Proacrosin activation in the presence of a 32-kDa protein from boar spermatozoa

Biochemical and Biophysical Research Communications
T BabaY Arai

Abstract

A 32-kDa protein was purified from acrosomal extracts of ejaculated boar spermatozoa as a complex with 55- and 53-kDa proacrosins. In the presence of the 32-kDa protein, these proacrosins were sequentially converted by autoactivation to a 49-kDa intermediate, a 43-kDa intermediate, and then a 35-kDa mature acrosin. This activation process was consistent with that in the absence of the 32-kDa protein, but differed in producing the 49-kDa form as the predominant acrosin intermediate. Thus, the 32-kDa protein may be a regulatory protein for proacrosin activation. The 49-kDa intermediate was a two-chain polypeptide with the amino-terminal sequences corresponding to those of the light and heavy chains of mature acrosin, whereas the carboxyl-terminal sequence of its heavy chain was identical with that of the 53-kDa proacrosin. These results suggest that the 49-kDa intermediate is produced from 53-kDa proacrosin during proacrosin activation by the cleavage of the peptide bond between Arg-23 and Val-24, which results in the formation of the light and heavy chains.

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Citations

Jul 28, 1999·Molecular Reproduction and Development·K Huh, L S Yi
Apr 1, 1992·Journal of Reproductive Immunology·L S Yi, K L Polakoski
Aug 5, 2000·Journal of Reproductive Immunology·T MoriE Mori
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Feb 22, 2013·Biology of Reproduction·Yoshinori KanemoriTadashi Baba
Mar 22, 2013·Biology of Reproduction·James A Foster
Mar 2, 2019·Reproduction in Domestic Animals = Zuchthygiene·Muhammad Aslam M KTirtha K Datta
Aug 31, 2019·Scientific Reports·Michal ZigoPeter Sutovsky
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Apr 30, 1992·Biochemical and Biophysical Research Communications·L S YiK L Polakoski

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