ACTIVATION OF TIMP-2/PROGELATINASE-A COMPLEX BY STROMELYSIN

被引:36
作者
MIYAZAKI, K
UMENISHI, F
FUNAHASHI, K
KOSHIKAWA, N
YASUMITSU, H
UMEDA, M
机构
[1] Division of Cell Biology, Kihara Institute for Biological Research, Yokohama City University, Minami-ku, Yokohama, 232
关键词
D O I
10.1016/0006-291X(92)91705-U
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
Progelatinase A was purified as a complex with TIMP-2 from the conditioned medium of a human glioblastoma cell line. The TIMP-2/progelatinase complex was resistant to the activation by p-aminophenylmercuric acetic acid (APMA), and showed less than 10% of the activity of the TIMP-2-free active enzyme. When the complex was incubated with stromelysin in the presence of APMA, the 64-kDa progelatinase was effectively converted to the 57-kDa mature enzyme, increasing its gelatinolytic activity about 8-fold. These results suggest that stromelysin is a natural activator of TIMP-2-bound progelatinase A. © 1992.
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收藏
页码:852 / 859
页数:8
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