Premium
Matrix degrading properties of sperm serine proteinase, acrosin
Author(s) -
Planchenault T.,
Čechová D.,
Keil-Dlouha V.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)81448-h
Subject(s) - acrosin , serine , sperm , chemistry , biochemistry , andrology , acrosome , enzyme , medicine
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.