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Abstract

Volume 9, Issue 1 (January 2007) 9, 23–29; 10.1111/j.1745-7262.2007.00247.x

Inhibition of mouse acrosome reaction and sperm-zona pellucida binding by anti-human sperm membrane protein 1 antibody

Guo-Yan Cheng, Jian-Li Shi, Min Wang, Yan-Qin Hu, Chun-Meng Liu, Yi-Fei Wang and Chen Xu

1.Department of Histology and Embryology, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China
2.Shanghai Key Laboratory for Reproductive Medicine, Shanghai 200025, China

Correspondence: Prof. Chen Xu, Department of Histology and Embryology, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China. Fax: +86-21-6466-3160. E-mail: chenx@shsmu.edu.cn

Received 7 April 2006; Accepted 2 November 2006.

Abstract

Aim: To investigate the possible functions of human sperm membrane protein (hSMP-1) in the process of fertilization.

Methods: A 576-bp cDNA fragment of HSD-1 gene coding for the extracellular domain of hSMP-1 was cloned and expressed. The localization of this protein on human and mouse sperm was determined by indirect immunofluorescent staining by using anti-recombinant hSMP-1 (anti-rhSMP-1) antibodies. Sperm acrosome reaction and sperm-zona pellucida (ZP) binding assay were carried out in 10-week-old BALB/c mice.

Results: Recombinant hSMP-1 was successfully cloned and expressed. The expression of the native protein was limited on the acrosome of human and mouse sperm. Treatment of anti-rhSMP-1 antibodies significantly decreased the average number of sperms bound to each egg. Meanwhile, the percentage of acrosome reaction was decreased in comparison to pre-immune control after treatment with anti-rhSMP-1 (P < 0.05).

Conclusion: The results suggest that anti-rhSMP-1 antibody inhibited mouse acrosome reaction and sperm-ZP binding.

Keywords: human sperm membrane protein-1, SPAG8 protein, gene expression, acrosome reaction, sperm-oocyte interactions, zona pellucida, fertilization

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Asian Journal of Andrology CN 31-1795/R ISSN 1008-682X  Copyright © 2023  Shanghai Materia Medica, Chinese Academy of Sciences.  All rights reserved.