精子丝氨酸蛋白酶（顶体蛋白酶）的基质降解特性

Matrix degrading properties of sperm serine proteinase, acrosin.

作者信息

Planchenault T, Cechová D, Keil-Dlouha V

机构信息

Laboratoire de Chimie des Protéines, Institut Pasteur, Paris, France.

出版信息

FEBS Lett. 1991 Dec 9;294(3):279-81. doi: 10.1016/0014-5793(91)81448-h.

DOI:10.1016/0014-5793(91)81448-h

PMID:1661689

Abstract

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.

摘要

丝氨酸蛋白酶顶体蛋白酶在精子穿透透明带过程中起重要作用。在本研究中，我们研究了该酶对各种基质蛋白的影响。顶体蛋白酶能蛋白水解降解纤连蛋白、IV型胶原蛋白和热变性I型胶原蛋白，而天然I型胶原蛋白和层粘连蛋白均未被该酶切割。以IV型胶原蛋白为底物时顶体蛋白酶的比活性（66.6μg/h/mg）比已知的IV型胶原酶或基质溶素高125倍。这些结果表明顶体蛋白酶可能作为一种基质降解蛋白酶发挥作用。