Suppression effect of seminal vesicle autoantigen on platelet-activating factor-induced mouse sperm capacitation
| Autor: | Chwen Ming Shih, Yee Hsiung Chen, Chun Mao Lin, Shin Peih Kuo, Yen Hua Huang, E. E. Chang, Yi Yun Ciou, Chien Tsu Chen |
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| Rok vydání: | 2007 |
| Předmět: |
Male
medicine.medical_specialty Acrosome reaction Biology Seminal Vesicle Secretory Proteins Autoantigens Biochemistry Mice chemistry.chemical_compound Human fertilization Seminal vesicle Capacitation Internal medicine Cyclic AMP medicine Animals Phosphorylation Platelet Activating Factor Phosphotyrosine Molecular Biology Platelet-activating factor urogenital system Tyrosine phosphorylation Cell Biology Flow Cytometry Spermatozoa Sperm Cell biology Secretory protein Endocrinology medicine.anatomical_structure chemistry Calcium Chromatography Thin Layer Sperm Capacitation Protein Binding |
| Zdroj: | Journal of Cellular Biochemistry. 100:941-951 |
| ISSN: | 1097-4644 0730-2312 |
| Popis: | Mammalian sperm gain the ability to fertilize an egg successfully by the capacitation process. An unregulated capacitation process causes sperm to undergo a spontaneous acrosome reaction (AR) and resulting in loss of their fertilization activity. Thus, functional sperm activation is tightly regulated by a capacitation and suppression (decapacitation) mechanism. Factors, such as platelet-activating factor (PAF) present in both sperm and the female genital tract, are able to stimulate sperm capacitation. Seminal plasma is thought to have the ability to suppress sperm capacitation; however, the regulatory mechanisms of seminal plasma protein on sperm capacitation are not well understood. Recently, we demonstrated that seminal vesicle autoantigen (SVA), a major seminal vesicle secretory protein, is able to suppress mouse sperm capacitation. To further study the suppression spectra of SVA on sperm capacitation, we investigated the effect of SVA on PAF-induced mouse sperm capacitation-related signals. Here, we demonstrate that SVA decreases the (Ca 2þ )i to suppress the PAF's effects on (Ca 2þ )i, the cAMP level, protein tyrosine phosphorylation, and capacitation. The inhibition of PAF-induced protein tyrosine phosphorylation and capacitation by SVA can be reversed by cAMP agonists. Characterization of the interactions of SVA with PAF by TLC overlay and tryptophan fluorescence spectrum analyses indicates that SVA is capable of binding PAF with an apparent dissociation constant Kd > 50 mM. Together with these results, we demonstrate that SVA deceases (Ca 2þ )i and cross-talks with PAF-induced intracellular signals to regulate mouse sperm capacitation. J. Cell. Biochem. 100: 941-951, 2007. 2006 Wiley-Liss, Inc. |
| Databáze: | OpenAIRE |
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