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p-Aminobenzamidine-sensitive acrosomal protease(s) other than acrosin serve the sperm penetration of the egg zona pellucida in mouse

Published online by Cambridge University Press:  01 November 1998


Kazuo Yamagata
Affiliation:
Institute of Applied Biochemistry (IAB) and Tsukuba Advanced Research Alliance (TARA), University of Tsukuba, and the National Institute for Advanced Interdisciplinary Research (NAIR), Tsukuba Science City, Ibaraki, Japan
Keitaro Murayama
Affiliation:
Institute of Applied Biochemistry (IAB) and Tsukuba Advanced Research Alliance (TARA), University of Tsukuba, and the National Institute for Advanced Interdisciplinary Research (NAIR), Tsukuba Science City, Ibaraki, Japan
Nobuhisa Kohno
Affiliation:
Institute of Applied Biochemistry (IAB) and Tsukuba Advanced Research Alliance (TARA), University of Tsukuba, and the National Institute for Advanced Interdisciplinary Research (NAIR), Tsukuba Science City, Ibaraki, Japan
Shin-ichi Kashiwabara
Affiliation:
Institute of Applied Biochemistry (IAB) and Tsukuba Advanced Research Alliance (TARA), University of Tsukuba, and the National Institute for Advanced Interdisciplinary Research (NAIR), Tsukuba Science City, Ibaraki, Japan
Tadashi Baba
Affiliation:
Institute of Applied Biochemistry (IAB) and Tsukuba Advanced Research Alliance (TARA), University of Tsukuba, and the National Institute for Advanced Interdisciplinary Research (NAIR), Tsukuba Science City, Ibaraki, Japan

Abstract

It has been reported that a significant delay in protein dispersal from the acrosomal matrix is observed in wild-type sperm by adding p-aminobenzamidine, a trypsin/acrosin inhibitor, to the incubation medium. The pattern of this delayed release was similar to that of the acrosin-deficient mutant mouse sperm (Yamagata et al., J. Biol. Chem., 273, 10470–4, 1998). In the present study, no further delay in protein dispersal was found when the acrosin-deficient sperm were treated with p-aminobenzamidine, indicating that among the p-aminobenzamidine-sensitive protease(s) only acrosin may function to accelerate this process. Although the acrosin-deficient sperm penetrated the zona pellucida (Baba et al., J. Biol. Chem., 269, 31845–9, 1994), the addition of p-aminobenzamidine to the fertilisation medium caused a significant inhibition of fertilisation in vitro. This indicates that there is a p-aminobenzamidine-sensitive protease(s) other than acrosin participating in the zona penetration step. Indeed, we demonstrated that a non-acrosin protease with a size of 42 kDa was present in the supernatant of the acrosome-reacted sperm suspension. The enzyme was inhibited by p-amimobenzamidine, diisopropyl fluorophosphate and Nα-tosyl-L-lysine chloromethyl ketone, and was apparently activated by acrosin.


Type
Research Article
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Copyright
1998 Cambridge University Press

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