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Mol. Hum. Reprod. Advance Access published online on January 18, 2008
Molecular Human Reproduction, doi:10.1093/molehr/gan003
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© The Author 2008. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Physiological roles of semenogelin I and zinc in sperm motility and semen coagulation on ejaculation in humans

Kaoru Yoshida, Natsuko Kawano§, Miki Yoshiike*, Manabu Yoshida§, Teruaki Iwamoto and Masaaki Morisawa{dagger}

Biomedical Engineering Center, Toin University of Yokohama, 1614 Kurogane-cho, Aoba-ku, Yokohama 225-8502, Japan § Misaki Marine Biological Station, Graduate School of Science, The University of Tokyo, 1024 Misaki-Koajiro, Miura, Kanagawa 238-0225, Japan * Department of Urology, St. Marianna University School of Medicine, 2-16-1 Sugao, Miyamae-ku, Kawasaki, Kanagawa 216-8511, Japan Division of Male Infertility, Center for Infertility and IVF, International University of Health and Welfare Hospital, 537-3 Iguchi, Nasushiobara, Tochigi 329-2763, Japan {dagger} Department of Biology, Faculty of Science, Yamagata University, 1-4-12 Kojirakawa-machi, Yamagata 990-8560, Japan

Correspondence and reprint requests: Kaoru Yoshida, PhD. Biomedical Engineering Center, Toin University of Yokohama, 1614 Kurogane-cho, Aoba-ku, Yokohama 225-8502, Japan (e-mail: yoshidak{at}cc.toin.ac.jp)

At ejaculation, human sperm are considered to be mechanically trapped and become immotile in the semen coagulum by binding to semenogelins from the seminal vesicle and zinc ions from the prostate. However, the physiological combined roles of the protein and heavy metal on sperm motility are unknown. Here, we have first demonstrated that semenogelin I alone, which does not form the semen coagulum without zinc, is an inhibitor of the motility of intact human sperm at physiological concentration. On the other hand, zinc ions alone had no effect on sperm motility, but confer recovery of sperm motility that has been inhibited by semenogelin I at a concentration equal to or less than 1 mg/ml. These observations suggest that the roles played by semenogelin I and zinc on sperm motility are not mechanical but physiological. Quartz crystal microbalance analysis suggests that the sperm extract first bind to semenogelin I and then zinc ions which subsequently increase the protein accumulation, suggesting that semenogelins inhibit sperm motility by directly binding to the sperm surface. Further accumulation of semenogelin I mediated by zinc ions may entrap the quiescent sperm at semen ejaculation.

Key Words: semenogelin I/human sperm/motility/zinc

Submitted on July 25, 2007; resubmitted on January 11, 2008; accepted on January 11, 2008.


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