MATRIX DEGRADING PROPERTIES OF SPERM SERINE PROTEINASE, ACROSIN

被引：11
|
作者：
PLANCHENAULT, T
CECHOVA, D
KEILDLOUHA, V
机构：
[1] INST PASTEUR, CHIM PROT LAB, 28 RUE DOCTEUR ROUX, F-75724 PARIS 15, FRANCE
[2] CZECHOSLOVAK ACAD SCI, INST MOLEC GENET, CS-16637 PRAGUE 6, CZECHOSLOVAKIA
来源：
FEBS LETTERS | 1991年 / 294卷 / 03期
关键词：
ACROSIN; MATRIX-DEGRADING ACTIVITY; COLLAGEN-IV; FIBRONECTIN;
D O I：
10.1016/0014-5793(91)81448-H
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
The serine proteinase acrosin plays an important role in sperm penetration of the zona pellucida. In the present study we investigated the effect of the enzyme on various matrix proteins. Acrosin degraded proteolytically fibronectin, type IV collagen and heat denatured type I collagen, whereas neither native type I collagen nor laminin were cleaved by the enzyme. The specific activity of acrosin with type IV collagen as substrate (66.6 g/h/g) was 125-fold higher than that of known type IV collagenase or stromelysin. These results suggest that acrosin may act as a matrix-degrading proteinase.
引用
收藏
页码：279 / 281
页数：3
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