.
MeSH Terms
- Acrosin / analysis
- Animals
- Blotting, Western
- Carrier Proteins / analysis
- Cattle
- Cricetinae
- Electrophoresis, Polyacrylamide Gel
- Enzyme Precursors / analysis
- Horses
- Humans
- Male
- Polysaccharides
- Receptors, Cell Surface
- Sheep
- Spermatozoa / analysis
- Spermatozoa / immunology
- Swine
- Urea
Citations
This article has been cited 2 times.- Bhattacharyya AK, Kanjilal S. Assessment of sperm functional competence and sperm-egg interaction. Mol Cell Biochem 2003 Nov;253(1-2):255-61.
- Avilés M, Abascal I, Martínez-Menárguez JA, Castells MT, Skalaban SR, Ballesta J, Alhadeff JA. Immunocytochemical localization and biochemical characterization of a novel plasma membrane-associated, neutral pH optimum alpha-L-fucosidase from rat testis and epididymal spermatozoa. Biochem J 1996 Sep 15;318 ( Pt 3)(Pt 3):821-31.
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