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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Defaus, Sira Avilés, Manuel Andreu, David Gutiérrez-Gallego, Ricardo |
| Description | Author Affiliation: Defaus S ( From the Department of Experimental and Health Sciences, Pompeu Fabra University, Barcelona Biomedical Research Park, 08003 Barcelona, Spain); Avilés M ( §Department of Cell Biology and Histology, School of Medicine, University of Murcia and IMIB, Campus Mare Nostrum, 30071 Murcia, Spain.); Andreu D ( From the Department of Experimental and Health Sciences, Pompeu Fabra University, Barcelona Biomedical Research Park, 08003 Barcelona, Spain); Gutiérrez-Gallego R ( From the Department of Experimental and Health Sciences, Pompeu Fabra University, Barcelona Biomedical Research Park, 08003 Barcelona, Spain) |
| Abstract | Glycan-protein interactions play a key role in mammalian fertilization, but data on the composition and identities of protein complexes involved in fertilization events are scarce, with the added complication that the glycans in such interactions tend to differ among species. In this study we have used a bovine model to detect, characterize and identify sperm lectins relevant in fertilization. Given the complexity of the sperm-toward-egg journey, two important aspects of the process, both primarily mediated by protein-sugar interactions, have been addressed: (1) formation of the sperm reservoir in the oviductal epithelium, and (2) gamete recognition (oocyte-sperm interaction). Using whole sperm cells and a novel affinity capture method, several groups of proteins with different glycan specificities, including 58 hitherto unreported as lectins, have been identified in sperm surface, underscoring both the efficacy of our selective approach and the complex composition and function of sperm. Based on these results and previous data, we suggest that sperm surface proteins play significant roles in fertilization events such as membrane remodeling, transport, protection and function, thus supporting the hypothesis that rather than a simple lock-and-key model, mammalian fertilization relies on a complex interactome involving multiple ligands/receptors and recognition/binding events. |
| File Format | HTM / HTML |
| ISSN | 15359476 |
| e-ISSN | 15359484 |
| Journal | Molecular & Cellular Proteomics |
| Issue Number | 7 |
| Volume Number | 15 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology |
| Publisher Date | 2016-07-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Discipline Proteomics |
| Content Type | Text |
| Resource Type | Article |
| Subject | Medicine Analytical Chemistry Molecular Biology Biochemistry |
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