A monoclonal antibody to human SP-10 inhibits in vitro the binding of human sperm to hamster oolemma but not to human zona pellucida

Toshio Hamatani, Kiyoo Tanabe, Kiyoshi Kamei, Nozomi Sakai, Yurie Yamamoto, Yasunori Yoshimura

研究成果: Article査読

32 被引用数 (Scopus)

抄録

SP-10 is a sperm intra-acrosomal protein, specific to the testis, that is believed to play an important role in egg-sperm binding. While the molecular characterization of the SP-10 protein has been clarified, little is yet known of its functional role in fertilization. We therefore established a monoclonal antibody (mAb pep-SP10) against a peptide (pep-SP10) that included the most hydrophilic portion of human SP-10 between the 135th and 149th amino acids. Human SP-10 was found to be localized in the equatorial region of acrosome-reacted sperm by immunofluorescent staining using our mab pep-SP10. Monoclonal Ab pep-SP10 inhibited sperm-oolemma binding in the zona-free hamster egg penetration test, but it did not inhibit sperm-zona binding in the hemizona assay. Furthermore, we demonstrated that the oolemmal ligands of human SP-10 did not include β1 integrins, the most promising candidates for oocyte ligands involved in sperm-oolemma binding, based on the findings of a human sperm-cultured cell binding assay using F9 mouse embryonal carcinoma cells and F9-transformed cells lacking β1 integrins. In conclusion, our present data suggest that human SP10, expressed on the equatorial region of acrosome-reacted sperm, indeed mediates sperm-oolemma binding in a β1 integrin-independent manner, but not sperm-zona binding.

本文言語English
ページ(範囲)1201-1208
ページ数8
ジャーナルBiology of reproduction
62
5
DOI
出版ステータスPublished - 2000

ASJC Scopus subject areas

  • 生殖医学
  • 細胞生物学

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