Matrix degrading properties of sperm serine proteinase, acrosin.
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.
Planchenault
T
T
Laboratoire de Chimie des Protéines, Institut Pasteur, Paris, France.
Cechová
D
D
Keil-Dlouha
V
V
D000176:Acrosin / Q000037:antagonists & inhibitors / Q000378:metabolism* / Q000494:pharmacology; D000818:Animals; D003094:Collagen / Q000378:metabolism*; D005353:Fibronectins / Q000378:metabolism*; D006358:Hot Temperature; D006801:Humans; D007797:Laminin / Q000378:metabolism; D008297:Male; D019278:Matrix Metalloproteinase 3; D008666:Metalloendopeptidases / Q000378:metabolism; D003012:Microbial Collagenase / Q000378:metabolism; D011489:Protein Denaturation; D051381:Rats; D013094:Spermatozoa / Q000201:enzymology*; D013379:Substrate Specificity
D005353:Fibronectins; D007797:Laminin; D003094:Collagen; D000176:Acrosin; D008666:Metalloendopeptidases; D019278:Matrix Metalloproteinase 3; D003012:Microbial Collagenase