METALLOPROTEINASES FROM RABBIT BONE CULTURE-MEDIUM DEGRADE TYPE-IV AND TYPE-V COLLAGENS, LAMININ AND FIBRONECTIN
METALLOPROTEINASES FROM RABBIT BONE CULTURE-MEDIUM DEGRADE TYPE-IV AND TYPE-V COLLAGENS, LAMININ AND FIBRONECTIN
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DOI:
10.1042/bj1990807
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发表时间:
1981-01-01
影响因子:
4.1
通讯作者:
BURGESON, RE
中科院分区:
文献类型:
--
作者:
MURPHY, G;CAWSTON, TE;BURGESON, RE
Gel-filtration chromatography of culture medium from rabbit bone explants separates 3 latent metalloproteinases with activities against collagen, proteoglycan and gelatin, respectively. The fractions degrading proteoglycan also degrade laminin, fibronectin and the polymeric products of pepsin-solubilized type IV collagen and can also solubilize insoluble type IV collagen. The fractions degrading gelatin are capable of degrading solubilized type V and 1.alpha.,2.alpha.,3.alpha. (cartilage) collagens, as well as the lower-MW products of pepsin-solubilized type IV collagen. All activities can be inhibited by 1,10-phenanthroline and occur in either partially or totally latent forms that can be activated by 4-aminophenylmercuric acetate.