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Molecular Modifications of MC31/CE9, a Sperm Surface Molecule, During Sperm Capacitation and the Acrosome Reaction in the Rat: Is MC31/CE9 Required for Fertilization?¹

Center for Research for Reproduction and Women's Health,³ Department of Gynecology, University of Pennsylvania Medical Center, BRB II/III, Philadelphia, Pennsylvania 19104 Department of Anatomy,⁴ Miyazaki Medical College, Kiyotake, Miyazaki 889-1653, Japan Department of Anatomy and Developmental Biology,⁵ Graduate School of Medicine, Chiba University, 1-8-1 Inohana, Chiba 260-8670, Japan

We examined the modification of the MC31 molecule during capacitation, the acrosome reaction, and studied its role in fertilization. These studies revealed that the molecular mass of MC31 in cauda spermatozoa was approximately 28 000–26 000 Dalton (28–26 kDa). A limited change in molecular mass was seen in capacitated spermatozoa. Treatment of sperm extracts with peptide-N-glycosidase (PN glycosidase) reduced the molecular mass of MC31 in both cauda and capacitated spermatozoa from 28–26 kDa to 23–20 kDa, suggesting that MC31 from both cauda and capacitated spermatozoa is glycosylated, and indicating that capacitation induces minor posttranslational modifications in the structure of the MC31 antigen. The MC31 antigen was redistributed from the midpiece of cauda epididymal spermatozoa to the head and equatorial segment after capacitation and acrosome reaction, respectively, when traced by indirect immunofluorescence under in vitro fertilization (IVF) conditions. Some spermatozoa did not stain for the MC31 antigen and might represent spermatozoa that have shed the antigen. IVF experiments conducted to assess the effect of an anti-MC31 monoclonal antibody (mMC31) revealed that this antibody significantly (P < 0.01) inhibited fertilization of cumulus-invested zona pellucida-intact and the zona pellucida-free oocytes in a dose-dependent manner. However, sperm-oolemma binding was not affected. These findings suggest the MC31 antigen facilitates sperm-oocyte interactions.

¹ This study was supported by grants from JSPS to D.K.S., and the Ministry of Education, Science, Sports, and Culture of Japan grant-in-aid for scientific research to K.T. (12670022 and 14570019).

² Correspondence: K. Toshimori, Department of Anatomy and Developmental Biology (G1), Graduate School of Medicine, Chiba University, 1-8-1 Inohana, Chiba 260-8670, Japan. FAX: +81 43 226 2019; ktoshi{at}faculty.chiba-u.jp

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