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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
1999-4-5
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pubmed:abstractText |
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-aminobenzamidine, diisopropyl fluorophosphate and N alpha-tosyl-L-lysine chloromethyl ketone, and was apparently activated by acrosin.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/4-aminobenzamidine,
http://linkedlifedata.com/resource/pubmed/chemical/Acrosin,
http://linkedlifedata.com/resource/pubmed/chemical/Benzamidines,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Isoflurophate,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Tosyllysine Chloromethyl Ketone
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0967-1994
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
311-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9921641-Acrosin,
pubmed-meshheading:9921641-Acrosome,
pubmed-meshheading:9921641-Animals,
pubmed-meshheading:9921641-Benzamidines,
pubmed-meshheading:9921641-Endopeptidases,
pubmed-meshheading:9921641-Female,
pubmed-meshheading:9921641-Isoflurophate,
pubmed-meshheading:9921641-Male,
pubmed-meshheading:9921641-Mice,
pubmed-meshheading:9921641-Mice, Inbred ICR,
pubmed-meshheading:9921641-Molecular Weight,
pubmed-meshheading:9921641-Protease Inhibitors,
pubmed-meshheading:9921641-Sperm-Ovum Interactions,
pubmed-meshheading:9921641-Tosyllysine Chloromethyl Ketone,
pubmed-meshheading:9921641-Zona Pellucida
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pubmed:year |
1998
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pubmed:articleTitle |
p-Aminobenzamidine-sensitive acrosomal protease(s) other than acrosin serve the sperm penetration of the egg zona pellucida in mouse.
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pubmed:affiliation |
Institute of Applied Biochemistry (IAB), University of Tsukuba, Ibaraki, Japan.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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