| Molecular mechanism of epididymal protease inhibitor modulating the liquafication of human semen |
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| 引用本文： | Zengjun Wang,Wei Zhang,Hongfei Wu,Yuangeng Xu. Molecular mechanism of epididymal protease inhibitor modulating the liquafication of human semen[J]. 南京医科大学学报(自然科学版), 2007, 21(1): 59-62 |
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| 作者姓名： | Zengjun Wang Wei Zhang Hongfei Wu Yuangeng Xu |
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| 作者单位： | Department of Urology, The First Affiliated Hospital of Nanjing Medical University, Nanjing 210029, China |
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| 基金项目： | We thank Dr.M.G.0＇Rand,Dr.F.S.French and Dr.R. T.Richardson （Labs for Reproductive Biology, Department of Cell and Developmental Biology,University of North Carolina at Chapel Hill）for their technical assistance. This study was supported by Forgarty international fellowship. |
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| 摘 要： | To study the molecular mechanism of epididymal protease inhibitor （Eppin） modulating the liquafication of semen. Methods： Human semenogelin cDNA （nucleotides 82-849） and Eppin cDNA （nucleotides 70-423） were generated by PCR and cloned into pET-100D/TOPO.Recombinant Eppin and Sg were produced by BL21 （DE3）. The association of Eppin with Sg was studied by far-western and radioautography.In vitro the digestion of Sg by PSA in the presence or absence of recombinant Eppin was studied. The effect of anti-Q20E （N-terminal） and C-terminal of Eppin on Eppin-Sg binding was monitored. Results： Eppin binds Sg on the surface of human spermatozoa with C-terminal Eppin （aa75-133）.Recombinant Sg was digested with PSA ,many low molecular weight fragments were produced, when Eppin is bound to Sg ,then digested by PSA ,producing incomplete digestion and a 14.5-14.8 kDa fragmen. Antibody binding to the N-terminal of Eppin did not affect Sg digestion. Addition of antibodies to the C-terminal of Eppin inhibited the modulating effects of Eppin. Conclusion： Eppin modulates the digestion activity of PSA through binding Sg.The active site locates at C-terminal.
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| 关 键 词： | 分子机制 蛋白酶 抑制剂 精子 |
| 收稿时间： | 2006-09-08 |
Molecular mechanism of epididymal protease inhibitor modulating the liquafication of human semen |
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| Zengjun Wang,Wei Zhang,Hongfei Wu and Yuangeng Xu. Molecular mechanism of epididymal protease inhibitor modulating the liquafication of human semen[J]. Acta Universitatis Medicinalis Nanjing, 2007, 21(1): 59-62 |
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| Authors: | Zengjun Wang Wei Zhang Hongfei Wu Yuangeng Xu |
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| Abstract: | Objective: To study the molecular mechanism of epididymal protease inhibitor (Eppin) modulating the liquafication of semen.Methods: Human semenogelin cDNA (nucleotides 82-849) and Eppin cDNA (nucleotides 70-423) were generated by PCR and cloned into pET-100D/TOPO.Recombinant Eppin and Sg were produced by BL21 (DE3). The association of Eppin with Sg was studied by far-western and radioautography.In vitro the digestion of Sg by PSA in the presence or absence of recombinant Eppin was studied. The effect of anti-Q20E (N-terminal) and C-terminal of Eppin on Eppin-Sg binding was monitored. Results: Eppin binds Sg on the surface of human spermatozoa with C-terminal Eppin (aa75-133).Recombinant Sg was digested with PSA ,many low molecular weight fragments were produced, when Eppin is bound to Sg,then digested by PSA , producing incomplete digestion and a 14.5-14.8 kDa fragmen. Antibody binding to the N-terminal of Eppin did not affect Sg digestion. Addition of antibodies to the C-terminal of Eppin inhibited the modulating effects of Eppin. Conclusion: Eppin modulates the digestion activity of PSA through binding Sg. The active site locates at C-terminal. |
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| Keywords: | epididymal protease inhibitor semenogelin prostate specific antigen semen human protease inhibitor mechanism active site activity Addition antibodies effects Antibody affect producing incomplete bound low molecular weight fragments surface spermatozoa Results binding |
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