Pig sperm membrane microdomains contain a highly glycosylated 15–25-kDa wheat germ agglutinin-binding protein
| Autor: | Estelle Garénaux, Xue Lian, Ken Kitajima, Chihiro Sato, Waraporn Kasekarn, Kazuki Hori, Nongnuj Tanphaichitr, Kessiri Kongmanas, H. Yasue, Takeru Kanazawa, Tomoyuki Tsuchiyama |
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| Rok vydání: | 2012 |
| Předmět: |
Male
Glycosylation Wheat Germ Agglutinins Sus scrofa Biophysics Flagellum Biochemistry chemistry.chemical_compound Membrane Microdomains biology.animal Animals Molecular Biology Sea urchin Lipid raft Glycoproteins chemistry.chemical_classification biology Binding protein Cell Biology Spermatozoa Sperm Wheat germ agglutinin chemistry Carrier Proteins Glycoprotein |
| Zdroj: | Biochemical and Biophysical Research Communications. 426:356-362 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2012.08.090 |
| Popis: | A highly glycosylated protein, which has unique, novel features in localization, structure, and potential function, is found in pig sperm, and named WGA-gp due to its high binding property with wheat germ agglutinin (WGA). WGA-gp is localized mainly in flagella and enriched in membrane microdomains or lipid rafts. It is not detected by ordinary protein staining methods due to a high content of both N- and O-glycans consisting of neutral monosaccharides. Interestingly, WGA-gp may be involved in intracellular Ca(2+) regulation. Treatment of sperm with anti-WGA-gp antibody enhances the amplitude of Ca(2+) oscillation without changing the basal intracellular Ca(2+) concentrations. All these features of WGA-gp, except for different carbohydrate structures occupying most part of the molecules, are similar to those of flagellasialin in sea urchin sperm, which regulates the intracellular Ca(2+) concentration. Presence of carbohydrate-enriched flagellar proteins involved in intracellular Ca(2+) regulation may be a common feature among animal sperm. |
| Databáze: | OpenAIRE |
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