A Mouse Acrosomal Cortical Matrix Protein, MC41, Has ZP2-Binding Activity and Forms a Complex with a 75-kDa Serine Protease

Autor: Tadasuke Oh-oka, Kiyotaka Toshimori, Kazuya Yoshinaga, Ichiro Tanii
Rok vydání: 2001
Předmět:
Zdroj: Developmental Biology. 238:332-341
ISSN: 0012-1606
DOI: 10.1006/dbio.2001.0380
Popis: Sperm with a large acrosome such as that of guinea pigs and hamsters have a subdomain structure in the anterior acrosome, but the mouse acrosome looks homogeneous and its matrix has not been precisely analyzed. The intra-acrosomal protein MC41 is localized in the cortical region of the mouse anterior acrosome, suggesting a subdomain structure in the mouse acrosome. Thus, the present study was undertaken to analyze the mouse acrosomal matrix using an anti-MC41 antibody. When mouse sperm were treated with 2% Triton X-100, Triton-insoluble matrix components remained in the acrosomal cortical region. Immunogold for MC41 labeled the Triton X-100 and high-salt-insoluble matrix components, demonstrating that MC41 is a subdomain-specific acrosomal matrix protein. We further examined interactions of MC41 with acrosomal proteases and zona proteins. A serine protease of 75 kDa was associated with MC41 under low-salt conditions, presumably forming a complex. Far Western blotting technique indicated that MC41 bound to both ZP2 and ZP2 f in the presence of high-salt-soluble sperm proteins. In acrosome-reacting sperm, MC41 was present on the hybrid vesicles formed by the fusion of the plasma and outer acrosomal membranes. Presumably, MC41 has a significant role in secondary sperm–zona binding during the acrosomal reaction.
Databáze: OpenAIRE